期刊
PROTEIN AND PEPTIDE LETTERS
卷 16, 期 12, 页码 1485-1495出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986609789839278
关键词
Diacetylcurcumin; Ribonuclease A; Fluorescence; binding; CD; FTIR; Docking
资金
- All India Council for Technical Education (AICTE)
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据