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Multi-spectroscopic and computational evaluation on the binding of sinapic acid and its Cu(II) complex with bovine serum albumin.

Authors
  • Sengupta, Priti1
  • Pal, Uttam2
  • Mondal, Prasenjit1
  • Bose, Adity3
  • 1 Department of Chemistry, Presidency University, 86/1 College Street, Kolkata 700073, India. , (India)
  • 2 Chemical Sciences Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India. , (India)
  • 3 Department of Chemistry, Presidency University, 86/1 College Street, Kolkata 700073, India. Electronic address: [email protected] , (India)
Type
Published Article
Journal
Food chemistry
Publication Date
Dec 15, 2019
Volume
301
Pages
125254–125254
Identifiers
DOI: 10.1016/j.foodchem.2019.125254
PMID: 31398672
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Researches based on metal complexes of plant-derived phenolic acids have attracted much attention due to their beneficial applications in the development of functional food products, dietary supplements and pharmacology. Binding of phenolic acids with serum proteins greatly influences their pharmacological properties. In this context, interactions of a naturally occurring phenolic acid, sinapic acid (SA) and its Cu2+ complex with a model transport protein, bovine serum albumin (BSA), have been explored by means of different spectroscopic and theoretical tools. Spectroscopic studies revealed that the interaction of SA and its Cu2+ complex with BSA occurred through quenching of intrinsic fluorescence of BSA. Site-specific experimental and docking studies were performed to predict the binding site. The geometies of bound Cu2+ and interacting residues of protein were predicted from a solution dynamics study. Interestingly, the complexation of SA with Cu2+ enhanced the antioxidant activity of SA. Copyright © 2019 Elsevier Ltd. All rights reserved.

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