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.

Cite this paper

@article{Binnie1990InhibitionOT, title={Inhibition of thrombin by synthetic hirudin peptides.}, author={C G Binnie and Bruce W. Erickson and Jan Hermans}, journal={FEBS letters}, year={1990}, volume={270 1-2}, pages={85-9} }