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Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies
Author(s) -
Sharma Kumkum,
Yadav Priyanka,
Sharma Bhawana,
Pandey Meenakshi,
Awasthi Satish K.
Publication year - 2020
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2834
Subject(s) - circular dichroism , chemistry , docking (animal) , bovine serum albumin , human serum albumin , titration , fluorescence , quenching (fluorescence) , binding constant , serum albumin , fluorescence spectroscopy , stereochemistry , binding site , chromatography , biochemistry , organic chemistry , physics , quantum mechanics , medicine , nursing
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.