TY  - JOUR
AU  - Zelenović, Nevena
AU  - Kojadinovic, Milica
AU  - Filipović, Lidija
AU  - Vucic, Vesna
AU  - Milčić, Miloš
AU  - Arsić, Aleksndra
AU  - Popović, Milica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7223
AB  - Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236   ±   5706 and 69653   ±   14922, respectively, while for UROAG and UROBG, these values were 15179   ±   2770 and 9462   ±   1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.
PB  - SAGE Publications
T2  - Natural Product Communications
T1  - Interactions of Different Urolithins With Bovine Serum Albumin
VL  - 18
IS  - 5
SP  - 1934578X2311693
DO  - 10.1177/1934578X231169366
ER  - 

@article{
author = "Zelenović, Nevena and Kojadinovic, Milica and Filipović, Lidija and Vucic, Vesna and Milčić, Miloš and Arsić, Aleksndra and Popović, Milica",
year = "2023",
abstract = "Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236   ±   5706 and 69653   ±   14922, respectively, while for UROAG and UROBG, these values were 15179   ±   2770 and 9462   ±   1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.",
publisher = "SAGE Publications",
journal = "Natural Product Communications",
title = "Interactions of Different Urolithins With Bovine Serum Albumin",
volume = "18",
number = "5",
pages = "1934578X2311693",
doi = "10.1177/1934578X231169366"
}

Zelenović, N., Kojadinovic, M., Filipović, L., Vucic, V., Milčić, M., Arsić, A.,& Popović, M.. (2023). Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications
SAGE Publications., 18(5), 1934578X2311693.
https://doi.org/10.1177/1934578X231169366

Zelenović N, Kojadinovic M, Filipović L, Vucic V, Milčić M, Arsić A, Popović M. Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications. 2023;18(5):1934578X2311693.
doi:10.1177/1934578X231169366 .

Zelenović, Nevena, Kojadinovic, Milica, Filipović, Lidija, Vucic, Vesna, Milčić, Miloš, Arsić, Aleksndra, Popović, Milica, "Interactions of Different Urolithins With Bovine Serum Albumin" in Natural Product Communications, 18, no. 5 (2023):1934578X2311693,
https://doi.org/10.1177/1934578X231169366 . .

TY  - JOUR
AU  - Zelenović, Nevena
AU  - Filipović, Lidija
AU  - Popović, Milica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7216
AB  - Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.
PB  - Springer
T2  - Biochemistry (Moscow)
T1  - Recent Developments in Bioprocessing of Recombinant Antibody Fragments
VL  - 88
IS  - 9
SP  - 1191
EP  - 1204
DO  - 10.1134/S0006297923090018
ER  - 

@article{
author = "Zelenović, Nevena and Filipović, Lidija and Popović, Milica",
year = "2023",
abstract = "Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.",
publisher = "Springer",
journal = "Biochemistry (Moscow)",
title = "Recent Developments in Bioprocessing of Recombinant Antibody Fragments",
volume = "88",
number = "9",
pages = "1191-1204",
doi = "10.1134/S0006297923090018"
}

Zelenović, N., Filipović, L.,& Popović, M.. (2023). Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow)
Springer., 88(9), 1191-1204.
https://doi.org/10.1134/S0006297923090018

Zelenović N, Filipović L, Popović M. Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow). 2023;88(9):1191-1204.
doi:10.1134/S0006297923090018 .

Zelenović, Nevena, Filipović, Lidija, Popović, Milica, "Recent Developments in Bioprocessing of Recombinant Antibody Fragments" in Biochemistry (Moscow), 88, no. 9 (2023):1191-1204,
https://doi.org/10.1134/S0006297923090018 . .

TY  - CONF
AU  - Protić-Rosić, Isidora
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3546
AB  - The sublingual route of allergens administration in allergen-specific immunotherapy (ASIT) is proven to be a successful way to treat patients with respiratory allergy. The trend of replacing natural extracts with purified recombinant allergens is growing. Although the purified allergens themselves are not good immunogens, the combined vector systems and adjuvans can improve their immunogenicity 1. Cell surfaces are decorated by different glycan structures, so the lectins specific for these glycans can be used to deliver particular therapeutic to target specific tissue 2. Banana lectin (BanLec) is mannose-specific protein which belongs to the subfamily of Jacalin related lectins 3. Apart from its characteristic to bind glycans, BanLec also modulates immune cells in vitro 4. On the other hand, Bet v 1 (Betula verrucosa) is the major birch pollen allergen. T-cell epitops are distributed over almost entire protein structure 5. In the study the recombinant BanLec-Bet v 1 construct is designed, produced by the recombinant DNA technology, purified and characterized by classical biochemical methods for the application in the ASIT of birch pollen allergy. The expression of newly designed BanLec-Bet v 1 was performed in E. coli BL21 (DE3). After expression the protein was found in the inclusion bodies from which it was extracted with 4 M urea solution. After renaturation, affinity chromatography (Sephadex G-75 superfine) was used for protein purification. Biochemical characterization of the chimera was performed by: SDS PAGE electrophoreses, CD spectroscopy and mass spectrometry. Biological activity of the construct was confirmed by binding of BanLecBet v 1 to a horseradish peroxidase glycoprotein in ELISA. Purified BanLec-Bet v 1 showed molecular mass of 32 kDa. CD spectra of the recombinant construct revealed well defined secondary structures with predominant beta sheets (41.2%). By mass spectrometry 51.8% of the BanLec-Bet v 1 primary structure was confirmed. Biologicaly active recombinant BanLec-Bet v 1 was produced by the recombinant DNA technology. Further in vitro and in vivo studies will evaluate immunomodulatory potential of BanLec-Bet v 1 for application in ASIT.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia
T1  - Production, purification and structural characterisation of recombinant BanLec-Bet v 1
SP  - 177
EP  - 178
UR  - https://hdl.handle.net/21.15107/rcub_cer_3546
ER  - 

@conference{
author = "Protić-Rosić, Isidora and Popović, Milica and Anđelković, Uroš and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "The sublingual route of allergens administration in allergen-specific immunotherapy (ASIT) is proven to be a successful way to treat patients with respiratory allergy. The trend of replacing natural extracts with purified recombinant allergens is growing. Although the purified allergens themselves are not good immunogens, the combined vector systems and adjuvans can improve their immunogenicity 1. Cell surfaces are decorated by different glycan structures, so the lectins specific for these glycans can be used to deliver particular therapeutic to target specific tissue 2. Banana lectin (BanLec) is mannose-specific protein which belongs to the subfamily of Jacalin related lectins 3. Apart from its characteristic to bind glycans, BanLec also modulates immune cells in vitro 4. On the other hand, Bet v 1 (Betula verrucosa) is the major birch pollen allergen. T-cell epitops are distributed over almost entire protein structure 5. In the study the recombinant BanLec-Bet v 1 construct is designed, produced by the recombinant DNA technology, purified and characterized by classical biochemical methods for the application in the ASIT of birch pollen allergy. The expression of newly designed BanLec-Bet v 1 was performed in E. coli BL21 (DE3). After expression the protein was found in the inclusion bodies from which it was extracted with 4 M urea solution. After renaturation, affinity chromatography (Sephadex G-75 superfine) was used for protein purification. Biochemical characterization of the chimera was performed by: SDS PAGE electrophoreses, CD spectroscopy and mass spectrometry. Biological activity of the construct was confirmed by binding of BanLecBet v 1 to a horseradish peroxidase glycoprotein in ELISA. Purified BanLec-Bet v 1 showed molecular mass of 32 kDa. CD spectra of the recombinant construct revealed well defined secondary structures with predominant beta sheets (41.2%). By mass spectrometry 51.8% of the BanLec-Bet v 1 primary structure was confirmed. Biologicaly active recombinant BanLec-Bet v 1 was produced by the recombinant DNA technology. Further in vitro and in vivo studies will evaluate immunomodulatory potential of BanLec-Bet v 1 for application in ASIT.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia",
title = "Production, purification and structural characterisation of recombinant BanLec-Bet v 1",
pages = "177-178",
url = "https://hdl.handle.net/21.15107/rcub_cer_3546"
}

Protić-Rosić, I., Popović, M., Anđelković, U.,& Gavrović-Jankulović, M.. (2018). Production, purification and structural characterisation of recombinant BanLec-Bet v 1. in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia
Serbian Biochemical Society., 177-178.
https://hdl.handle.net/21.15107/rcub_cer_3546

Protić-Rosić I, Popović M, Anđelković U, Gavrović-Jankulović M. Production, purification and structural characterisation of recombinant BanLec-Bet v 1. in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia. 2018;:177-178.
https://hdl.handle.net/21.15107/rcub_cer_3546 .

Protić-Rosić, Isidora, Popović, Milica, Anđelković, Uroš, Gavrović-Jankulović, Marija, "Production, purification and structural characterisation of recombinant BanLec-Bet v 1" in Serbian Biochemical Society Eighth Conference with international participation, “Coordination in Biochemistry and Life”, University of Novi Sad – Rectorate Hall, 16.11.2018. Novi Sad, Serbia (2018):177-178,
https://hdl.handle.net/21.15107/rcub_cer_3546 .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2122
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2985
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - JOUR
AU  - Prokopovic, Vladimir
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Marsavelski, Aleksandra
AU  - Raskovic, Brankica
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1508
AB  - Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Archives of Oral Biology
T1  - Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
VL  - 59
IS  - 3
SP  - 302
EP  - 309
DO  - 10.1016/j.archoralbio.2013.12.005
ER  - 

@article{
author = "Prokopovic, Vladimir and Popović, Milica and Anđelković, Uroš and Marsavelski, Aleksandra and Raskovic, Brankica and Gavrović-Jankulović, Marija and Polović, Natalija",
year = "2014",
abstract = "Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Archives of Oral Biology",
title = "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein",
volume = "59",
number = "3",
pages = "302-309",
doi = "10.1016/j.archoralbio.2013.12.005"
}

Prokopovic, V., Popović, M., Anđelković, U., Marsavelski, A., Raskovic, B., Gavrović-Jankulović, M.,& Polović, N.. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology
Oxford : Pergamon-Elsevier Science Ltd., 59(3), 302-309.
https://doi.org/10.1016/j.archoralbio.2013.12.005

Prokopovic V, Popović M, Anđelković U, Marsavelski A, Raskovic B, Gavrović-Jankulović M, Polović N. Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology. 2014;59(3):302-309.
doi:10.1016/j.archoralbio.2013.12.005 .

Prokopovic, Vladimir, Popović, Milica, Anđelković, Uroš, Marsavelski, Aleksandra, Raskovic, Brankica, Gavrović-Jankulović, Marija, Polović, Natalija, "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein" in Archives of Oral Biology, 59, no. 3 (2014):302-309,
https://doi.org/10.1016/j.archoralbio.2013.12.005 . .

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1189
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
VL  - 94
SP  - 53
EP  - 59
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
volume = "94",
pages = "53-59",
doi = "10.1016/j.phytochem.2013.06.006"
}

Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Oxford : Pergamon-Elsevier Science Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006

Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .

Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1290
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
VL  - 53
IS  - 1
SP  - 100
EP  - 105
DO  - 10.1007/s12088-012-0319-2
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
volume = "53",
number = "1",
pages = "100-105",
doi = "10.1007/s12088-012-0319-2"
}

Popović, M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M.. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2

Popović M, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology. 2013;53(1):100-105.
doi:10.1007/s12088-012-0319-2 .

Popović, Milica, Anđelković, Uroš, Grozdanović, Milica, Aleksić, Ivana, Gavrović-Jankulović, Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" in Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 . .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1024
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley-Blackwell, Malden
T2  - Molecular Nutrition & Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
VL  - 56
IS  - 3
SP  - 446
EP  - 453
DO  - 10.1002/mnfr.201100541
ER  - 

@article{
author = "Aleksić, Ivana and Popović, Milica and Dimitrijević, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley-Blackwell, Malden",
journal = "Molecular Nutrition & Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
volume = "56",
number = "3",
pages = "446-453",
doi = "10.1002/mnfr.201100541"
}

Aleksić, I., Popović, M., Dimitrijević, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition & Food Research
Wiley-Blackwell, Malden., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541

Aleksić I, Popović M, Dimitrijević R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition & Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .

Aleksić, Ivana, Popović, Milica, Dimitrijević, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition & Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .

TY  - JOUR
AU  - Ahmedi, Khaled S. O. H
AU  - Milosavić, Nenad
AU  - Popović, Milica
AU  - Prodanović, Radivoje M.
AU  - Knežević-Jugović, Zorica D.
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4302
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
T1  - Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae
VL  - 72
IS  - 12
SP  - 1255
EP  - 1263
DO  - 10.2298/JSC0712255A
ER  - 

@article{
author = "Ahmedi, Khaled S. O. H and Milosavić, Nenad and Popović, Milica and Prodanović, Radivoje M. and Knežević-Jugović, Zorica D. and Jankov, Ratko M.",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae",
volume = "72",
number = "12",
pages = "1255-1263",
doi = "10.2298/JSC0712255A"
}

Ahmedi, K. S. O. H., Milosavić, N., Popović, M., Prodanović, R. M., Knežević-Jugović, Z. D.,& Jankov, R. M.. (2007). Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 72(12), 1255-1263.
https://doi.org/10.2298/JSC0712255A

Ahmedi KSOH, Milosavić N, Popović M, Prodanović RM, Knežević-Jugović ZD, Jankov RM. Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
doi:10.2298/JSC0712255A .

Ahmedi, Khaled S. O. H, Milosavić, Nenad, Popović, Milica, Prodanović, Radivoje M., Knežević-Jugović, Zorica D., Jankov, Ratko M., "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://doi.org/10.2298/JSC0712255A . .

TY  - JOUR
AU  - Dešić, Maja N.
AU  - Popović, Milica
AU  - Obradović, Maja
AU  - Vračar, Ljiljana M.
AU  - Grgur, Branimir N.
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/202
AB  - Surface modification of the electrodes was conducted from sulfuric acid solutions containing the corresponding metal-chloride complexes using cyclic voltammeter. Comparing the charges of the hydrogen underpotential deposition region, and the corresponding oxide reduction regions, it is concluded that a platinum overlayer on gold forms 3D islands, while gold on platinum forms 2D islands. Foreign metals present in an amount of up to one monolayer exert an influence on the change in reaction rate with respect to both hydrogen evolution (HER) and oxygen reduction (ORR) reactions. Aplatinum overlayer on a gold substrate increases the activity for HER and for ORR, compared with pure gold. These results can be understood in terms of a simple model, in which the change in the H and OH binding energies are directly proportional to the shift of the d-bond center of the overlayer. On the contrary, a gold layer on platinum slightly decreases the activity for both reactions compared with pure platinum.
AB  - Površinska modifikacija platine zlatom i zlata platinom je izvršena iz rastvora sumporne kiseline i odgovarajućih hloridnih kompleksa metala primenom ciklične voltametrije. Poređenjem količine naelektrisanja u oblasti potpotencijalne depozicije vodonika i odgovarajućih oblasti redukcije oskida čistih i modifikovanih elektroda zaključeno je da platina na zlatu formira 3D, a zlato na platini 2D ostrva. Aktivnosti ovako modifikovanih površina za reakcije izdvajanja vodonika i redukcije kiseonika u rastvoru sumporne kiseline poređene sa aktivnostima čistih metala. Elektroda od zlata modifikovana platinom značajno uvećava aktivnost za obe ispitivane rekacije u poređenju sa čistim zlatom. Sa druge strane, elektroda od platine modifikovana zlatom ima neznatno manju aktivnost u poređenju sa čistom platinom. Zbog ograničenih resursa i visoke cene platine platina modifikovana zlatom može biti zamena za čistu platinu kao dobar katalizator za reakciju redukcije kiseonika, posebno u gorivim spregovima u oblasti niskih temperatura.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Study of gold-platinum and platinum-gold surface modification and its influence on hydrogen evolution and oxygen reduction
T1  - Površinska modifikacija platine zlatom i zlata platinom i njen uticaj na reakcije izdvajanja vodonika i redukcije kiseonika
VL  - 70
IS  - 2
SP  - 231
EP  - 242
DO  - 10.2298/JSC0502231D
ER  - 

@article{
author = "Dešić, Maja N. and Popović, Milica and Obradović, Maja and Vračar, Ljiljana M. and Grgur, Branimir N.",
year = "2005",
abstract = "Surface modification of the electrodes was conducted from sulfuric acid solutions containing the corresponding metal-chloride complexes using cyclic voltammeter. Comparing the charges of the hydrogen underpotential deposition region, and the corresponding oxide reduction regions, it is concluded that a platinum overlayer on gold forms 3D islands, while gold on platinum forms 2D islands. Foreign metals present in an amount of up to one monolayer exert an influence on the change in reaction rate with respect to both hydrogen evolution (HER) and oxygen reduction (ORR) reactions. Aplatinum overlayer on a gold substrate increases the activity for HER and for ORR, compared with pure gold. These results can be understood in terms of a simple model, in which the change in the H and OH binding energies are directly proportional to the shift of the d-bond center of the overlayer. On the contrary, a gold layer on platinum slightly decreases the activity for both reactions compared with pure platinum., Površinska modifikacija platine zlatom i zlata platinom je izvršena iz rastvora sumporne kiseline i odgovarajućih hloridnih kompleksa metala primenom ciklične voltametrije. Poređenjem količine naelektrisanja u oblasti potpotencijalne depozicije vodonika i odgovarajućih oblasti redukcije oskida čistih i modifikovanih elektroda zaključeno je da platina na zlatu formira 3D, a zlato na platini 2D ostrva. Aktivnosti ovako modifikovanih površina za reakcije izdvajanja vodonika i redukcije kiseonika u rastvoru sumporne kiseline poređene sa aktivnostima čistih metala. Elektroda od zlata modifikovana platinom značajno uvećava aktivnost za obe ispitivane rekacije u poređenju sa čistim zlatom. Sa druge strane, elektroda od platine modifikovana zlatom ima neznatno manju aktivnost u poređenju sa čistom platinom. Zbog ograničenih resursa i visoke cene platine platina modifikovana zlatom može biti zamena za čistu platinu kao dobar katalizator za reakciju redukcije kiseonika, posebno u gorivim spregovima u oblasti niskih temperatura.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Study of gold-platinum and platinum-gold surface modification and its influence on hydrogen evolution and oxygen reduction, Površinska modifikacija platine zlatom i zlata platinom i njen uticaj na reakcije izdvajanja vodonika i redukcije kiseonika",
volume = "70",
number = "2",
pages = "231-242",
doi = "10.2298/JSC0502231D"
}

Dešić, M. N., Popović, M., Obradović, M., Vračar, L. M.,& Grgur, B. N.. (2005). Study of gold-platinum and platinum-gold surface modification and its influence on hydrogen evolution and oxygen reduction. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 70(2), 231-242.
https://doi.org/10.2298/JSC0502231D

Dešić MN, Popović M, Obradović M, Vračar LM, Grgur BN. Study of gold-platinum and platinum-gold surface modification and its influence on hydrogen evolution and oxygen reduction. in Journal of the Serbian Chemical Society. 2005;70(2):231-242.
doi:10.2298/JSC0502231D .

Dešić, Maja N., Popović, Milica, Obradović, Maja, Vračar, Ljiljana M., Grgur, Branimir N., "Study of gold-platinum and platinum-gold surface modification and its influence on hydrogen evolution and oxygen reduction" in Journal of the Serbian Chemical Society, 70, no. 2 (2005):231-242,
https://doi.org/10.2298/JSC0502231D . .