Study on interaction of mangiferin to insulin and glucagon in ternary system.
The binding of mangiferin to insulin and glucagon was investigated in the presence and absence of another Peptide by optical spectroscopy. Fluorescence titration experiments revealed that mangiferin quenched the intrinsic fluorescence of insulin and glucagon by static quenching. The ratios of binding constants of glucagon-mangiferin to insulin-mangiferin at different temperatures were calculated in "pure" and ternary system, respectively. The results indicated that the Peptides were competitive with each other to act on mangiferin. Values of the thermodynamic parameters and the experiments of pH effect proved that the key interacting forces between mangiferin and the Peptides were hydrophobic interaction. In addition, UV-vis absorption, synchronous fluorescence and Fourier transform infrared measurements showed that the conformation of insulin and glucagon were changed after adding mangiferin.
State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou 730000, China.
Hui
H
Lin
Rui
R
Chen
Xiaoyan
X
Liu
Fenling
F
Sheng
Haixia
H
Zhang
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005934:Glucagon / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D044004:Xanthones / Q000378:metabolism*
D007328:Insulin; D010455:Peptides; D044004:Xanthones; C013592:mangiferin; D005934:Glucagon