An Investigation of the Molecular Interactions of Diacetylcurcumin with Ribonuclease A

Title: An Investigation of the Molecular Interactions of Diacetylcurcumin with Ribonuclease A

Volume: 16 Issue: 12

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

Affiliation:

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

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.

Cite this article as:

Sahoo Ketan Bijaya, Ghosh Sundar Kalyan and Dasgupta Swagata, An Investigation of the Molecular Interactions of Diacetylcurcumin with Ribonuclease A, Protein & Peptide Letters 2009; 16 (12) . https://dx.doi.org/10.2174/092986609789839278

DOI https://dx.doi.org/10.2174/092986609789839278	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305