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Spectroscopic investigation of interaction between mangiferin and bovine serum albumin
Hui Lin #,Jingfeng Lan,Min Guan,Fenling Sheng,Haixia Zhang *
College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, China
*Correspondence author
#Submitted by
Subject:
Funding: 国家自然科学基金,新世纪人才计划,兰州大学青年骨干教师计划(No.20775029,,)
Opened online: 8 January 2009
Accepted by: none
Citation: Hui Lin,Jingfeng Lan,Min Guan.Spectroscopic investigation of interaction between mangiferin and bovine serum albumin[OL]. [ 8 January 2009] http://en.paper.edu.cn/en_releasepaper/content/27467
 
 
The mechanism of interaction between mangiferin (MA) and bovine serum albumin (BSA) in aqueous solution was investigated by fluorescence spectra, synchronous fluorescence spectra, absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy. The binding constants and binding sites of MA to BSA at different reaction time were calculated and the distance between the MA and BSA was estimated to be 5.20 nm based on Föster’s theory. In addition, synchronous fluorescence and FT-IR measurements revealed that the secondary structures of the protein changed by the interaction of MA with BSA. Furthermore, the influence of β-cyclodextrin on the system was studied. As a conclusion, the interaction between the anti-diabetes Chinese medicine MA and BSA was studied preliminary which may provide some significant information for the mechanism of the chinese traditional medicine MA on the protein level to cure diabetes or other diseases.
Keywords:Mangiferin;Bovine serum albumin;β-cyclodextrin;Fluorescence;Fourier transform infrared spectroscopy
 
 
 

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