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Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

Mechanistic insights into the interaction of five previously chemically synthesized triazole-linked chalcone analogs (CTs) with human serum albumin (HSA) were sought using various spectroscopic techniques (UV-visible absorption, fluorescence, and circular dichroism) and molecular docking. The fluore...

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Autores principales: Yadav, Priyanka, Yadav, Jitendra Kumar, Agarwal, Alka, Awasthi, Satish K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9072648/
https://www.ncbi.nlm.nih.gov/pubmed/35530759
http://dx.doi.org/10.1039/c9ra04192c
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author Yadav, Priyanka
Yadav, Jitendra Kumar
Agarwal, Alka
Awasthi, Satish K.
author_facet Yadav, Priyanka
Yadav, Jitendra Kumar
Agarwal, Alka
Awasthi, Satish K.
author_sort Yadav, Priyanka
collection PubMed
description Mechanistic insights into the interaction of five previously chemically synthesized triazole-linked chalcone analogs (CTs) with human serum albumin (HSA) were sought using various spectroscopic techniques (UV-visible absorption, fluorescence, and circular dichroism) and molecular docking. The fluorescence quenching experiments performed at three different temperatures (288, 298 and 308 K) revealed the static mode of quenching and the binding constants (K(b) ∼ 10(6–9)) obtained indicated the strong affinity of these analogs for HSA. Furthermore, significant changes in the secondary structure of HSA in the presence of these analogs were also confirmed by far UV-CD spectroscopy. The thermodynamic properties such as the enthalpy change (ΔH°), Gibbs free energy change (ΔG°) and entropy change (ΔS°) revealed that the binding process was spontaneous and exothermic. Theoretical studies, viz., DFT and molecular docking corroborated the experimental results as these five analogs could bind with HSA through hydrogen bonding and hydrophobic interactions. The present study provides useful information regarding the interaction mechanism of these analogs with HSA, which can provide a new avenue to design more potent chalcone triazole analogs for use in the biomedical field.
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spelling pubmed-90726482022-05-06 Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches Yadav, Priyanka Yadav, Jitendra Kumar Agarwal, Alka Awasthi, Satish K. RSC Adv Chemistry Mechanistic insights into the interaction of five previously chemically synthesized triazole-linked chalcone analogs (CTs) with human serum albumin (HSA) were sought using various spectroscopic techniques (UV-visible absorption, fluorescence, and circular dichroism) and molecular docking. The fluorescence quenching experiments performed at three different temperatures (288, 298 and 308 K) revealed the static mode of quenching and the binding constants (K(b) ∼ 10(6–9)) obtained indicated the strong affinity of these analogs for HSA. Furthermore, significant changes in the secondary structure of HSA in the presence of these analogs were also confirmed by far UV-CD spectroscopy. The thermodynamic properties such as the enthalpy change (ΔH°), Gibbs free energy change (ΔG°) and entropy change (ΔS°) revealed that the binding process was spontaneous and exothermic. Theoretical studies, viz., DFT and molecular docking corroborated the experimental results as these five analogs could bind with HSA through hydrogen bonding and hydrophobic interactions. The present study provides useful information regarding the interaction mechanism of these analogs with HSA, which can provide a new avenue to design more potent chalcone triazole analogs for use in the biomedical field. The Royal Society of Chemistry 2019-10-08 /pmc/articles/PMC9072648/ /pubmed/35530759 http://dx.doi.org/10.1039/c9ra04192c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Yadav, Priyanka
Yadav, Jitendra Kumar
Agarwal, Alka
Awasthi, Satish K.
Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title_full Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title_fullStr Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title_full_unstemmed Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title_short Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
title_sort insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9072648/
https://www.ncbi.nlm.nih.gov/pubmed/35530759
http://dx.doi.org/10.1039/c9ra04192c
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