Spectroscopic investigation of interaction between mangiferin and bovine serum albumin.
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 times were calculated. And the distance between 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 after the interaction of MA with BSA. As a conclusion, the interaction between the anti-diabetes Chinese medicine MA and BSA may provide some significant information for the mechanism of the traditional chinese medicine MA on the protein level to cure diabetes or other diseases.
Lin
Hui
H
College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000, China.
Lan
Jingfeng
J
Guan
Min
M
Sheng
Fenling
F
Zhang
Haixia
H
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004365:Drugs, Chinese Herbal / Q000737:chemistry / Q000494:pharmacology*; D004735:Energy Transfer; D007004:Hypoglycemic Agents / Q000737:chemistry / Q000494:pharmacology*; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D044004:Xanthones / Q000737:chemistry / Q000494:pharmacology*
D004365:Drugs, Chinese Herbal; D007004:Hypoglycemic Agents; D044004:Xanthones; C013592:mangiferin; D012710:Serum Albumin, Bovine