Literature DB >> 18037556

Investigating the binding of curcumin derivatives to bovine serum albumin.

Bijaya Ketan Sahoo1, Kalyan Sundar Ghosh, Swagata Dasgupta.   

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.

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Year:  2007        PMID： 18037556     DOI： 10.1016/j.bpc.2007.10.007

Source DB:  PubMed          Journal:  Biophys Chem        ISSN： 0301-4622            Impact factor:   2.352


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