Study of nobiletin binding to bovine serum albumin by capillary electrophoresis-frontal analysis and circular dichroism.
A very recent epidemiological study provided strong support for nobiletin (NOB) as a potential candidate chemopreventive agent against cancer. From the pharmacology point of view, drug-protein interactions are determining factors in therapeutic, pharmacodynamic and toxicological drug properties. In this work, for the first time, detection of NOB at near-physiological conditions was accomplished by means of capillary electrophoresis-frontal analysis (CE-FA), and then the binding constants of NOB with bovine serum albumin (BSA) at the same conditions were determined. Complexation of NOB-BSA led to a decrease of the height for free NOB with increasing concentration of BSA. These results revealed the presence of a single class of binding site on BSA, and provided the binding constant of 10(3)/m, showing the strong affinity of NOB for BSA. Furthermore, circular dichroism spectra showed that, when the molar ratio of NOB to BSA was up to 2:1, NOB did not affect the overall protein conformation significantly and the protein thus retained a native-like structure. These results may provide important information for preclinical studies of nobiletin in pharmaceutical research.
Department of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan, People's Republic of China.
Lian
L
Yi
Hailing
H
Li
Qingqing
Q
Deng
Zhongzheng
Z
Yuan
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism / Q000379:methods*; D019075:Electrophoresis, Capillary / Q000379:methods*; D047309:Flavones / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*
D047309:Flavones; D012709:Serum Albumin; C008661:nobiletin