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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

An Investigation of the Molecular Interactions of Diacetylcurcumin with Ribonuclease A

Author(s): Bijaya Ketan Sahoo, Kalyan Sundar Ghosh and Swagata Dasgupta

Volume 16, Issue 12, 2009

Page: [1485 - 1495] Pages: 11

DOI: 10.2174/092986609789839278

Price: $65

Abstract

Curcumin is a natural product with diverse pharmacological activities. Studies of curcumin and its structural derivatives have been a subject of growing interest as a result of their diverse biological activities. We report the interaction of diacetylcurcumin (DAC) with Ribonuclease A (RNase A). The binding constant of DAC with RNase A was found to be of the order of 104 M-1. The intrinsic fluorescence of RNase A was quenched by DAC with a quenching constant of 2.2 x 104 M-1. The distance between the fluorophore of RNase A and DAC was found to be 2.6 nm, calculated from a Förster type fluorescence resonance energy transfer (FRET). Secondary structural changes of RNase A after binding were analyzed from circular dichroism and Fourier transform infrared studies. Protein-ligand docking studies were conducted to determine the residues involved in the interaction of RNase A with DAC and changes in the accessible surface of the interacting residues were calculated accordingly.

Keywords: Diacetylcurcumin, Ribonuclease A, Fluorescence, binding, CD, FTIR, Docking


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