TY  - CONF
AU  - Stevanović, Kristina
AU  - Maksimović, Jelena
AU  - Senćanski, Jelena
AU  - Pagnacco, Maja
AU  - Senćanski, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7292
AB  - The organic pigments offer promising opportunities for developing new sustainable electrode materials for lithium batteries. Some of them have been identified as cathode material with very encouraging reversible lithium ion storage characteristics. One of them is a naturally occurring purpurin extracted from the Madder plant (Rubia tinctorum) for which we confirmed this good electrochemical behavior by cyclic voltammetry. One of the strategies towards obtaining materials with even better characteristics is a structural modification of already existing pigments. Building a theoretical model that could predict the redox properties of these new compounds can be very useful towards achieving that goal. In order to build a 3D QSAR (quantitative structure–activity relationship) model for material redox potential prediction, 9 organic pigments with known redox potentials were extracted from the literature. Based on molecular interaction field (MIF) probes we calculated standard GRIND (grid-independent) descriptors and constructed following principal PLS (partial least squares) model. By validation with the literature data, but also with the obtained experimental data for purpurin, this model proved very reliable in predicting the redox potential. A comparison was also made with the machine learning model that was formed in parallel.
PB  - Belgrade : Institute of Technical Sciences of SASA
C3  - 21st Young Researchers' Conference Materials Sciences and Engineering : program and the book of abstracts
T1  - QSAR and machine learning models of redox potentials of some organic pigments
SP  - 35
EP  - 35
UR  - https://hdl.handle.net/21.15107/rcub_cer_7292
ER  - 

@conference{
author = "Stevanović, Kristina and Maksimović, Jelena and Senćanski, Jelena and Pagnacco, Maja and Senćanski, Milan",
year = "2023",
abstract = "The organic pigments offer promising opportunities for developing new sustainable electrode materials for lithium batteries. Some of them have been identified as cathode material with very encouraging reversible lithium ion storage characteristics. One of them is a naturally occurring purpurin extracted from the Madder plant (Rubia tinctorum) for which we confirmed this good electrochemical behavior by cyclic voltammetry. One of the strategies towards obtaining materials with even better characteristics is a structural modification of already existing pigments. Building a theoretical model that could predict the redox properties of these new compounds can be very useful towards achieving that goal. In order to build a 3D QSAR (quantitative structure–activity relationship) model for material redox potential prediction, 9 organic pigments with known redox potentials were extracted from the literature. Based on molecular interaction field (MIF) probes we calculated standard GRIND (grid-independent) descriptors and constructed following principal PLS (partial least squares) model. By validation with the literature data, but also with the obtained experimental data for purpurin, this model proved very reliable in predicting the redox potential. A comparison was also made with the machine learning model that was formed in parallel.",
publisher = "Belgrade : Institute of Technical Sciences of SASA",
journal = "21st Young Researchers' Conference Materials Sciences and Engineering : program and the book of abstracts",
title = "QSAR and machine learning models of redox potentials of some organic pigments",
pages = "35-35",
url = "https://hdl.handle.net/21.15107/rcub_cer_7292"
}

Stevanović, K., Maksimović, J., Senćanski, J., Pagnacco, M.,& Senćanski, M.. (2023). QSAR and machine learning models of redox potentials of some organic pigments. in 21st Young Researchers' Conference Materials Sciences and Engineering : program and the book of abstracts
Belgrade : Institute of Technical Sciences of SASA., 35-35.
https://hdl.handle.net/21.15107/rcub_cer_7292

Stevanović K, Maksimović J, Senćanski J, Pagnacco M, Senćanski M. QSAR and machine learning models of redox potentials of some organic pigments. in 21st Young Researchers' Conference Materials Sciences and Engineering : program and the book of abstracts. 2023;:35-35.
https://hdl.handle.net/21.15107/rcub_cer_7292 .

Stevanović, Kristina, Maksimović, Jelena, Senćanski, Jelena, Pagnacco, Maja, Senćanski, Milan, "QSAR and machine learning models of redox potentials of some organic pigments" in 21st Young Researchers' Conference Materials Sciences and Engineering : program and the book of abstracts (2023):35-35,
https://hdl.handle.net/21.15107/rcub_cer_7292 .

TY  - JOUR
AU  - Đukić, Ivana
AU  - Kaličanin, Nevena
AU  - Senćanski, Milan
AU  - Pajović, Snežana B.
AU  - Milićević, Jelena
AU  - Prljić, Jelena
AU  - Paessler, Slobodan
AU  - Prodanović, Radivoje
AU  - Glišić, Sanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5629
AB  - Drug resistance is a critical problem in health care that affects therapy outcomes and requires new approaches to drug
design. SARS-CoV-2 Mpro mutations are of concern as they can potentially reduce therapeutic efficacy. Viral infections are amongst the
many disorders for which nutraceuticals have been employed as an adjunct therapy. The aim of this study was to examine the potential
in vitro activity of L-arginine and vitamin C against SARS-CoV-2 Mpro. Methods: The Mpro inhibition assay was developed by cloning,
expression, purification, and characterization of Mpro. Selected compounds were then screened for protease inhibition. Results: Larginine
was found to be active against SARS-CoV-2 Mpro, while a vitamin C/L-arginine combination had a synergistic antiviral action
against Mpro. These findings confirm the results of our previous in silico repurposing study that showed L-arginine and vitamin C were
potential Mpro inhibitors. Moreover, they suggest a possible molecular mechanism to explain the beneficial effect of arginine in COVID
patients. Conclusions: The findings of the current study are important because they help to identify COVID-19 treatments that are
efficient, inexpensive, and have a favorable safety profile. The results of this study also suggest a possible adjuvant nutritional strategy
for COVID-19 that could be used in conjunction with pharmacological agents.
PB  - IMR Press
T2  - Frontiers in Bioscience Landmark
T1  - Inhibition of SARS-CoV-2 Mpro with Vitamin C, L-Arginine and a Vitamin C/L-Arginine Combination
VL  - 28
IS  - 1
SP  - 8
DO  - 10.31083/j.fbl2801008
ER  - 

@article{
author = "Đukić, Ivana and Kaličanin, Nevena and Senćanski, Milan and Pajović, Snežana B. and Milićević, Jelena and Prljić, Jelena and Paessler, Slobodan and Prodanović, Radivoje and Glišić, Sanja",
year = "2023",
abstract = "Drug resistance is a critical problem in health care that affects therapy outcomes and requires new approaches to drug
design. SARS-CoV-2 Mpro mutations are of concern as they can potentially reduce therapeutic efficacy. Viral infections are amongst the
many disorders for which nutraceuticals have been employed as an adjunct therapy. The aim of this study was to examine the potential
in vitro activity of L-arginine and vitamin C against SARS-CoV-2 Mpro. Methods: The Mpro inhibition assay was developed by cloning,
expression, purification, and characterization of Mpro. Selected compounds were then screened for protease inhibition. Results: Larginine
was found to be active against SARS-CoV-2 Mpro, while a vitamin C/L-arginine combination had a synergistic antiviral action
against Mpro. These findings confirm the results of our previous in silico repurposing study that showed L-arginine and vitamin C were
potential Mpro inhibitors. Moreover, they suggest a possible molecular mechanism to explain the beneficial effect of arginine in COVID
patients. Conclusions: The findings of the current study are important because they help to identify COVID-19 treatments that are
efficient, inexpensive, and have a favorable safety profile. The results of this study also suggest a possible adjuvant nutritional strategy
for COVID-19 that could be used in conjunction with pharmacological agents.",
publisher = "IMR Press",
journal = "Frontiers in Bioscience Landmark",
title = "Inhibition of SARS-CoV-2 Mpro with Vitamin C, L-Arginine and a Vitamin C/L-Arginine Combination",
volume = "28",
number = "1",
pages = "8",
doi = "10.31083/j.fbl2801008"
}

Đukić, I., Kaličanin, N., Senćanski, M., Pajović, S. B., Milićević, J., Prljić, J., Paessler, S., Prodanović, R.,& Glišić, S.. (2023). Inhibition of SARS-CoV-2 Mpro with Vitamin C, L-Arginine and a Vitamin C/L-Arginine Combination. in Frontiers in Bioscience Landmark
IMR Press., 28(1), 8.
https://doi.org/10.31083/j.fbl2801008

Đukić I, Kaličanin N, Senćanski M, Pajović SB, Milićević J, Prljić J, Paessler S, Prodanović R, Glišić S. Inhibition of SARS-CoV-2 Mpro with Vitamin C, L-Arginine and a Vitamin C/L-Arginine Combination. in Frontiers in Bioscience Landmark. 2023;28(1):8.
doi:10.31083/j.fbl2801008 .

Đukić, Ivana, Kaličanin, Nevena, Senćanski, Milan, Pajović, Snežana B., Milićević, Jelena, Prljić, Jelena, Paessler, Slobodan, Prodanović, Radivoje, Glišić, Sanja, "Inhibition of SARS-CoV-2 Mpro with Vitamin C, L-Arginine and a Vitamin C/L-Arginine Combination" in Frontiers in Bioscience Landmark, 28, no. 1 (2023):8,
https://doi.org/10.31083/j.fbl2801008 . .

TY  - JOUR
AU  - Protić, Sara
AU  - Kaličanin, Nevena
AU  - Senćanski, Milan
AU  - Prodanović, Olivera
AU  - Milićević, Jelena
AU  - Perović, Vladimir
AU  - Paessler, Slobodan
AU  - Prodanović, Radivoje
AU  - Glišić, Sanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5652
AB  - Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent
pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing
can be an effective option for achieving a rapid response. This study used a combined in silico virtual
screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched
first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking.
Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro.
After the expression and purification of PLpro, gramicidin D was screened for protease inhibition
in vitro and was found to be active against PLpro. The current study’s findings are significant
because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable
safety profile.
PB  - Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D
VL  - 24
IS  - 3
SP  - 1955
DO  - 10.3390/ijms24031955
ER  - 

@article{
author = "Protić, Sara and Kaličanin, Nevena and Senćanski, Milan and Prodanović, Olivera and Milićević, Jelena and Perović, Vladimir and Paessler, Slobodan and Prodanović, Radivoje and Glišić, Sanja",
year = "2023",
abstract = "Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent
pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing
can be an effective option for achieving a rapid response. This study used a combined in silico virtual
screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched
first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking.
Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro.
After the expression and purification of PLpro, gramicidin D was screened for protease inhibition
in vitro and was found to be active against PLpro. The current study’s findings are significant
because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable
safety profile.",
publisher = "Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D",
volume = "24",
number = "3",
pages = "1955",
doi = "10.3390/ijms24031955"
}

Protić, S., Kaličanin, N., Senćanski, M., Prodanović, O., Milićević, J., Perović, V., Paessler, S., Prodanović, R.,& Glišić, S.. (2023). In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in International Journal of Molecular Sciences
Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)., 24(3), 1955.
https://doi.org/10.3390/ijms24031955

Protić S, Kaličanin N, Senćanski M, Prodanović O, Milićević J, Perović V, Paessler S, Prodanović R, Glišić S. In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in International Journal of Molecular Sciences. 2023;24(3):1955.
doi:10.3390/ijms24031955 .

Protić, Sara, Kaličanin, Nevena, Senćanski, Milan, Prodanović, Olivera, Milićević, Jelena, Perović, Vladimir, Paessler, Slobodan, Prodanović, Radivoje, Glišić, Sanja, "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D" in International Journal of Molecular Sciences, 24, no. 3 (2023):1955,
https://doi.org/10.3390/ijms24031955 . .

Stanišić, M., Ristić, P., Balaž, A. M., Senćanski, M., Mitić, D., Prodanović, R.,& Todorović, T.. (2022). Efficient enzyme@MOF composites for biocatalysis. in Book of abstracts - EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland, 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5751

Stanišić M, Ristić P, Balaž AM, Senćanski M, Mitić D, Prodanović R, Todorović T. Efficient enzyme@MOF composites for biocatalysis. in Book of abstracts - EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5751 .

Stanišić, Marija, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Mitić, Dragana, Prodanović, Radivoje, Todorović, Tamara, "Efficient enzyme@MOF composites for biocatalysis" in Book of abstracts - EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5751 .

TY  - JOUR
AU  - Stanišić, Marija D.
AU  - Popović Kokar, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Ognanović, Miloš
AU  - Đokić, Veljko R.
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4895
AB  - Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a protective coating to en-capsulate proteins via biomimetic mineralization. The formation of nucleation centers and further biocomposite crystal growth is entirely governed by the pure electrostatic interactions between the protein’s surface and the positively charged Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification of surface amino acid residues can lead to a rapid biocomposite crystal formation. However, a chemical modification of carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule, from −10.2 to −36.9 mV, as shown by zeta potential measurements and native PAGE electrophoresis. Biomineralization experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of the ZIF-8 biocomposites. Periodate oxidation of carbohydrate components for glycoproteins can serve as a facile and general method for facilitating the biomimetic mineralization of other industrially relevant glycoproteins.
PB  - MDPI
T2  - Polymers
T1  - Chemical modification of glycoproteins’ carbohydrate moiety as a general strategy for the synthesis of efficient biocatalysts by biomimetic mineralization: The case of glucose oxidase
VL  - 13
IS  - 22
SP  - 2
EP  - 12
DO  - 10.3390/polym13223875
ER  - 

@article{
author = "Stanišić, Marija D. and Popović Kokar, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Ognanović, Miloš and Đokić, Veljko R. and Prodanović, Radivoje and Todorović, Tamara",
year = "2021",
abstract = "Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a protective coating to en-capsulate proteins via biomimetic mineralization. The formation of nucleation centers and further biocomposite crystal growth is entirely governed by the pure electrostatic interactions between the protein’s surface and the positively charged Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification of surface amino acid residues can lead to a rapid biocomposite crystal formation. However, a chemical modification of carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule, from −10.2 to −36.9 mV, as shown by zeta potential measurements and native PAGE electrophoresis. Biomineralization experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of the ZIF-8 biocomposites. Periodate oxidation of carbohydrate components for glycoproteins can serve as a facile and general method for facilitating the biomimetic mineralization of other industrially relevant glycoproteins.",
publisher = "MDPI",
journal = "Polymers",
title = "Chemical modification of glycoproteins’ carbohydrate moiety as a general strategy for the synthesis of efficient biocatalysts by biomimetic mineralization: The case of glucose oxidase",
volume = "13",
number = "22",
pages = "2-12",
doi = "10.3390/polym13223875"
}

Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical modification of glycoproteins’ carbohydrate moiety as a general strategy for the synthesis of efficient biocatalysts by biomimetic mineralization: The case of glucose oxidase. in Polymers
MDPI., 13(22), 2-12.
https://doi.org/10.3390/polym13223875

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Senćanski M, Ognanović M, Đokić VR, Prodanović R, Todorović T. Chemical modification of glycoproteins’ carbohydrate moiety as a general strategy for the synthesis of efficient biocatalysts by biomimetic mineralization: The case of glucose oxidase. in Polymers. 2021;13(22):2-12.
doi:10.3390/polym13223875 .

Stanišić, Marija D., Popović Kokar, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Ognanović, Miloš, Đokić, Veljko R., Prodanović, Radivoje, Todorović, Tamara, "Chemical modification of glycoproteins’ carbohydrate moiety as a general strategy for the synthesis of efficient biocatalysts by biomimetic mineralization: The case of glucose oxidase" in Polymers, 13, no. 22 (2021):2-12,
https://doi.org/10.3390/polym13223875 . .

TY  - CONF
AU  - Stanišić, Marija
AU  - Popović, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5564
AB  - Glucose oxidase (GOx) is an enzyme that belongs to a group of oxidoreductases. This enzyme catalyzes the oxidation of glucose to gluconic acid using molecular oxygen as an electron acceptor. Glucose oxidase contains carbohydrates in its structure, most often mannose and glucose (11-13%) 1. Durability of GOx in harsh conditions can be enhanced by encapsulation within metal–organic frameworks via a process called biomimetic mineralisation. We demonstrate that chemical modification of carbohydrate parts on the protein surface by periodate oxidation is an effective method for control of biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8). Obtained GOx-ZIF-8 biocomposite had the higher half-life at 65oC, and higher specific activity than native GOx.
PB  - Beograd : Biohemijsko društvo Srbije
C3  - Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts
T1  - Biomimetic mineralisation of periodate oxidized glucose oxidase
SP  - 148
EP  - 148
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5748
ER  - 

@conference{
author = "Stanišić, Marija and Popović, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Prodanović, Radivoje and Todorović, Tamara",
year = "2021",
abstract = "Glucose oxidase (GOx) is an enzyme that belongs to a group of oxidoreductases. This enzyme catalyzes the oxidation of glucose to gluconic acid using molecular oxygen as an electron acceptor. Glucose oxidase contains carbohydrates in its structure, most often mannose and glucose (11-13%) 1. Durability of GOx in harsh conditions can be enhanced by encapsulation within metal–organic frameworks via a process called biomimetic mineralisation. We demonstrate that chemical modification of carbohydrate parts on the protein surface by periodate oxidation is an effective method for control of biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8). Obtained GOx-ZIF-8 biocomposite had the higher half-life at 65oC, and higher specific activity than native GOx.",
publisher = "Beograd : Biohemijsko društvo Srbije",
journal = "Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts",
title = "Biomimetic mineralisation of periodate oxidized glucose oxidase",
pages = "148-148",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5748"
}

Stanišić, M., Popović, N., Ristić, P., Balaž, A. M., Senćanski, M., Prodanović, R.,& Todorović, T.. (2021). Biomimetic mineralisation of periodate oxidized glucose oxidase. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts
Beograd : Biohemijsko društvo Srbije., 148-148.
https://hdl.handle.net/21.15107/rcub_cherry_5748

Stanišić M, Popović N, Ristić P, Balaž AM, Senćanski M, Prodanović R, Todorović T. Biomimetic mineralisation of periodate oxidized glucose oxidase. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts. 2021;:148-148.
https://hdl.handle.net/21.15107/rcub_cherry_5748 .

Stanišić, Marija, Popović, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Prodanović, Radivoje, Todorović, Tamara, "Biomimetic mineralisation of periodate oxidized glucose oxidase" in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts (2021):148-148,
https://hdl.handle.net/21.15107/rcub_cherry_5748 .

TY  - CONF
AU  - Balaž, Ana Marija
AU  - Crnoglavac Popović, Milica
AU  - Stanišić, Marija
AU  - Ristić, Predrag
AU  - Senćanski, Milan
AU  - Todorović, Tamara
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5566
AB  - Enzyme immobilization enables maintenance of enzyme activity and structural stability even in adverse conditions 1. Structural changes in enzymes that can occur due to the action of organic solvents, inhibitors or increased temperature can be prevented by immobilization of the enzymes in metal–organic frameworks (MOFs). It is reported that several enzymes, such as cytochrome c and horseradish peroxidase (HRP) have been successfully incorporated into MOFs 2. The aim of this work is to produce wild type horseradish peroxidase, isoform C1A, and several mutants specially designed to increase the activity and stability of HRP while immobilized within selected MOFs. Wild type and its variants were produced in metalotrophic yeast, Pichia pastoris KM71H strain, their activity and basic kinetic parameters were determined and compared prior imobilization.
C3  - Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac
T1  - Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain
SP  - 49
EP  - 49
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5747
ER  - 

@conference{
author = "Balaž, Ana Marija and Crnoglavac Popović, Milica and Stanišić, Marija and Ristić, Predrag and Senćanski, Milan and Todorović, Tamara and Prodanović, Radivoje",
year = "2021",
abstract = "Enzyme immobilization enables maintenance of enzyme activity and structural stability even in adverse conditions 1. Structural changes in enzymes that can occur due to the action of organic solvents, inhibitors or increased temperature can be prevented by immobilization of the enzymes in metal–organic frameworks (MOFs). It is reported that several enzymes, such as cytochrome c and horseradish peroxidase (HRP) have been successfully incorporated into MOFs 2. The aim of this work is to produce wild type horseradish peroxidase, isoform C1A, and several mutants specially designed to increase the activity and stability of HRP while immobilized within selected MOFs. Wild type and its variants were produced in metalotrophic yeast, Pichia pastoris KM71H strain, their activity and basic kinetic parameters were determined and compared prior imobilization.",
journal = "Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac",
title = "Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain",
pages = "49-49",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5747"
}

Balaž, A. M., Crnoglavac Popović, M., Stanišić, M., Ristić, P., Senćanski, M., Todorović, T.,& Prodanović, R.. (2021). Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, 49-49.
https://hdl.handle.net/21.15107/rcub_cherry_5747

Balaž AM, Crnoglavac Popović M, Stanišić M, Ristić P, Senćanski M, Todorović T, Prodanović R. Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac. 2021;:49-49.
https://hdl.handle.net/21.15107/rcub_cherry_5747 .

Balaž, Ana Marija, Crnoglavac Popović, Milica, Stanišić, Marija, Ristić, Predrag, Senćanski, Milan, Todorović, Tamara, Prodanović, Radivoje, "Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain" in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac (2021):49-49,
https://hdl.handle.net/21.15107/rcub_cherry_5747 .

TY  - JOUR
AU  - Bondžić, Aleksandra
AU  - Senćanski, Milan
AU  - Vujačić Nikezić, Ana V.
AU  - Kirillova, Marina V.
AU  - André, Vânia
AU  - Kirillov, Alexander M.
AU  - Bondžić, Bojan
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3958
AB  - Three coordination compounds featuring different types of tetracopper(II) cores, namely
[O⊂Cu4{N(CH2CH2O)3}4(BOH)4][BF4]2 (1), [Cu4(μ4-H2edte)(μ5-H2edte)(sal)2]n·7nH2O, (H4edte=N,N,N′,
N′-tetrakis(2-hydroxyethyl)ethylenediamine, H2sal=salicylic acid) (2), and [{Cu4(μ3-Hbes)4(μ-hba)}K
(H2O)3]n, H3bes=N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (3), were assayed for their potency to
inhibit the acetyl (AChE) and butyrylcholinesterase (BuChE) enzymes aiming to test these compounds as potential
dual inhibitors in the treatment of Alzheimer's disease. All the investigated compounds showed a strong
inhibitory potency toward both enzymes with IC50 values in micromolar range of concentration; compound 1
displayed the most potent inhibitory behaviour toward both enzymes. The mechanism of the AChE and BuChE
inhibition was examined by enzyme kinetic measurements. The obtained kinetic parameters, Vmax and Km indicated
an uncompetitive type of inhibition of both enzymes by compound 1. For the other two compounds a
non-competitive inhibition mode was observed. To get further insight into the mechanism of action and to
elucidate binding modes in details we examined the interactions of 1–3 with acetylcholinesterase, using molecular
docking approach. Grid based docking studies indicated that these compounds can bind to peripheral
anionic site (PAS) of the AChE with Ki values in micromolar range. Moreover, blind docking revealed the
capability of investigated compounds to bind to new allosteric site (i.e. binding site II) distinct from PAS.
Showing that these Cu-based compounds can act as new allosteric inhibitors of AChE and identifying novel
allosteric binding site on AChE represents a significant contribution toward the design of novel and more
effective inhibitors of AChE.
PB  - Elsevier
T2  - Journal of Inorganic Biochemistry
T1  - Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action
VL  - 205
SP  - 110990
DO  - 10.1016/j.jinorgbio.2019.110990
ER  - 

@article{
author = "Bondžić, Aleksandra and Senćanski, Milan and Vujačić Nikezić, Ana V. and Kirillova, Marina V. and André, Vânia and Kirillov, Alexander M. and Bondžić, Bojan",
year = "2020",
abstract = "Three coordination compounds featuring different types of tetracopper(II) cores, namely
[O⊂Cu4{N(CH2CH2O)3}4(BOH)4][BF4]2 (1), [Cu4(μ4-H2edte)(μ5-H2edte)(sal)2]n·7nH2O, (H4edte=N,N,N′,
N′-tetrakis(2-hydroxyethyl)ethylenediamine, H2sal=salicylic acid) (2), and [{Cu4(μ3-Hbes)4(μ-hba)}K
(H2O)3]n, H3bes=N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (3), were assayed for their potency to
inhibit the acetyl (AChE) and butyrylcholinesterase (BuChE) enzymes aiming to test these compounds as potential
dual inhibitors in the treatment of Alzheimer's disease. All the investigated compounds showed a strong
inhibitory potency toward both enzymes with IC50 values in micromolar range of concentration; compound 1
displayed the most potent inhibitory behaviour toward both enzymes. The mechanism of the AChE and BuChE
inhibition was examined by enzyme kinetic measurements. The obtained kinetic parameters, Vmax and Km indicated
an uncompetitive type of inhibition of both enzymes by compound 1. For the other two compounds a
non-competitive inhibition mode was observed. To get further insight into the mechanism of action and to
elucidate binding modes in details we examined the interactions of 1–3 with acetylcholinesterase, using molecular
docking approach. Grid based docking studies indicated that these compounds can bind to peripheral
anionic site (PAS) of the AChE with Ki values in micromolar range. Moreover, blind docking revealed the
capability of investigated compounds to bind to new allosteric site (i.e. binding site II) distinct from PAS.
Showing that these Cu-based compounds can act as new allosteric inhibitors of AChE and identifying novel
allosteric binding site on AChE represents a significant contribution toward the design of novel and more
effective inhibitors of AChE.",
publisher = "Elsevier",
journal = "Journal of Inorganic Biochemistry",
title = "Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action",
volume = "205",
pages = "110990",
doi = "10.1016/j.jinorgbio.2019.110990"
}

Bondžić, A., Senćanski, M., Vujačić Nikezić, A. V., Kirillova, M. V., André, V., Kirillov, A. M.,& Bondžić, B.. (2020). Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action. in Journal of Inorganic Biochemistry
Elsevier., 205, 110990.
https://doi.org/10.1016/j.jinorgbio.2019.110990

Bondžić A, Senćanski M, Vujačić Nikezić AV, Kirillova MV, André V, Kirillov AM, Bondžić B. Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action. in Journal of Inorganic Biochemistry. 2020;205:110990.
doi:10.1016/j.jinorgbio.2019.110990 .

Bondžić, Aleksandra, Senćanski, Milan, Vujačić Nikezić, Ana V., Kirillova, Marina V., André, Vânia, Kirillov, Alexander M., Bondžić, Bojan, "Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action" in Journal of Inorganic Biochemistry, 205 (2020):110990,
https://doi.org/10.1016/j.jinorgbio.2019.110990 . .

TY  - JOUR
AU  - Senćanski, Milan
AU  - Đorđević, Ivana
AU  - Grubišić, Sonja
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2265
AB  - Selenium has been increasingly recognized as an important element in biological systems, which participates in numerous biochemical processes in organisms, notably in enzyme reactions. Selenium can substitute sulfur of cysteine and methionine to form their selenium analogues, selenocysteine (Sec) and selenomethionine (SeM). The nature of amino acid pockets in proteins is dependent on their composition and thus different non-covalent forces determine the interactions between selenium of Sec or SeM and other functional groups, resulting in specific biophysical behavior. The discrimination of selenium toward sulfur has been reported. In order to elucidate the difference between the nature of S-pi and Se-pi interactions, we performed extensive DFT calculations of dispersive and electrostatic contributions of Se-pi interactions in substituted benzenes/hydrogen selenide (H2Se) complexes. The results are compared with our earlier reported S-pi calculations, as well as with available experimental data. Our results show a larger contribution of dispersive interactions in Se-pi systems than in S-pi ones, which mainly originate from the attraction between Se and substituent groups. We found that selenium exhibits a strong interaction with aromatic systems and may thus play a significant role in stabilizing protein folds and protein-inhibitor complexes. Our findings can also provide molecular insights for understanding enzymatic specificity discrimination between single selenium versus a sulfur atom, notwithstanding their very similar chemical properties.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT
VL  - 23
IS  - 5
DO  - 10.1007/s00894-017-3330-z
ER  - 

@article{
author = "Senćanski, Milan and Đorđević, Ivana and Grubišić, Sonja",
year = "2017",
abstract = "Selenium has been increasingly recognized as an important element in biological systems, which participates in numerous biochemical processes in organisms, notably in enzyme reactions. Selenium can substitute sulfur of cysteine and methionine to form their selenium analogues, selenocysteine (Sec) and selenomethionine (SeM). The nature of amino acid pockets in proteins is dependent on their composition and thus different non-covalent forces determine the interactions between selenium of Sec or SeM and other functional groups, resulting in specific biophysical behavior. The discrimination of selenium toward sulfur has been reported. In order to elucidate the difference between the nature of S-pi and Se-pi interactions, we performed extensive DFT calculations of dispersive and electrostatic contributions of Se-pi interactions in substituted benzenes/hydrogen selenide (H2Se) complexes. The results are compared with our earlier reported S-pi calculations, as well as with available experimental data. Our results show a larger contribution of dispersive interactions in Se-pi systems than in S-pi ones, which mainly originate from the attraction between Se and substituent groups. We found that selenium exhibits a strong interaction with aromatic systems and may thus play a significant role in stabilizing protein folds and protein-inhibitor complexes. Our findings can also provide molecular insights for understanding enzymatic specificity discrimination between single selenium versus a sulfur atom, notwithstanding their very similar chemical properties.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT",
volume = "23",
number = "5",
doi = "10.1007/s00894-017-3330-z"
}

Senćanski, M., Đorđević, I.,& Grubišić, S.. (2017). Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT. in Journal of Molecular Modeling
Springer, New York., 23(5).
https://doi.org/10.1007/s00894-017-3330-z

Senćanski M, Đorđević I, Grubišić S. Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT. in Journal of Molecular Modeling. 2017;23(5).
doi:10.1007/s00894-017-3330-z .

Senćanski, Milan, Đorđević, Ivana, Grubišić, Sonja, "Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT" in Journal of Molecular Modeling, 23, no. 5 (2017),
https://doi.org/10.1007/s00894-017-3330-z . .

TY  - JOUR
AU  - Filipovic, Nenad R.
AU  - Bjelogrlić, Snežana K.
AU  - Todorović, Tamara
AU  - Blagojević, Vladimir A.
AU  - Muller, Christian D.
AU  - Marinković, Aleksandar D.
AU  - Vujčić, Miroslava
AU  - Janović, Barbara
AU  - Malešević, Aleksandar S.
AU  - Begovic, Nebojsa
AU  - Senćanski, Milan
AU  - Minić, Dragica M.
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2010
AB  - A new Ni(II) complex, [Ni(L)(H2O)] (1), with diethyl 3,3'-(2,2'-(1,1'-(pyridine-2,6-diyl) bis(ethan-1-yl-1-ylidene)) bis(hydrazin-1-yl-2-ylidene)) bis(3-oxopropanoate) ligand (H2L) was synthesized as a potential chemotherapeutic agent. Polidentate ligand was coordinated to Ni(II) NNN-tridentately, in dianionic form, while monodentate water coordination completed square-planar geometry around metal. Structure in the solution was determined by NMR spectroscopy and the same coordination mode was observed in the solid state using IR spectroscopy and further verified by DFT calculations and electrochemical studies. Thermal stability of 1 was determined in both air and nitrogen atmosphere. Anticancer activity of 1 was investigated on acute monocytic leukemia (THP-1) and pancreatic adenocarcinoma (AsPC-1) cell lines. On THP-1 cells 1 induced powerful apoptotic response (ED50 = 10 +/- 3 mu M), which was revealed to be only partially caspase-dependent, with activation of caspase-8 as the dominant course. This suggested that experimentally validated covalent binding of 1 to DNA is not the only mechanism responsible for programmed cell death. This was supported with experiments on AsPC-1 cells. Although treatment of those cells with 1 resulted in poor apoptotic response, cell cycle changes showed concentration-dependent shifts indicating a dual mechanism of activity. This study also reviews the results of preliminary biological screening, which demonstrates that 1 displays a unique pattern of anticancer activity with at least two mechanisms involved.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Ni(II) complex with bishydrazone ligand: synthesis, characterization, DNA binding studies and pro-apoptotic and pro-differentiation induction in human cancerous cell lines
VL  - 6
IS  - 110
SP  - 108726
EP  - 108740
DO  - 10.1039/c6ra24604d
ER  - 

@article{
author = "Filipovic, Nenad R. and Bjelogrlić, Snežana K. and Todorović, Tamara and Blagojević, Vladimir A. and Muller, Christian D. and Marinković, Aleksandar D. and Vujčić, Miroslava and Janović, Barbara and Malešević, Aleksandar S. and Begovic, Nebojsa and Senćanski, Milan and Minić, Dragica M.",
year = "2016",
abstract = "A new Ni(II) complex, [Ni(L)(H2O)] (1), with diethyl 3,3'-(2,2'-(1,1'-(pyridine-2,6-diyl) bis(ethan-1-yl-1-ylidene)) bis(hydrazin-1-yl-2-ylidene)) bis(3-oxopropanoate) ligand (H2L) was synthesized as a potential chemotherapeutic agent. Polidentate ligand was coordinated to Ni(II) NNN-tridentately, in dianionic form, while monodentate water coordination completed square-planar geometry around metal. Structure in the solution was determined by NMR spectroscopy and the same coordination mode was observed in the solid state using IR spectroscopy and further verified by DFT calculations and electrochemical studies. Thermal stability of 1 was determined in both air and nitrogen atmosphere. Anticancer activity of 1 was investigated on acute monocytic leukemia (THP-1) and pancreatic adenocarcinoma (AsPC-1) cell lines. On THP-1 cells 1 induced powerful apoptotic response (ED50 = 10 +/- 3 mu M), which was revealed to be only partially caspase-dependent, with activation of caspase-8 as the dominant course. This suggested that experimentally validated covalent binding of 1 to DNA is not the only mechanism responsible for programmed cell death. This was supported with experiments on AsPC-1 cells. Although treatment of those cells with 1 resulted in poor apoptotic response, cell cycle changes showed concentration-dependent shifts indicating a dual mechanism of activity. This study also reviews the results of preliminary biological screening, which demonstrates that 1 displays a unique pattern of anticancer activity with at least two mechanisms involved.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Ni(II) complex with bishydrazone ligand: synthesis, characterization, DNA binding studies and pro-apoptotic and pro-differentiation induction in human cancerous cell lines",
volume = "6",
number = "110",
pages = "108726-108740",
doi = "10.1039/c6ra24604d"
}

Filipovic, N. R., Bjelogrlić, S. K., Todorović, T., Blagojević, V. A., Muller, C. D., Marinković, A. D., Vujčić, M., Janović, B., Malešević, A. S., Begovic, N., Senćanski, M.,& Minić, D. M.. (2016). Ni(II) complex with bishydrazone ligand: synthesis, characterization, DNA binding studies and pro-apoptotic and pro-differentiation induction in human cancerous cell lines. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(110), 108726-108740.
https://doi.org/10.1039/c6ra24604d

Filipovic NR, Bjelogrlić SK, Todorović T, Blagojević VA, Muller CD, Marinković AD, Vujčić M, Janović B, Malešević AS, Begovic N, Senćanski M, Minić DM. Ni(II) complex with bishydrazone ligand: synthesis, characterization, DNA binding studies and pro-apoptotic and pro-differentiation induction in human cancerous cell lines. in RSC Advances. 2016;6(110):108726-108740.
doi:10.1039/c6ra24604d .

Filipovic, Nenad R., Bjelogrlić, Snežana K., Todorović, Tamara, Blagojević, Vladimir A., Muller, Christian D., Marinković, Aleksandar D., Vujčić, Miroslava, Janović, Barbara, Malešević, Aleksandar S., Begovic, Nebojsa, Senćanski, Milan, Minić, Dragica M., "Ni(II) complex with bishydrazone ligand: synthesis, characterization, DNA binding studies and pro-apoptotic and pro-differentiation induction in human cancerous cell lines" in RSC Advances, 6, no. 110 (2016):108726-108740,
https://doi.org/10.1039/c6ra24604d . .

TY  - JOUR
AU  - Senćanski, Milan
AU  - Došen-Mićović, Ljiljana
AU  - Šukalović, Vladimir
AU  - Kostić Rajačić, Slađana
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1617
AB  - Contacts between aromatic rings and sulfur-containing amino acids are frequent in proteins. However, little is known about the nature of their interactions particularly if substituents are present on aromatic ring. In this paper, DFT quantum chemical calculations were used to study substituted benzenes in complex with hydrogen sulfide (H2S), methanethiol (CH3SH), and (Methylsulfanyl)methane (CH3SCH3). It was found that SH(...)a interaction is more stabilizing than the S(...)a interaction in the case of benzene, but this is changed with increasing electronegativity of the substituent on benzene ring. Although the change of energy of SH...pi and S-...pi interaction follows the conventional model of substituent effect, where S-...pi interactions are maximized and SH...pi interactions are diminished with electron-withdrawing substituent on benzene as a result of changes in the aryl it-system, it was found that it is mainly a consequence of direct electrostatic interaction between substituent and the sulfur-containing molecule. We also investigated the model system of Cys(...)Trp interaction, adjacent to a cluster of aromatic amino acids, in proteins, using explicit membrane molecular dynamics simulations results of D-3 dopamine receptor crystal structure as starting point. It was found that fluorination in aromatic cluster enhances the Cys(...)Trp interaction. The effect is maximized when transferred through the rest of aromatic system suggesting possible explanation for frequent contacts between sulfur-containing and aromatic amino acids in proteins and their effects on protein folding and stabilization.
PB  - Springer/Plenum Publishers, New York
T2  - Structural Chemistry
T1  - Theoretical insight into sulfur aromatic interactions with extension to D-2 receptor activation mechanism
VL  - 26
IS  - 4
SP  - 1139
EP  - 1149
DO  - 10.1007/s11224-015-0574-z
ER  - 

@article{
author = "Senćanski, Milan and Došen-Mićović, Ljiljana and Šukalović, Vladimir and Kostić Rajačić, Slađana",
year = "2015",
abstract = "Contacts between aromatic rings and sulfur-containing amino acids are frequent in proteins. However, little is known about the nature of their interactions particularly if substituents are present on aromatic ring. In this paper, DFT quantum chemical calculations were used to study substituted benzenes in complex with hydrogen sulfide (H2S), methanethiol (CH3SH), and (Methylsulfanyl)methane (CH3SCH3). It was found that SH(...)a interaction is more stabilizing than the S(...)a interaction in the case of benzene, but this is changed with increasing electronegativity of the substituent on benzene ring. Although the change of energy of SH...pi and S-...pi interaction follows the conventional model of substituent effect, where S-...pi interactions are maximized and SH...pi interactions are diminished with electron-withdrawing substituent on benzene as a result of changes in the aryl it-system, it was found that it is mainly a consequence of direct electrostatic interaction between substituent and the sulfur-containing molecule. We also investigated the model system of Cys(...)Trp interaction, adjacent to a cluster of aromatic amino acids, in proteins, using explicit membrane molecular dynamics simulations results of D-3 dopamine receptor crystal structure as starting point. It was found that fluorination in aromatic cluster enhances the Cys(...)Trp interaction. The effect is maximized when transferred through the rest of aromatic system suggesting possible explanation for frequent contacts between sulfur-containing and aromatic amino acids in proteins and their effects on protein folding and stabilization.",
publisher = "Springer/Plenum Publishers, New York",
journal = "Structural Chemistry",
title = "Theoretical insight into sulfur aromatic interactions with extension to D-2 receptor activation mechanism",
volume = "26",
number = "4",
pages = "1139-1149",
doi = "10.1007/s11224-015-0574-z"
}

Senćanski, M., Došen-Mićović, L., Šukalović, V.,& Kostić Rajačić, S.. (2015). Theoretical insight into sulfur aromatic interactions with extension to D-2 receptor activation mechanism. in Structural Chemistry
Springer/Plenum Publishers, New York., 26(4), 1139-1149.
https://doi.org/10.1007/s11224-015-0574-z

Senćanski M, Došen-Mićović L, Šukalović V, Kostić Rajačić S. Theoretical insight into sulfur aromatic interactions with extension to D-2 receptor activation mechanism. in Structural Chemistry. 2015;26(4):1139-1149.
doi:10.1007/s11224-015-0574-z .

Senćanski, Milan, Došen-Mićović, Ljiljana, Šukalović, Vladimir, Kostić Rajačić, Slađana, "Theoretical insight into sulfur aromatic interactions with extension to D-2 receptor activation mechanism" in Structural Chemistry, 26, no. 4 (2015):1139-1149,
https://doi.org/10.1007/s11224-015-0574-z . .

TY  - JOUR
AU  - Filipovic, Nenad R.
AU  - Bjelogrlić, Snežana K.
AU  - Marinković, Aleksandar D.
AU  - Verbić, Tatjana
AU  - Cvijetić, Ilija
AU  - Senćanski, Milan
AU  - Rodić, Marko V.
AU  - Vujčić, Miroslava
AU  - Sladić, Dušan
AU  - Strikovic, Zlatko
AU  - Todorović, Tamara
AU  - Muller, Christian D.
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1830
AB  - A new Zn(II)-based potential chemotherapeutic agent was synthesized from the ligand 2-quinolinecarboxaldehyde selenosemicarbazone (Hqasesc). Single crystal X-ray diffraction analysis showed that the Zn(II) complex consists of a cation [Zn(Hqasesc)(2)](2+), two perchlorate anions and one ethanol solvent molecule. The interaction of calf thymus (CT) DNA and human serum albumin (HSA) with the Zn(II) complex was explored using absorption and emission spectral methods, and also has been supported by molecular docking studies. The complex has more affinity to minor DNA groove than major, with no significant intercalation. The HSA interaction studies of the complex revealed the quenching of the intrinsic fluorescence of the HSA through a static quenching mechanism. The antitumor activity of the ligand and the complex against pancreatic adenocarcinoma cell line (AsPC-1) and acute monocytic leukemia (THP-1) cells was evaluated. Both compounds are strong concentration-dependent apoptosis inducers in THP-1 cells. While Hqasesc in AsPC-1 cells induces apoptosis only at the highest concentration, treatment with the Zn complex shows a concentration-dependent apoptotic response, where the treated cells are arrested in the G1-to-S phase accompanied with extensive activation of caspase-8 and -9. These results indicate that the ligand and Zn(II) complex display cell phenotype specific activity.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction
VL  - 5
IS  - 115
SP  - 95191
EP  - 95211
DO  - 10.1039/c5ra19849f
ER  - 

@article{
author = "Filipovic, Nenad R. and Bjelogrlić, Snežana K. and Marinković, Aleksandar D. and Verbić, Tatjana and Cvijetić, Ilija and Senćanski, Milan and Rodić, Marko V. and Vujčić, Miroslava and Sladić, Dušan and Strikovic, Zlatko and Todorović, Tamara and Muller, Christian D.",
year = "2015",
abstract = "A new Zn(II)-based potential chemotherapeutic agent was synthesized from the ligand 2-quinolinecarboxaldehyde selenosemicarbazone (Hqasesc). Single crystal X-ray diffraction analysis showed that the Zn(II) complex consists of a cation [Zn(Hqasesc)(2)](2+), two perchlorate anions and one ethanol solvent molecule. The interaction of calf thymus (CT) DNA and human serum albumin (HSA) with the Zn(II) complex was explored using absorption and emission spectral methods, and also has been supported by molecular docking studies. The complex has more affinity to minor DNA groove than major, with no significant intercalation. The HSA interaction studies of the complex revealed the quenching of the intrinsic fluorescence of the HSA through a static quenching mechanism. The antitumor activity of the ligand and the complex against pancreatic adenocarcinoma cell line (AsPC-1) and acute monocytic leukemia (THP-1) cells was evaluated. Both compounds are strong concentration-dependent apoptosis inducers in THP-1 cells. While Hqasesc in AsPC-1 cells induces apoptosis only at the highest concentration, treatment with the Zn complex shows a concentration-dependent apoptotic response, where the treated cells are arrested in the G1-to-S phase accompanied with extensive activation of caspase-8 and -9. These results indicate that the ligand and Zn(II) complex display cell phenotype specific activity.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction",
volume = "5",
number = "115",
pages = "95191-95211",
doi = "10.1039/c5ra19849f"
}

Filipovic, N. R., Bjelogrlić, S. K., Marinković, A. D., Verbić, T., Cvijetić, I., Senćanski, M., Rodić, M. V., Vujčić, M., Sladić, D., Strikovic, Z., Todorović, T.,& Muller, C. D.. (2015). Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(115), 95191-95211.
https://doi.org/10.1039/c5ra19849f

Filipovic NR, Bjelogrlić SK, Marinković AD, Verbić T, Cvijetić I, Senćanski M, Rodić MV, Vujčić M, Sladić D, Strikovic Z, Todorović T, Muller CD. Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction. in RSC Advances. 2015;5(115):95191-95211.
doi:10.1039/c5ra19849f .

Filipovic, Nenad R., Bjelogrlić, Snežana K., Marinković, Aleksandar D., Verbić, Tatjana, Cvijetić, Ilija, Senćanski, Milan, Rodić, Marko V., Vujčić, Miroslava, Sladić, Dušan, Strikovic, Zlatko, Todorović, Tamara, Muller, Christian D., "Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction" in RSC Advances, 5, no. 115 (2015):95191-95211,
https://doi.org/10.1039/c5ra19849f . .

TY  - JOUR
AU  - Senćanski, Milan
AU  - Šukalović, Vladimir
AU  - Shakib, Kaveh
AU  - Šoškić, Vukić
AU  - Došen-Mićović, Ljiljana
AU  - Kostić Rajačić, Slađana
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1504
AB  - In this paper, we report the molecular modeling of the 5HT(2A) receptor and the molecular docking of arylpiperazine-like ligands. The focus of the research was on explaining the effects the ligand structure has on the binding properties of the 5HT(2A) receptor and on the key interactions between the ligands and the receptor-binding site. To see what the receptor-ligand interactions were, various substituents were introduced in one part of the ligand, keeping the rest unchanged. In this way, using a docking analysis on the proposed 5HT(2A) receptor model, we identified key receptor-ligand interactions and determined their properties. Those properties were correlated with experimentally determined binding affinities in order to determine the structure to activity relationship of the examined compounds.
PB  - Wiley-Blackwell, Hoboken
T2  - Chemical Biology & Drug Design
T1  - Molecular Modeling of 5HT(2A) Receptor - Arylpiperazine Ligands Interactions
VL  - 83
IS  - 4
SP  - 462
EP  - 471
DO  - 10.1111/cbdd.12261
ER  - 

@article{
author = "Senćanski, Milan and Šukalović, Vladimir and Shakib, Kaveh and Šoškić, Vukić and Došen-Mićović, Ljiljana and Kostić Rajačić, Slađana",
year = "2014",
abstract = "In this paper, we report the molecular modeling of the 5HT(2A) receptor and the molecular docking of arylpiperazine-like ligands. The focus of the research was on explaining the effects the ligand structure has on the binding properties of the 5HT(2A) receptor and on the key interactions between the ligands and the receptor-binding site. To see what the receptor-ligand interactions were, various substituents were introduced in one part of the ligand, keeping the rest unchanged. In this way, using a docking analysis on the proposed 5HT(2A) receptor model, we identified key receptor-ligand interactions and determined their properties. Those properties were correlated with experimentally determined binding affinities in order to determine the structure to activity relationship of the examined compounds.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Chemical Biology & Drug Design",
title = "Molecular Modeling of 5HT(2A) Receptor - Arylpiperazine Ligands Interactions",
volume = "83",
number = "4",
pages = "462-471",
doi = "10.1111/cbdd.12261"
}

Senćanski, M., Šukalović, V., Shakib, K., Šoškić, V., Došen-Mićović, L.,& Kostić Rajačić, S.. (2014). Molecular Modeling of 5HT(2A) Receptor - Arylpiperazine Ligands Interactions. in Chemical Biology & Drug Design
Wiley-Blackwell, Hoboken., 83(4), 462-471.
https://doi.org/10.1111/cbdd.12261

Senćanski M, Šukalović V, Shakib K, Šoškić V, Došen-Mićović L, Kostić Rajačić S. Molecular Modeling of 5HT(2A) Receptor - Arylpiperazine Ligands Interactions. in Chemical Biology & Drug Design. 2014;83(4):462-471.
doi:10.1111/cbdd.12261 .

Senćanski, Milan, Šukalović, Vladimir, Shakib, Kaveh, Šoškić, Vukić, Došen-Mićović, Ljiljana, Kostić Rajačić, Slađana, "Molecular Modeling of 5HT(2A) Receptor - Arylpiperazine Ligands Interactions" in Chemical Biology & Drug Design, 83, no. 4 (2014):462-471,
https://doi.org/10.1111/cbdd.12261 . .

TY  - JOUR
AU  - Šukalović, Vladimir
AU  - Šoškić, Vukić
AU  - Senćanski, Milan
AU  - Andrić, Deana
AU  - Kostić Rajačić, Slađana
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1349
AB  - Interest in structure-based G-protein-coupled receptor (GPCR) ligand discovery is huge, given that almost 30 % of all approved drugs belong to this category of active compounds. The GPCR family includes the dopamine receptor subtype D2 (D2DR), but unfortunately-as is true of most GPCRs-no experimental structures are available for these receptors. In this publication, we present the molecular model of D2DR based on the previously published crystal structure of the dopamine D3 receptor (D3DR). A molecular modeling study using homology modeling and docking simulation provided a rational explanation for the behavior of the arylpiperazine ligand. The observed binding modes and receptor-ligand interactions provided us with fresh clues about how to optimize selectivity for D2DR receptors.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - Determination of key receptor-ligand interactions of dopaminergic arylpiperazines and the dopamine D2 receptor homology model
VL  - 19
IS  - 4
SP  - 1751
EP  - 1762
DO  - 10.1007/s00894-012-1731-6
ER  - 

@article{
author = "Šukalović, Vladimir and Šoškić, Vukić and Senćanski, Milan and Andrić, Deana and Kostić Rajačić, Slađana",
year = "2013",
abstract = "Interest in structure-based G-protein-coupled receptor (GPCR) ligand discovery is huge, given that almost 30 % of all approved drugs belong to this category of active compounds. The GPCR family includes the dopamine receptor subtype D2 (D2DR), but unfortunately-as is true of most GPCRs-no experimental structures are available for these receptors. In this publication, we present the molecular model of D2DR based on the previously published crystal structure of the dopamine D3 receptor (D3DR). A molecular modeling study using homology modeling and docking simulation provided a rational explanation for the behavior of the arylpiperazine ligand. The observed binding modes and receptor-ligand interactions provided us with fresh clues about how to optimize selectivity for D2DR receptors.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "Determination of key receptor-ligand interactions of dopaminergic arylpiperazines and the dopamine D2 receptor homology model",
volume = "19",
number = "4",
pages = "1751-1762",
doi = "10.1007/s00894-012-1731-6"
}

Šukalović, V., Šoškić, V., Senćanski, M., Andrić, D.,& Kostić Rajačić, S.. (2013). Determination of key receptor-ligand interactions of dopaminergic arylpiperazines and the dopamine D2 receptor homology model. in Journal of Molecular Modeling
Springer, New York., 19(4), 1751-1762.
https://doi.org/10.1007/s00894-012-1731-6

Šukalović V, Šoškić V, Senćanski M, Andrić D, Kostić Rajačić S. Determination of key receptor-ligand interactions of dopaminergic arylpiperazines and the dopamine D2 receptor homology model. in Journal of Molecular Modeling. 2013;19(4):1751-1762.
doi:10.1007/s00894-012-1731-6 .

Šukalović, Vladimir, Šoškić, Vukić, Senćanski, Milan, Andrić, Deana, Kostić Rajačić, Slađana, "Determination of key receptor-ligand interactions of dopaminergic arylpiperazines and the dopamine D2 receptor homology model" in Journal of Molecular Modeling, 19, no. 4 (2013):1751-1762,
https://doi.org/10.1007/s00894-012-1731-6 . .

TY  - JOUR
AU  - Senćanski, Milan V.
AU  - Šukalović, Vladimir
AU  - Došen-Mićović, Ljiljana
AU  - Šoškić, Vukić
AU  - Andrić, Deana
AU  - Roglić, Goran
AU  - Kostić Rajačić, Slađana
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1057
AB  - Molecular modelling studies were undertaken in order to identify key interactions of selected ligands with alpha(1A) adrenergic receptor, responsible for their binding and presumably receptor activation. The previously made model of alpha(1A) adrenergic receptor was optimized by molecular dynamics and different arylpiperazine ligands were docked. The results show a high correlation to the experimentally determined binding affinities. Ligand orientations and its interactions with specific amino acid residues in the binding site explain trends in its structure-activity relationship. The key interactions for those trends are mainly aromatic, which are suggested by the calculation of their ESP surfaces.
PB  - Inst Materials Physics, Bucharest
T2  - Digest Journal of Nanomaterials and Biostructures
T1  - Modeling interactions of alpha(1a) adrenergic receptor and different arylpiperazine ligands
VL  - 7
IS  - 4
SP  - 1767
EP  - 1777
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1567
ER  - 

@article{
author = "Senćanski, Milan V. and Šukalović, Vladimir and Došen-Mićović, Ljiljana and Šoškić, Vukić and Andrić, Deana and Roglić, Goran and Kostić Rajačić, Slađana",
year = "2012",
abstract = "Molecular modelling studies were undertaken in order to identify key interactions of selected ligands with alpha(1A) adrenergic receptor, responsible for their binding and presumably receptor activation. The previously made model of alpha(1A) adrenergic receptor was optimized by molecular dynamics and different arylpiperazine ligands were docked. The results show a high correlation to the experimentally determined binding affinities. Ligand orientations and its interactions with specific amino acid residues in the binding site explain trends in its structure-activity relationship. The key interactions for those trends are mainly aromatic, which are suggested by the calculation of their ESP surfaces.",
publisher = "Inst Materials Physics, Bucharest",
journal = "Digest Journal of Nanomaterials and Biostructures",
title = "Modeling interactions of alpha(1a) adrenergic receptor and different arylpiperazine ligands",
volume = "7",
number = "4",
pages = "1767-1777",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1567"
}

Senćanski, M. V., Šukalović, V., Došen-Mićović, L., Šoškić, V., Andrić, D., Roglić, G.,& Kostić Rajačić, S.. (2012). Modeling interactions of alpha(1a) adrenergic receptor and different arylpiperazine ligands. in Digest Journal of Nanomaterials and Biostructures
Inst Materials Physics, Bucharest., 7(4), 1767-1777.
https://hdl.handle.net/21.15107/rcub_cherry_1567

Senćanski MV, Šukalović V, Došen-Mićović L, Šoškić V, Andrić D, Roglić G, Kostić Rajačić S. Modeling interactions of alpha(1a) adrenergic receptor and different arylpiperazine ligands. in Digest Journal of Nanomaterials and Biostructures. 2012;7(4):1767-1777.
https://hdl.handle.net/21.15107/rcub_cherry_1567 .

Senćanski, Milan V., Šukalović, Vladimir, Došen-Mićović, Ljiljana, Šoškić, Vukić, Andrić, Deana, Roglić, Goran, Kostić Rajačić, Slađana, "Modeling interactions of alpha(1a) adrenergic receptor and different arylpiperazine ligands" in Digest Journal of Nanomaterials and Biostructures, 7, no. 4 (2012):1767-1777,
https://hdl.handle.net/21.15107/rcub_cherry_1567 .

TY  - JOUR
AU  - Senćanski, Milan V.
AU  - Šukalović, Vladimir
AU  - Došen-Mićović, Ljiljana
AU  - Šoškić, Vukić
AU  - Andrić, Deana
AU  - Roglić, Goran
AU  - Kostić Rajačić, Slađana
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1146
AB  - Molecular modelling studies were undertaken in order to identify key interactions of selected ligands with α1A adrenergic receptor, responsible for their binding and presumably receptor activation. The previously made model of α1A adrenergic receptor was optimized by molecular dynamics and different arylpiperazine ligands were docked. The results show a high correlation to the experimentally determined binding affinities. Ligand orientations and its interactions with specific amino acid residues in the binding site explain trends in its structure-activity relationship. The key interactions for those trends are mainly aromatic, which are suggested by the calculation of their ESP surfaces.
PB  - Inst Materials Physics, Bucharest
T2  - Digest Journal of Nanomaterials and Biostructures
T1  - Modeling interactions of α1a adrenergic receptor and different arylpiperazine ligands
VL  - 7
IS  - 4
SP  - 1761
EP  - 1777
UR  - https://hdl.handle.net/21.15107/rcub_cherry_112
ER  - 

@article{
author = "Senćanski, Milan V. and Šukalović, Vladimir and Došen-Mićović, Ljiljana and Šoškić, Vukić and Andrić, Deana and Roglić, Goran and Kostić Rajačić, Slađana",
year = "2012",
abstract = "Molecular modelling studies were undertaken in order to identify key interactions of selected ligands with α1A adrenergic receptor, responsible for their binding and presumably receptor activation. The previously made model of α1A adrenergic receptor was optimized by molecular dynamics and different arylpiperazine ligands were docked. The results show a high correlation to the experimentally determined binding affinities. Ligand orientations and its interactions with specific amino acid residues in the binding site explain trends in its structure-activity relationship. The key interactions for those trends are mainly aromatic, which are suggested by the calculation of their ESP surfaces.",
publisher = "Inst Materials Physics, Bucharest",
journal = "Digest Journal of Nanomaterials and Biostructures",
title = "Modeling interactions of α1a adrenergic receptor and different arylpiperazine ligands",
volume = "7",
number = "4",
pages = "1761-1777",
url = "https://hdl.handle.net/21.15107/rcub_cherry_112"
}

Senćanski, M. V., Šukalović, V., Došen-Mićović, L., Šoškić, V., Andrić, D., Roglić, G.,& Kostić Rajačić, S.. (2012). Modeling interactions of α1a adrenergic receptor and different arylpiperazine ligands. in Digest Journal of Nanomaterials and Biostructures
Inst Materials Physics, Bucharest., 7(4), 1761-1777.
https://hdl.handle.net/21.15107/rcub_cherry_112

Senćanski MV, Šukalović V, Došen-Mićović L, Šoškić V, Andrić D, Roglić G, Kostić Rajačić S. Modeling interactions of α1a adrenergic receptor and different arylpiperazine ligands. in Digest Journal of Nanomaterials and Biostructures. 2012;7(4):1761-1777.
https://hdl.handle.net/21.15107/rcub_cherry_112 .

Senćanski, Milan V., Šukalović, Vladimir, Došen-Mićović, Ljiljana, Šoškić, Vukić, Andrić, Deana, Roglić, Goran, Kostić Rajačić, Slađana, "Modeling interactions of α1a adrenergic receptor and different arylpiperazine ligands" in Digest Journal of Nanomaterials and Biostructures, 7, no. 4 (2012):1761-1777,
https://hdl.handle.net/21.15107/rcub_cherry_112 .