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Inhibition of thrombin by synthetic hirudin peptides
Author(s) -
Binnie Cameron G.,
Erickson Bruce W.,
Hermans Jan
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81240-o
Subject(s) - hirudin , thrombin , peptide , chemistry , fibrinogen , potency , biochemistry , discovery and development of direct thrombin inhibitors , in vitro , biology , platelet , immunology
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.