title: Binding of engeletin with bovine serum albumin: insights from spectroscopic investigations.
abstract: In this paper, several spectroscopic techniques were used to investigate the interaction of engeletin (ELN) with bovine serum albumin (BSA). The analysis of UV-Vis absorption and fluorescence spectra revealed that ELN and BSA formed a static complex ELN-BSA, and ELN quenched the fluorescence of BSA effectively. According to the thermodynamic parameters ΔS(0) = 47.27 J·mol(-1)·K(-1) and ΔΗ(0) = -10.34 kJ·mol(-1), the hydrophobic and hydrogen bond interactions were suggested to be the major interaction forces between ELN and BSA. Raman spectroscopy indicated that the binding of ELN slightly changed the conformations and microenviroment of BSA and decreased the α-helix content of BSA.
authors.affiliation: College of Chemistry and Chemical Engineering, Guangxi Normal University, Guilin, 541004, Guangxi Province, People's Republic of China.
authors.forename: Xialian
authors.initials: X
authors.lastname: Peng
authors.forename: Jing
authors.initials: J
authors.lastname: Yu
authors.forename: Qing
authors.initials: Q
authors.lastname: Yu
authors.forename: Hedong
authors.initials: H
authors.lastname: Bian
authors.forename: Fuping
authors.initials: F
authors.lastname: Huang
authors.forename: Hong
authors.initials: H
authors.lastname: Liang
mesh_terms: D000818:Animals; D002417:Cattle; D004365:Drugs, Chinese Herbal / Q000737:chemistry / Q000378:metabolism*; D044948:Flavonols / Q000737:chemistry / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry; D006027:Glycosides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D004365:Drugs, Chinese Herbal; D044948:Flavonols; D005456:Fluorescent Dyes; D006027:Glycosides; C522936:engeletin; D012710:Serum Albumin, Bovine