Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II.

  title={Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II.},
  author={Glen L. Hortin and Douglas M. Tollefsen and Barbara M. Benutto},
  journal={The Journal of biological chemistry},
  volume={264 24},
Comparison of Heparin- and Dermatan Sulfate-mediated Catalysis of Thrombin Inactivation by Heparin Cofactor II*
Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatAn sulfate stimulates HCII by producing more effective displacement of the amino terminus.
Role of thrombin exosites in inhibition by heparin cofactor II.
The complete N-terminal extension of heparin cofactor II is required for maximal effectiveness as a thrombin exosite 1 ligand
The results support a model in which thrombin first binds to GAGs, followed by HCII addition to the ternary complex and release of HCII 1-75 for exosite 1 binding and serpin mechanism inhibition.
Conformational stability of a thrombin-binding peptide derived from the hirudin C-terminus.
The thrombin-bound structure of the peptide fragment, hirudin 55-65, has been determined by use of transferred NOE spectroscopy and the apparent preference for a gauche- (chi 1 = +60) side-chain conformation of Ile(59) in the bound state may be explained by the existence of a positively charged arginine residue among the hydrophobic residues in theThrombin exosite.
Deciphering the structural elements of hirudin C-terminal peptide that bind to the fibrinogen recognition site of alpha-thrombin.
  • J. Chang
  • Biology, Chemistry
  • 1991
The anticoagulant activities of hirudin C-terminal peptides were quantitatively related to their abilities to shield the five identified lysines of thrombin.