C-terminal peptide alcohol, acid and amide analogs of desulfato hirudin54-65 as antithrombin agents.

  title={C-terminal peptide alcohol, acid and amide analogs of desulfato hirudin54-65 as antithrombin agents.},
  author={John L Krstenansky and Marguerite H. Payne and Thomas J. Owen and Mark T. Yates and Simon J. T. Mao},
  journal={Thrombosis research},
  volume={54 4},
C-Terminus of the B-Chain of Relaxin-3 Is Important for Receptor Activity
It is reported here for the first time that amidation at the C-terminus of the B-chain of H3 relaxin leads to significant drop in the binding and activity of the peptide at RXFP3/RXFP4 receptors.
Hirudin was originally isolated from the salivary glands of the medicinal leech Hirudo medicinalis and all of these forms seem to have antithrombin activity and the disulfide bridges and the acidic nature of the molecule, including the sulfated tyrosine, are invariant.
A Comparison of the Effects of Amide and Acid Groups at the C-Terminus on the Collision-Induced Dissociation of Deprotonated Peptides
The end group specific fragmentation of peptide amides in the negative ion mode may be useful for identifying such groups in proteomic applications.
Methods and Approaches for the Solid-Phase Synthesis of Peptide Alcohols.
The use of the chlorotrityl resin, one of the most common linkers used to obtain peptide alcohols, is discussed and the recently developed resins with the Rink, Ramage and Sieber handles are outlined.
Evaluating prodrug characteristics of a novel anticoagulant fusion protein neorudin, a prodrug targeting release of hirudin variant 2‐Lys47 at the thrombosis site, by means of in vitro pharmacokinetics
  • Xiaona Dong, Ruo-lan Gu, G. Dou
  • Biology, Medicine
    European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
  • 2018


N-terminal requirements of small peptide anticoagulants based on hirudin54-65.
The sensitivity of position 56 to modification demonstrates the significance of this residue in the interaction between the C-terminal region of hirudin and thrombin.
Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin.
A "kinked" amphipathic alpha-helical structure, which orients all of the residues most critical for activity on one face of the helix, is proposed for anticoagulant activity in hirudin.
Interaction of hirudin with thrombin: identification of a minimal binding domain of hirudin that inhibits clotting activity.
It is shown that the carboxyl-terminal 10 amino acid residues 56-65 are minimally required for binding to thrombin and inhibition of clotting and associated with a significant conformational change of Thrombin as judged by circular dichroism.