Journal
LUMINESCENCE
Volume 28, Issue 2, Pages 244-252Publisher
WILEY-BLACKWELL
DOI: 10.1002/bio.2374
Keywords
cyproheptadine hydrochloride; human serum albumin; fluorescence quenching; Fourier transform infrared spectroscopy; molecular modeling
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Funding
- Bio-engineering Institute, College of Life Science and Technology, Jinan University, Guangzhou, China
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The interaction between cyproheptadine hydrochloride (CYP) and human serum albumin (HSA) was investigated by fluorescence spectroscopy, UVvis absorption spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular modeling at a physiological pH (7.40). Fluorescence of HSA was quenched remarkably by CYP and the quenching mechanism was considered as static quenching since it formed a complex. The association constants Ka and number of binding sites n were calculated at different temperatures. According to Forster's theory of non-radiation energy transfer, the distance r between donor (human serum albumin) and acceptor (cyproheptadine hydrochloride) was obtained. The effect of common ions on the binding constant was also investigated. The effect of CYP on the conformation of HSA was analyzed using FT-IR, synchronous fluorescence spectroscopy and 3D fluorescence spectra. The thermodynamic parameters H and S were calculated to be 14.37kJmol1 and 38.03Jmol1K1, respectively, which suggested that hydrophobic forces played a major role in stabilizing the HSA-CYP complex. In addition, examination of molecular modeling indicated that CYP could bind to site I of HSA and that hydrophobic interaction was the major acting force, which was in agreement with binding mode studies. Copyright (c) 2012 John Wiley & Sons, Ltd.
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