title: An investigation of the molecular interactions of diacetylcurcumin with ribonuclease A.
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 10(4) M(-1). The intrinsic fluorescence of RNase A was quenched by DAC with a quenching constant of 2.2 x10(4) 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.
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Kharagpur, India.
authors.forename: Bijaya Ketan
authors.initials: BK
authors.lastname: Sahoo
authors.forename: Kalyan Sundar
authors.initials: KS
authors.lastname: Ghosh
authors.forename: Swagata
authors.initials: S
authors.lastname: Dasgupta
mesh_terms: D001665:Binding Sites; D003474:Curcumin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D012259:Ribonuclease, Pancreatic / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008024:Ligands; C493686:diacetylcurcumin; D012259:Ribonuclease, Pancreatic; D003474:Curcumin