Desirudin is a synthetic recombinant form of the naturally occurring hirudin, the anticoagulant substance found in leech. Desirudin is a selective and almost irreversible inhibitor of thrombin, both free and clot-bound, by blocking its active site. This anticoagulant agent has no effect on other components of the hemostatic system. Desirudin is particularly used to prevent deep vein thrombosis in patients undergoing hip and knee replacement surgery.
CAT No: 10-101-340
CAS No:120993-53-5
Synonyms/Alias:Desirudin;120993-53-5;CGP 39393;CGP-39393;IK-HIR02;Revasc;UNII-U0JZ726775;63-Desulfohirudin (Hirudo medicinalis isoform HV1);DTXSID90153094;CGP39393;U0JZ726775;recombinant HV1 hirudin;Desirudin [USAN:INN:BAN];Hirudin desirudin;63-Desulfohirudin;DESIRUDIN (MART.);GTPL6458;DTXCID9075585;Hirudin (Hirudo medicinalis isoform HV1), 63-desulfo-;63-Desulfohirudin (recombinant);B01AE01;DA-52459;63-Desulfohirudin(Hirudo medicinalis isoform HV1);
Chemical Name:(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-1-[(2S,3R)-2-[[2-[[(2S)-2-[[2-[[(2S,3R)-2-[[(2S)-2-[[(1R,6R,9S,12S,15S,18S,24S,27S,33S,36S,39R,44R,47S,53S,56S,59S,67S,73S,76S)-15,76-bis(4-aminobutyl)-44-[[(2S)-2-[[(4R,7S,10S,13S,19S,22S,25S,28R)-28-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]-3-carboxypropanoyl]amino]-10-(2-amino-2-oxoethyl)-13-(3-amino-3-oxopropyl)-22-(2-carboxyethyl)-25-[(1R)-1-hydroxyethyl]-19-(hydroxymethyl)-7-(2-methylpropyl)-6,9,12,15,18,21,24,27-octaoxo-1,2-dithia-5,8,11,14,17,20,23,26-octazacyclononacosane-4-carbonyl]amino]-4-methylpentanoyl]amino]-12,56,73-tris(2-amino-2-oxoethyl)-9,67-bis(3-amino-3-oxopropyl)-36-[(2S)-butan-2-yl]-18,47-bis(2-carboxyethyl)-24-(carboxymethyl)-27,53-bis(hydroxymethyl)-33-(2-methylpropyl)-8,11,14,17,20,23,26,29,32,35,38,45,48,51,54,57,60,62,65,68,71,74,77-tricosaoxo-59-propan-2-yl-3,4,41,42-tetrathia-7,10,13,16,19,22,25,28,31,34,37,46,49,52,55,58,61,63,66,69,72,75,78-tricosazabicyclo[37.22.17]octaheptacontane-6-carbonyl]amino]-3-methylbutanoyl]amino]-3-hydroxybutanoyl]amino]acetyl]amino]-4-carboxybutanoyl]amino]acetyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-oxobutanoyl]amino]-3-carboxypropanoyl]amino]acetyl]amino]-3-carboxypropanoyl]amino]-3-phenylpropanoyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoic acid
Desirudin is a recombinant peptide belonging to the hirudin family, recognized as a potent and highly specific direct thrombin inhibitor. Structurally derived from the naturally occurring anticoagulant found in leech saliva, this peptide is engineered to interact with thrombin, a key serine protease in the coagulation cascade. Its unique ability to bind both the active site and exosite I of thrombin distinguishes it from other anticoagulants, making it an invaluable tool for researchers investigating coagulation mechanisms, thrombosis, and related biochemical pathways. The molecular precision of desirudin has established it as a reference compound in studies seeking to elucidate thrombin's physiological and pathological roles.
Coagulation Pathway Research: Desirudin is extensively utilized in the exploration of the coagulation cascade, particularly in dissecting the specific interactions and regulatory mechanisms of thrombin. By providing a highly selective means of inhibiting thrombin activity, it allows researchers to study downstream effects on fibrin formation, platelet activation, and clot stabilization. This application is crucial for understanding the molecular basis of hemostasis and for identifying novel therapeutic targets involved in thrombotic disorders.
Antithrombotic Mechanism Studies: As a direct thrombin inhibitor, desirudin serves as a model compound for examining antithrombotic strategies at the biochemical level. Its use enables detailed investigation into the inhibition of thrombin-mediated processes, such as the conversion of fibrinogen to fibrin and the activation of various coagulation cofactors. Researchers leverage this peptide to differentiate between direct and indirect anticoagulant effects, facilitating the development of next-generation anticoagulant agents and refining mechanistic models of thrombosis.
Peptide-Protein Interaction Analysis: The specificity of desirudin for thrombin's active and exosite regions makes it a valuable probe in peptide-protein interaction studies. By employing this inhibitor in binding assays, surface plasmon resonance experiments, or crystallographic analyses, scientists can map interaction sites, characterize binding affinities, and investigate allosteric regulation within the thrombin molecule. These insights contribute to a deeper understanding of protein conformational dynamics and inform rational drug design efforts targeting serine proteases.
In Vitro Assay Development: The inclusion of desirudin in in vitro assay systems is instrumental for validating thrombin-dependent processes and screening potential anticoagulant compounds. Its well-characterized inhibitory profile allows for the calibration of chromogenic, fluorogenic, or clot-based assays designed to measure thrombin activity. This application supports the standardization of research protocols, enhances assay reproducibility, and provides a benchmark for evaluating the potency and selectivity of new inhibitors.
Structural and Biophysical Characterization: Desirudin's defined sequence and stable inhibitory properties facilitate its use in structural biology and biophysical research. Crystallographic and NMR studies employing this peptide have elucidated the structural basis of thrombin inhibition, revealing key molecular interactions and conformational changes. Such investigations advance the fundamental understanding of serine protease inhibition, guide the design of novel peptide-based inhibitors, and expand the toolkit available for probing coagulation-related enzymes in diverse experimental settings.
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