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.
Yi
Lian
L
Department of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan, People's Republic of China.
Li
Hailing
H
Deng
Qingqing
Q
Yuan
Zhongzheng
Z
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