Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies.

Autor: Sharma K; Chemical Biology Laboratory, Department of Chemistry, University of Delhi, New Delhi, India., Yadav P; Chemical Biology Laboratory, Department of Chemistry, University of Delhi, New Delhi, India., Sharma B; Chemical Biology Laboratory, Department of Chemistry, University of Delhi, New Delhi, India., Pandey M; Chemical Biology Laboratory, Department of Chemistry, University of Delhi, New Delhi, India., Awasthi SK; Chemical Biology Laboratory, Department of Chemistry, University of Delhi, New Delhi, India.
Jazyk: angličtina
Zdroj: Journal of molecular recognition : JMR [J Mol Recognit] 2020 Jun; Vol. 33 (6), pp. e2834. Date of Electronic Publication: 2020 Feb 03.
DOI: 10.1002/jmr.2834
Abstrakt: The interaction of triazole substituted 4-methyl-7-hydroxycoumarin derivatives (CUM1-4) with serum albumin (bovine serum albumin [BSA] and human serum albumin [HSA]) have been studied employing ultraviolet-visible (UV-Vis), fluorescence, circular dichroism (CD) spectroscopy, and molecular docking methods at physiological pH 7.4. The fluorescence quenching occurred with increasing concentration of CUMs, and the binding constant of CUM derivatives with BSA and HSA obtained from fluorescence quenching experiment was found to be ~ 10 4  L mol -1 . CD study showed conformational changes in the secondary structure of serum albumin upon titration of CUMs. The observed experimental results were further validated by theoretical studies involving density functional theory (DFT) and molecular docking.
(© 2020 John Wiley & Sons Ltd.)
Databáze: MEDLINE
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