title: Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods.
abstract: The interaction between bisphenol A (BPA) and lysozyme (or trypsin) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. BPA effectively quenched the intrinsic fluorescence of lysozyme and trypsin via static quenching. H-bonds and van der Waals interactions played a major role in stabilizing the BPA-proteinase complex. The distance r between donor and acceptor was obtained to be 1.65 and 2.26 nm for BPA-lysozyme and BPA-trypsin complexes, respectively. The effect of BPA on the conformation of lysozyme and trypsin was analyzed using synchronous fluorescence and three-dimensional fluorescence spectra.
authors.affiliation: Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province, People's Republic of China. wyqing76@126.com
authors.forename: Yan-Qing
authors.initials: YQ
authors.lastname: Wang
authors.forename: Ting-Ting
authors.initials: TT
authors.lastname: Chen
authors.forename: Hong-Mei
authors.initials: HM
authors.lastname: Zhang
mesh_terms: D000818:Animals; D001559:Benzhydryl Compounds; D001665:Binding Sites; D002417:Cattle; D002645:Chickens; D004968:Estrogens, Non-Steroidal / Q000737:chemistry*; D005260:Female; D006801:Humans; D006860:Hydrogen Bonding; D015394:Molecular Structure; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D010636:Phenols / Q000737:chemistry*; D011247:Pregnancy; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence / Q000379:methods*; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism; D000098826:Bisphenol A Compounds
chemical_list: D001559:Benzhydryl Compounds; D004968:Estrogens, Non-Steroidal; D009113:Muramidase; D010636:Phenols; D014357:Trypsin; C006780:bisphenol A; D000098826:Bisphenol A Compounds