title: Study on the binding of luteolin to bovine serum albumin.
abstract: Binding of luteolin (LU) to bovine serum albumin (BSA) was investigated at 298, 308 and 318K at pH 7.4 using spectrophotometric techniques such as fluorescence emission, circular dichroism (CD). The data obtained from fluorescence quenching experiments showed that LU was bound to BSA and binding constants and the number of binding sites (n approximately 1) were obtained. The thermodynamic parameters DeltaH(0), DeltaS(0), DeltaG(0) at different temperatures were calculated. They indicated that both hydrophobic forces and hydrogen bonds are the major interactions between LU and BSA. A value of 3.12nm for the average distance r between LU (acceptor) and tryptophan residue (Trp) of BSA (donor) was derived from the fluorescence resonance energy transfer. The effects of some common metal ions on the binding are also considered. Besides, the interaction of BSA with LU led to a change in the conformation of BSA.
authors: Life and Science Department of Luoyang Teachers' College, Luoyang 471022, PR China.
authors: Yumin
authors: Y
authors: Yang
authors: Qiuluan
authors: Q
authors: Hu
authors: Yanli
authors: Y
authors: Fan
authors: Hongshuai
authors: H
authors: Shen
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D007477:Ions / Q000737:chemistry; D047311:Luteolin / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D015394:Molecular Structure; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D007477:Ions; D008670:Metals; D012710:Serum Albumin, Bovine; D047311:Luteolin