Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins

Roy, Durba ; Dutta, Samrajnee ; Maity, Shyam Sundar ; Ghosh, Sanjib ; Singha Roy, Atanu ; Ghosh, Kalyan Sundar ; Dasgupta, Swagata (2012) Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins Journal of Luminescence, 132 (6). pp. 1364-1375. ISSN 0022-2313

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Official URL: https://www.sciencedirect.com/science/article/pii/...

Related URL: http://dx.doi.org/10.1016/j.jlumin.2011.12.063

Abstract

The interactions of two stereoisomeric antioxidant flavonoids, catechin (C) and epicatechin (EC) with bovine serum albumin (BSA) and human serum albumin (HSA), have been investigated by steady state and time resolved fluorescence, phosphorescence, circular dichroism (CD), FTIR and protein–ligand docking studies. The steady-state fluorescence studies indicate a single binding site for both the ligands. FTIR spectra suggest that in both the albumins, C and EC stabilize the α-helix at the cost of a corresponding loss in the β-sheet structure. CD studies have been carried out using (±)C, and both the epimers (+)C and (−)C. The low temperature phosphorescence and protein–ligand [(+), (−) and (±) forms of C and EC] docking studies indicate that the ligands bind in the proximity of Trp 134 of BSA and Trp 214 of HSA, thereby changing their solvent accessible surface areas (ASA). Asn 158 and Glu 130 side chains are found to be within the hydrogen bonding distance from the phenolic –OH groups of C and EC in the case of BSA complex. C and EC are located within the binding pocket of sub-domain IIa of HSA.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Catechins; Serum Albumin; FTIR; Phosphorescence; Flexx Single Molecule Docking; Accessible Surface Area
ID Code:113817
Deposited On:15 May 2018 06:23
Last Modified:15 May 2018 06:23

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