title: [Interaction of human alpha-thrombin with organic ligands of ionic nature].
abstract: Investigations results of human thrombin interaction with organic ligands of ion nature containing nonpolar groups are presented. It is shown that electrostatic interaction is the basic one under enzyme binding, while hydrophobic binding is only additional function in the reaction enzyme-ligand, this fact is confirmed by the absence of interaction between thrombin and rivanol which has a positive charge side by side with cumbrous hydrophobic group. New data are presented about the ligand specificity of binding sites of thrombin active centre. The importance of relative arrangement of hydrophobic ligand groups for interaction with enzyme is shown. It is supposed that thrombin binding with organic ligands occurs owing anionic site of beta-domain of active thrombin centre with the major aminoacids arginine and lysine (Lys 68, Arg 78, Arg 77, Arg 66 etc.). It is shown that the compounds containing negative group SO3 and have some cunbours hydrophobic groups interact more intensively with the enzyme. Thus, rosseline--with symmetrical hydrophobic nucleus (four benzene rings)--is the most efficient ligand for the binding with thrombin. The obtained investigation results evidence for bacteriostatical and stabilizing effect of low-molecular asobenzene ligands on rather labile thrombin molecules.
authors.affiliation: Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv.
authors.forename: M V
authors.initials: MV
authors.lastname: Kolodzeĭskaia
authors.forename: Iu V
authors.initials: IuV
authors.lastname: Chumachenko
authors.forename: G L
authors.initials: GL
authors.lastname: Volkov
mesh_terms: D001665:Binding Sites; D006801:Humans; D007477:Ions / Q000737:chemistry*; D008024:Ligands; D008970:Molecular Weight; D009930:Organic Chemicals / Q000737:chemistry*; D055672:Static Electricity; D013917:Thrombin / Q000737:chemistry*
chemical_list: D007477:Ions; D008024:Ligands; D009930:Organic Chemicals; D013917:Thrombin