| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5371863 | Biophysical Chemistry | 2008 | 8 Pages |
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 105 Mâ 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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Authors
Bijaya Ketan Sahoo, Kalyan Sundar Ghosh, Swagata Dasgupta,