title: Kinetics and thermodynamics of 1-anilino-8-naphthalene sulfonate interactions with Urinary Trypsin Inhibitor.
abstract: The interactions between Urinary Trypsin Inhibitor (UTI) and 1-anilino-8-naphthalene sulfonate (ANS) were investigated by fluorescence spectra, isothermal titration calorimetry and molecular modeling. The results revealed the presence of four specific binding sites for ANS on UTI, with interactions driven mainly by electrostatic forces. The four specific binding sites indicated the involvement of four hydrophobic patches on UTI. Experimental data also confirmed the presence of a further five nonspecific binding sites that interacted mainly by the formation of salt bridges between the sulfonates of ANS and positive residues on the surface of UTI.
authors.affiliation: College of Chemical Engineering and Technology, Wuhan University of Science and Technology, Wuhan, 430081, China. zuozhenyu@wust.edu.cn
authors.forename: Zhenyu
authors.initials: Z
authors.lastname: Zuo
authors.forename: Handong
authors.initials: H
authors.lastname: Fan
authors.forename: Jianjun
authors.initials: J
authors.lastname: Guo
authors.forename: Wei
authors.initials: W
authors.lastname: Zhou
authors.forename: Lingling
authors.initials: L
authors.lastname: Li
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002151:Calorimetry; D005456:Fluorescent Dyes / Q000737:chemistry / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D006023:Glycoproteins; C027132:1-anilino-8-naphthalenesulfonate; C028665:urinastatin