Sahoo, Bijaya Ketan ; Ghosh, Kalyan Sundar ; Dasgupta, Swagata (2008) Investigating the binding of curcumin derivatives to bovine serum albumin Biophysical Chemistry, 132 (2-3). pp. 81-88. ISSN 0301-4622
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Official URL: https://www.sciencedirect.com/science/article/abs/...
Related URL: http://dx.doi.org/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 105 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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Bovine Serum Albumin; Isoxazolcurcumin; Diacetylcurcumin; UV–Visible; Conformational Studies; Docking |
| ID Code: | 113755 |
| Deposited On: | 15 May 2018 06:27 |
| Last Modified: | 15 May 2018 06:27 |
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