Investigating the binding of curcumin derivatives to bovine serum albumin

Bijaya Ketan Sahoo; Kalyan Sundar Ghosh; Swagata Dasgupta

doi:10.1016/j.bpc.2007.10.007

Investigating the binding of curcumin derivatives to bovine serum albumin

Biophys Chem. 2008 Feb;132(2-3):81-8. doi: 10.1016/j.bpc.2007.10.007. Epub 2007 Oct 23.

Authors

Bijaya Ketan Sahoo¹, Kalyan Sundar Ghosh, Swagata Dasgupta

Affiliation

¹ Department of Chemistry, Indian Institute of Technology, Kharagpur, India.

PMID: 18037556
DOI: 10.1016/j.bpc.2007.10.007

Abstract

The interaction of bovine serum albumin (BSA) with isoxazolcurcumin (IOC) and diacetylcurcumin (DAC) has been investigated. Binding constants obtained were found to be in the 10(5) M(-1) range. Minor conformational changes of BSA were observed from circular dichroism (CD) and Fourier transformed infrared (FT-IR) studies on binding. Based on Förster's theory of non-radiation energy transfer, the average binding distance, r between the donor (BSA) and acceptors IOC and DAC was found to be 3.79 and 4.27 nm respectively. Molecular docking of isoxazolcurcumin and diacetylcurcumin with bovine serum albumin indicated that they docked close to Trp 213, which is within the hydrophobic subdomain.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding Sites
Circular Dichroism
Curcumin / analogs & derivatives
Curcumin / analysis*
Curcumin / chemistry
Curcumin / metabolism
Energy Transfer
Hydrophobic and Hydrophilic Interactions
Protein Binding
Serum Albumin, Bovine / chemistry*
Serum Albumin, Bovine / metabolism
Spectroscopy, Fourier Transform Infrared

Substances

Serum Albumin, Bovine
diacetylcurcumin
Curcumin