American Society of Hirudotherapy

Identification and characterization of novel anticoagulant peptide with thrombolytic effect and nutrient oligopeptides from Whitmania pigra

Peptidomics study published in Amino Acids (2016)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Research reportGenomics & ProteomicsSalivary PharmacologyRen Y et al. · Amino acids, 2016

Abstract

Natural and nutrient substances for cardiovascular disease are promising and capture researchers' minds. Two kinds of novel bioactive peptides (high Fischer's ratio oligopeptides and anticoagulant peptides) were obtained from Whitmania pigra protein via enzymatic hydrolysis. An oligopeptide (MW<874.0 Da) named as HF2 was obtained via chromatography purification procedures with a high Fischer's ratio of 31.92 ± 1.36 and low phenylalanine + tyrosine content of 0.98 ± 0.04 %. Another peptide (WA3-1), prepared by alcalase AF 2.4 L-catalyzed hydrolysis and then purified by DEAE Sepharose FF, gel Sephadex G-15 chromatography, exhibited high anticoagulant activity with prolonging significantly plasma clotting time on activated partial thromboplastin time, prothrombin time, thrombin time (p < 0.01) and powerful thrombolytic activity. Amino acid composition and MALDI-TOF/TOF MS analysis showed that WA3-1 contained 11 amino acids (MW: 1422.0 Da) with the sequence as NH2-His-Asp-Phe-Leu-Asn-Asn-Lys-Leu-Glu-Tyr-Glu-COOH. Abundant negatively charged amino acids in C-terminal, as well as the special residue Lys contribute to its anticoagulant capacity. This research provided a novel natural candidate for the manufacture of nutrient oligopeptides with high branched chain amino acid, and anticoagulant thrombolytic agent in pharmaceutical industry with helping prevent from thrombosis and related cardiovascular diseases.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleResearch Support, Non-U.S. Gov't
Indexed MeSH termsAmino Acid SequenceAmino Acids, Branched-ChainAnimalsAnticoagulantsBlood CoagulationHumansLeechesOligopeptidesThrombolytic Therapy

Summary

Discovers a novel anticoagulant peptide with thrombolytic activity and nutrient oligopeptides rich in branched-chain amino acids in Whitmania pigra hydrolysates.

Why This Matters for Hirudotherapy

This study isolated and characterized two novel bioactive peptides from Whitmania pigra protein via enzymatic hydrolysis and chromatographic purification: a high Fischer's ratio oligopeptide (HF2, MW < 874.0 Da, Fischer's ratio 31.92 ± 1.36) and an anticoagulant peptide (WA3-1, MW 1422.0 Da, sequence NH2-His-Asp-Phe-Leu-Asn-Asn-Lys-Leu-Glu-Tyr-Glu-COOH). WA3-1 significantly prolonged activated partial thromboplastin time, prothrombin time, and thrombin time (p < 0.01) and exhibited thrombolytic activity, with negatively charged C-terminal amino acids and a Lys residue contributing to its anticoagulant capacity. This is relevant to ASH's domain as it characterizes novel anticoagulant and thrombolytic peptides from a leech species (per MeSH classification), identifying potential bioactive components of medicinal interest. However, all activity data are from in vitro plasma clotting assays and compositional analysis; no in vivo efficacy, pharmacokinetic, or safety data are presented.

Citation

Identification and characterization of novel anticoagulant peptide with thrombolytic effect and nutrient oligopeptides from Whitmania pigra.

Ren Y et al. · Amino acids, 2016

DOI

Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026

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