NDLI: Spectroscopic and in silico study of binding mechanism of cynidine-3-O-glucoside with human serum albumin and glycated human serum albumin.

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Year: 2016 Volume: 31

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Spectroscopic and in silico study of binding mechanism of cynidine-3-O-glucoside with human serum albumin and glycated human serum albumin.

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Spectroscopic and in silico study of binding mechanism of cynidine-3-O-glucoside with human serum albumin and glycated human serum albumin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gao, Xin Bi, Hongna Jia, Jingjing Tang, Lin
Description	Author Affiliation: Gao X ( School of Life Science, Shandong Normal University, Jinan, People's Republic of China.); Bi H ( School of Life Science, Shandong Normal University, Jinan, People's Republic of China.); Jia J ( School of Life Science, Shandong Normal University, Jinan, People's Republic of China.); Tang L ( School of Life Science, Shandong Normal University, Jinan, People's Republic of China. tanglin@sdnu.edu.cn.)
Abstract	The drug-serum albumin interaction plays a dominant role in drug efficacy and disposition. The glycation of serum albumin that occurs during diabetes may affect its drug-binding properties in vivo. In order to evaluate the interactivity characteristics of cyanidin-3-O-glucoside (C3G) with human serum albumin (HSA) and glycated human serum albumin (gHSA), this study was undertaken using multiple spectroscopic techniques and molecular modeling analysis. Time-resolved fluorescence and the thermodynamic parameters indicated that the quenching mechanism was static quenching, and hydrogen bonding and Van der Waals force were the main forces. The protein fluorescence could be quenched by C3G, whereas the polarity of the fluorophore was not obviously changed. C3G significantly altered the secondary structure of the proteins. Furthermore, the interaction force that existed in the HSA-C3G system was greater than that in the gHSA-C3G system. Fluorescence excitation emission matrix spectra, red edge excitation shift, Fourier transform infrared spectroscopy and circular dichroism spectra provided further evidence that glycation could inhibit the binding between C3G and proteins. In addition, molecular modeling analysis supported the experimental results. The results provided more details for the application of C3G in the treatment of diabetes.
File Format	HTM / HTML
ISSN	15227235
Journal	Luminescence
e-ISSN	15227243
Language	English
Publisher	Wiley-Blackwell
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biophysics Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Chemistry Biophysics

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