title: Inhibition of thrombin by synthetic hirudin peptides.
abstract: To investigate the role of different regions of hirudin in the interaction with the proteinase thrombin, segments of hirudin containing 15-51 residues were synthesized. The C-terminal segment 40-65 inhibited the fibrinogen clotting activity of thrombin but not amidolysis of tosyl-Gly-Pro-Arg-p-nitroanilide. Central peptide 15-42 was insoluble at pH 7, but peptide 15-65 inhibited fibrinogen clotting and amidolysis to an equal extent. The N-terminal loop peptide 1-15 had no inhibitory activity and did not affect the potency of peptide 15-65. These data suggest that the central region inhibits catalysis.
authors.affiliation: Department of Biochemistry, University of North Carolina, Chapel Hill 27599.
authors.forename: C G
authors.initials: CG
authors.lastname: Binnie
authors.forename: B W
authors.initials: BW
authors.lastname: Erickson
authors.forename: J
authors.initials: J
authors.lastname: Hermans
mesh_terms: D000595:Amino Acid Sequence; D006629:Hirudins / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000037:antagonists & inhibitors*
chemical_list: D006629:Hirudins; D010446:Peptide Fragments; D013917:Thrombin