期刊
JOURNAL OF PHARMACEUTICAL SCIENCES
卷 93, 期 4, 页码 1039-1046出版社
ELSEVIER SCIENCE INC
DOI: 10.1002/jps.20005
关键词
human serum albumin; antidiabetic agent; fluorescence spectroscopy; absorption spectroscopy; drug interactions; protein binding; thermodynamics
SU-118 is a newly synthesized antidiabetic agent and shows the best hypoglycemic effect among a series of analogs. Its binding properties and binding sites located on human serum albumin (HSA) have been studied using UV absorption and fluorescence spectroscopy. The results of spectroscopic study and the thermodynamic parameters obtained suggest that SU-118 binds to the hydrophobic cavity of human serum albumin and the hydrophobic interaction is the predominant intermolecular force stabilizing the complex. Fluorescent probe displacement studies show that SU-118 can displace competitively both dansylamide and dansylsarcosine from HSA. It is suggested that SU-118 can bind to both site I and site II, but the primary interaction may take place at site I. A binding constant of 1.4 x 10(4) M-1 and a binding site of 2.0 are obtained from absorbance titration data. The value of binding constant is of the same order of magnitude as that from fluorescence titration. This study provides a molecular basis for elucidating the mechanism of drug acting and predicting unfavorable drug interaction. (C) 2004 Wiley-Liss, Inc. and the American Pharmacists Association.
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