An Investigation of the Molecular Interactions of Diacetylcurcumin with Ribonuclease A

作者：Sahoo Bijaya Ketan; Ghosh Kalyan Sundar; Dasgupta Swagata^*

来源：Protein and Peptide Letters, 2009, 16(12): 1485-1495.

DOI：10.2174/092986609789839278

• Diacetylcurcumin
• Ribonuclease A
• Fluorescence
• binding
• CD
• FTIR
• Docking

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 10(4) M(-1). The intrinsic fluorescence of RNase A was quenched by DAC with a quenching constant of 2.2 x 10(4) M(-1). The distance between the fluorophore of RNase A and DAC was found to be 2.6 nm, calculated from a Forster 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.

• 出版日期2009