Lepirudin is a recombinant hirudin derived from yeast cells. It is almost identical to hirudin extracted from Hirudo medicinalis. Lepirudin is a highly specific direct inhibitor of thrombin.
CAT No: 10-101-90
CAS No:138068-37-8 (net)
Synonyms/Alias:(Leu1,Thr2)-Hirudin (desulfated); Lepirudin; Refludan; Refludin; Hbw 023; Hbw-023; Hbw023
Lepirudin is a recombinant hirudin peptide and a potent, highly specific inhibitor of thrombin, derived from the medicinal leech Hirudo medicinalis. As a synthetic polypeptide composed of 65 amino acids, it mimics the natural anticoagulant properties of hirudin, effectively binding to both the active site and exosite 1 of thrombin. The unique structure and targeted mechanism of action make Lepirudin a valuable tool in the study of coagulation pathways, enzyme inhibition, and the broader field of hemostasis research. Its well-characterized biochemical profile has established Lepirudin as a reference compound for investigating thrombin-related processes and for the development of novel anticoagulant strategies in laboratory settings.
Coagulation pathway research: Lepirudin serves as a gold standard for dissecting the molecular mechanisms of blood coagulation. By providing a direct, non-heparin-based means of inhibiting thrombin, it enables researchers to selectively block thrombin activity and examine downstream effects on fibrin formation, platelet aggregation, and clot stabilization. This selective inhibition is critical for elucidating the complex interactions within the coagulation cascade and for modeling disorders associated with dysregulated thrombin generation.
Enzyme inhibition studies: The compound's high specificity for thrombin makes it an indispensable reagent for in vitro enzyme kinetics and inhibition assays. Researchers utilize Lepirudin to characterize the binding dynamics, substrate specificity, and catalytic properties of thrombin and related serine proteases. Its use facilitates the validation of novel assay platforms, the screening of potential thrombin inhibitors, and the quantitative comparison of anticoagulant potencies in biochemical and pharmacological research.
Protein-protein interaction analysis: Lepirudin is widely employed to probe the structural and functional aspects of thrombin's interactions with substrates and cofactors. By occupying both the catalytic and exosite regions of thrombin, it provides a mechanistic model for studying allosteric modulation and the conformational changes induced upon inhibitor binding. These insights are essential for the rational design of next-generation anticoagulants and for understanding the molecular determinants of thrombin specificity.
Analytical method development: The compound is frequently used as a reference inhibitor in the development, calibration, and validation of thrombin activity assays, including chromogenic, fluorogenic, and clot-based formats. Its well-defined inhibitory profile supports the establishment of assay sensitivity, dynamic range, and specificity, ensuring reproducibility and accuracy in quantitative coagulation studies. Analytical laboratories benefit from the inclusion of Lepirudin as a control or standard in the assessment of thrombin function in complex biological matrices.
Structural biology and drug discovery: Lepirudin's defined sequence and binding characteristics make it a model ligand in structural studies of thrombin and related enzymes. Crystallographic and spectroscopic investigations leveraging Lepirudin have elucidated key aspects of enzyme-inhibitor recognition, guiding structure-based drug design efforts. Its application extends to the evaluation of molecular interactions in silico and in vitro, supporting the identification and optimization of novel anticoagulant candidates for preclinical research.
Through these multifaceted applications, Lepirudin continues to play an instrumental role in advancing the understanding of thrombin biology, refining analytical methodologies, and supporting the discovery of innovative anticoagulant agents in research environments.
Lepirudin is indicated for anticoagulation in patients with heparin-induced thrombocytopenia (HIT). We describe 2 cases of HIT and thrombosis in children with heart disease, including one that required extracorporeal membrane oxygenation. Lepirudin, dosed in the recommended adult weight--based fashion, was an effective antithrombotic agent in pediatric patients with HIT.
Deitcher, S. R., Topoulos, A. P., Bartholomew, J. R., & Kichuk-Chrisant, M. R. (2002). Lepirudin anticoagulation for heparin-induced thrombocytopenia. The Journal of pediatrics, 140(2), 264-266.
Lepirudin is one of few anticoagulants that can be safely used in patients with HIT. Because it is eliminated through the kidneys, great care must be taken when administering lepirudin to patients with renal failure; in fact, its use is currently not recommended in patients requiring hemodialysis. Lepirudin effectively prevented acute thrombosis in both of our patients with documented HIT, with no bleeding complications. We describe how we selected the initial doses and report results of aPTT monitoring.
Dager, W. E., & White, R. H. (2001). Use of lepirudin in patients with heparin-induced thrombocytopenia and renal failure requiring hemodialysis. Annals of Pharmacotherapy, 35(7-8), 885-890.
Lepirudin (Refludan), Berlex Laboratories, USA and Canada; Pharmion, all other countries), a recombinant derivative of the naturally occurring leech anticoagulant hirudin, was the first direct thrombin inhibitor to be approved by the European Agency for the Evaluation of Medicinal Products and the US Food and Drug Administration for the treatment of heparin-induced thrombocytopenia. Since its introduction into Europe and the USA, it has been studied in over 7000 patients requiring anticoagulation in conditions including acute coronary syndromes, percutaneous coronary intervention, cardiopulmonary bypass and heparin-induced thrombocytopenia. Three European clinical trials, designated Heparin-Associated Thrombocytopenia (HAT)-1, -2 and -3, demonstrated the efficacy and safety of lepirudin in the prevention and treatment of thrombosis in patients with antibody-confirmed heparin-induced thrombocytopenia.
Greinacher, A. (2004). Lepirudin: a bivalent direct thrombin inhibitor for anticoagulation therapy. Expert review of cardiovascular therapy, 2(3), 339-357.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More