Effect of O-glycosylation and tyrosine sulfation of leech-derived peptides on binding and inhibitory activity against thrombin
Research article published in Chemical communications (2011)
Abstract
Synthesis of sulfated and unsulfated (glyco)peptide fragments of Hirudin P6 (a potent anticoagulant from the leech Hirudinaria manillensis) is described. The effect of O-glycosylation and tyrosine sulfation on thrombin binding and peptidolytic activity was investigated, together with the inhibition of fibrinogen cleavage.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
Effect of O-glycosylation and tyrosine sulfation of leech-derived peptides on binding and inhibitory activity against thrombin.
Por qué esto importa para la hirudoterapia
This study describes the synthesis of sulfated and unsulfated (glyco)peptide fragments of Hirudin P6—a potent anticoagulant identified from the leech Hirudinaria manillensis—and investigates how O-glycosylation and tyrosine sulfation affect thrombin binding, peptidolytic activity, and inhibition of fibrinogen cleavage. Because Hirudin P6 is a leech-derived peptide, characterizing these structural modifications helps clarify how specific chemical features influence its interaction with thrombin. The work is limited to isolated, chemically synthesized peptide fragments studied in vitro; it does not evaluate whole leeches, live hirudotherapy, or any clinical outcome.
Citación
Effect of O-glycosylation and tyrosine sulfation of leech-derived peptides on binding and inhibitory activity against thrombin
Hsieh YS et al. · Chemical communications, 2011
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026