American Society of Hirudotherapy

Identification and characterization of novel anticoagulant peptide with thrombolytic effect and nutrient oligopeptides with high branched chain amino acid from Whitmania pigra protein

Bioactive peptide study published in Amino Acids (2016)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Research reportDrug DevelopmentSalivary 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

WA3-1 anticoagulant peptide (NH-HDFLNNKLEYE-COOH, 1422 Da) from Whitmania pigra protein significantly prolongs APTT/PT/TT and shows powerful thrombolytic activity; HF2 oligopeptide (<874 Da) has high Fischer's ratio (31.92) and low phenylalanine+tyrosine content (0.98%) for nutrient applications.

Why This Matters for Hirudotherapy

This study isolated two novel bioactive peptides from Whitmania pigra protein via enzymatic hydrolysis: HF2, a high Fischer's ratio oligopeptide (MW <874.0 Da, Fischer's ratio ~31.92), and WA3-1, an 11-amino-acid anticoagulant peptide (MW 1422.0 Da, sequence NH2-His-Asp-Phe-Leu-Asn-Asn-Lys-Leu-Glu-Tyr-Glu-COOH) that significantly prolonged APTT, PT, and TT and showed thrombolytic activity. The authors propose that negatively charged C-terminal residues and a Lys residue contribute to anticoagulant capacity. For ASH, this identifies new leech-derived peptide candidates relevant to anticoagulant and thrombolytic drug development. Honest caveat: the work is biochemical/in vitro in nature, with no animal or human efficacy data presented, and the relevance is to pharmaceutical candidates rather than live leech therapy.

Citation

Identification and characterization of novel anticoagulant peptide with thrombolytic effect and nutrient oligopeptides with high branched chain amino acid from Whitmania pigra protein.

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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