Interaction of cyproheptadine hydrochloride with human serum albumin using spectroscopy and molecular modeling methods.

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Jiang H, Chen R, Wang H, Pu H

Interaction of cyproheptadine hydrochloride with human serum albumin using spectroscopy and molecular modeling methods.

Luminescence. 2013 Mar-Apr;28(2):244-52. doi: 10.1002/bio.2374. Epub 2012 May 18.

PubMed ID

22605685 [ View in PubMed

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Abstract

The interaction between cyproheptadine hydrochloride (CYP) and human serum albumin (HSA) was investigated by fluorescence spectroscopy, UV-vis 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 DeltaH and DeltaS were calculated to be -14.37 kJ mol(-1) and 38.03 J mol(-1) K(-1), 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.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Cyproheptadine	Serum albumin	Protein	Humans	Unknown	Binder	Details