CER - Centralni Repozitorijum IHTM-a
Institut za hemiju, tehnologiju i metalurgiju
    • English
    • Српски
    • Српски (Serbia)
  • Srpski (latinica) 
    • Engleski
    • Srpski (ćirilica)
    • Srpski (latinica)
  • Prijava
Pregled rada 
  •   CER - Repozitorijum Instituta za hemiju, tehnologiju i metalurgiju
  • IHTM
  • Radovi istraživača / Researchers' publications
  • Pregled rada
  •   CER - Repozitorijum Instituta za hemiju, tehnologiju i metalurgiju
  • IHTM
  • Radovi istraživača / Researchers' publications
  • Pregled rada
JavaScript is disabled for your browser. Some features of this site may not work without it.

Human serum albumin binding of certain antimalarials

Samo za registrovane korisnike
2018
Autori
Marković, Olivera
Cvijetić, Ilija
Zlatović, Mario
Opsenica, Igor
Konstantinović, Jelena M.
Terzić-Jovanović, Nataša
Šolaja, Bogdan
Verbić, Tatjana
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentu
Apstrakt
Interactions between eight in-house synthesized aminoquinolines, along with well-known chloroquine, and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The synthesized aminoquinolines, despite being structurally diverse, were found to be very potent antimalarials. Fluorescence measurements indicate that three compounds having additional thiophene or benzothiophene substructure bind more strongly to HSA than other studied compounds. Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site. Fluorescence quenching at three temperatures (20, 25, and 37 degrees C) was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. The enthalpy and entropy changes upon sulphur-containing compound-HSA interactions were calculated using Van't Hoff equation. Positive values of enthalpy and entropy changes indicate that non-specific, hydrophobic interactio...ns are the main contributors to HSA-compound interaction. Molecular docking and calculated lipophilicity descriptors indicate the same, pointing out that the increased lipophilicity of sulphur-containing compounds might be a reason for their better binding to HSA. Obtained results might contribute to design of novel derivatives with improved-pharmacokinetic properties and drug efficacy.

Ključne reči:
Aminoquinolines / Human serum albumin / Fluorescence spectroscopy / Binding affinity / Molecular docking / Stem-Volmer plot
Izvor:
Spectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy, 2018, 192, 128-139
Izdavač:
  • Pergamon-Elsevier Science Ltd, Oxford
Projekti:
  • Sinteza aminohinolina i njihovih derivata kao antimalarika i inhibitora botulinum neurotoksina A (RS-172008)
  • Racionalni dizajn i sinteza biološki aktivnih i koordinacionih jedinjenja i funkcionalnih materijala, relevantnih u (bio)nanotehnologiji (RS-172035)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
  • Serbian Academy of Sciences and Arts [F80]

DOI: 10.1016/j.saa.2017.10.061

ISSN: 1386-1425

PubMed: 29128746

WoS: 000424716900019

Scopus: 2-s2.0-85032915981
[ Google Scholar ]
10
10
URI
http://cer.ihtm.bg.ac.rs/handle/123456789/2472
Kolekcije
  • Radovi istraživača / Researchers' publications
Institucija
IHTM
TY  - JOUR
AU  - Marković, Olivera
AU  - Cvijetić, Ilija
AU  - Zlatović, Mario
AU  - Opsenica, Igor
AU  - Konstantinović, Jelena M.
AU  - Terzić-Jovanović, Nataša
AU  - Šolaja, Bogdan
AU  - Verbić, Tatjana
PY  - 2018
UR  - http://cer.ihtm.bg.ac.rs/handle/123456789/2472
AB  - Interactions between eight in-house synthesized aminoquinolines, along with well-known chloroquine, and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The synthesized aminoquinolines, despite being structurally diverse, were found to be very potent antimalarials. Fluorescence measurements indicate that three compounds having additional thiophene or benzothiophene substructure bind more strongly to HSA than other studied compounds. Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site. Fluorescence quenching at three temperatures (20, 25, and 37 degrees C) was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. The enthalpy and entropy changes upon sulphur-containing compound-HSA interactions were calculated using Van't Hoff equation. Positive values of enthalpy and entropy changes indicate that non-specific, hydrophobic interactions are the main contributors to HSA-compound interaction. Molecular docking and calculated lipophilicity descriptors indicate the same, pointing out that the increased lipophilicity of sulphur-containing compounds might be a reason for their better binding to HSA. Obtained results might contribute to design of novel derivatives with improved-pharmacokinetic properties and drug efficacy.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Spectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy
T1  - Human serum albumin binding of certain antimalarials
VL  - 192
SP  - 128
EP  - 139
DO  - 10.1016/j.saa.2017.10.061
ER  - 
@article{
author = "Marković, Olivera and Cvijetić, Ilija and Zlatović, Mario and Opsenica, Igor and Konstantinović, Jelena M. and Terzić-Jovanović, Nataša and Šolaja, Bogdan and Verbić, Tatjana",
year = "2018",
url = "http://cer.ihtm.bg.ac.rs/handle/123456789/2472",
abstract = "Interactions between eight in-house synthesized aminoquinolines, along with well-known chloroquine, and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The synthesized aminoquinolines, despite being structurally diverse, were found to be very potent antimalarials. Fluorescence measurements indicate that three compounds having additional thiophene or benzothiophene substructure bind more strongly to HSA than other studied compounds. Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site. Fluorescence quenching at three temperatures (20, 25, and 37 degrees C) was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. The enthalpy and entropy changes upon sulphur-containing compound-HSA interactions were calculated using Van't Hoff equation. Positive values of enthalpy and entropy changes indicate that non-specific, hydrophobic interactions are the main contributors to HSA-compound interaction. Molecular docking and calculated lipophilicity descriptors indicate the same, pointing out that the increased lipophilicity of sulphur-containing compounds might be a reason for their better binding to HSA. Obtained results might contribute to design of novel derivatives with improved-pharmacokinetic properties and drug efficacy.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Spectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy",
title = "Human serum albumin binding of certain antimalarials",
volume = "192",
pages = "128-139",
doi = "10.1016/j.saa.2017.10.061"
}
Marković O, Cvijetić I, Zlatović M, Opsenica I, Konstantinović JM, Terzić-Jovanović N, Šolaja B, Verbić T. Human serum albumin binding of certain antimalarials. Spectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy. 2018;192:128-139
Marković, O., Cvijetić, I., Zlatović, M., Opsenica, I., Konstantinović, J. M., Terzić-Jovanović, N., Šolaja, B.,& Verbić, T. (2018). Human serum albumin binding of certain antimalarials.
Spectrochimica Acta Part A-Molecular and Biomolecular SpectroscopyPergamon-Elsevier Science Ltd, Oxford., 192, 128-139.
https://doi.org/10.1016/j.saa.2017.10.061
Marković Olivera, Cvijetić Ilija, Zlatović Mario, Opsenica Igor, Konstantinović Jelena M., Terzić-Jovanović Nataša, Šolaja Bogdan, Verbić Tatjana, "Human serum albumin binding of certain antimalarials" 192 (2018):128-139,
https://doi.org/10.1016/j.saa.2017.10.061 .

DSpace software copyright © 2002-2015  DuraSpace
O Centralnom repozitorijumu (CeR) | Pošaljite zapažanja

OpenAIRERCUB
 

 

Kompletan repozitorijumInstitucijeAutoriNasloviTemeOva institucijaAutoriNasloviTeme

Statistika

Pregled statistika

DSpace software copyright © 2002-2015  DuraSpace
O Centralnom repozitorijumu (CeR) | Pošaljite zapažanja

OpenAIRERCUB