Investigating the binding of curcumin derivatives to bovine serum albumin

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 dichroisin (CD) and Fourier transformed infrared (FT-IR) studies on binding. Based on Forster'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 isoxazoicurcumin and diacetylcurcumin with bovine serum albumin indicated that they docked close to Tip 213, which is within the hydrophobic subdomain. (C) 2007 Elsevier B.V. All rights reserved.