albumin - publications

Predict more albumin - ligand interactions now!


1. Luminescence. 2012 May 18. doi: 10.1002/bio.2374. [Epub ahead of print]

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

Jiang H, Chen R, Wang H, Pu H.

Bio-engineering Institute, College of Life Science and Technology, Jinan
University, Guangzhou, 510632, China.

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 K(a) and number of binding
sites n were calculated at different temperatures. According to Förster'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 ΔH and ΔS
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.
Copyright © 2012 John Wiley & Sons, Ltd.

Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 22605685 [PubMed - as supplied by publisher]