[Research progress in hirudin fusion protein--review]
Review article published in Zhongguo shi yan xue ye xue za zhi (2007)
Abstract
Natural hirudin extracted from the secretion of medical leech salivary gland is a single-chain peptide containing 65 aminoacid residues with molecular weight of 7000 D, and exists in three isomers of HV1, HV2 and HV3. Hirudin possesses three disulfide bridges forming the structure of core cyclic peptides, which binds to the catalytic site of thrombin so as to inhibit the catalysis of thrombin. Its c-terminus rich in acidic aminoacid residues possesses hydrophilicity, and is free on the molecular surface, and can bind with fibrin recognition site of hirudin. The minimal segment of 12 - 16 C-terminal acidic residues keeps the minimal activity of anti-thrombosis. Thus, hirudin, as a potent and specific inhibitor of thrombin, can be used to protect from and to treat clinically thrombosis. As it has some disadvantages such as short half-life, bleeding side-effect and mono-function, and so on, hirudin has been fused with some other functional proteins in recent years. The obtained fusion proteins can prolong the half life of hirudin, or relieve it bleeding side effect, or bring new functions, such as thrombolysis, inhibiting the platelet aggregation, targeting specifically. The research progress in hirudin fusion protein was summarized in this review.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
Natural hirudin extracted from the secretion of medical leech salivary gland is a single-chain peptide containing 65 aminoacid residues with molecular weight of 7000 D, and exists in three isomers of HV1, HV2 and HV3.
Why This Matters for Hirudotherapy
This review summarizes work on hirudin, the leech salivary-gland anticoagulant described here as a 65-residue, ~7000 D peptide (isoforms HV1-HV3) that directly inhibits thrombin, and surveys efforts to fuse it with other functional proteins to extend its short half-life, reduce bleeding side effects, or add functions such as thrombolysis, platelet-aggregation inhibition, and specific targeting. For ASH it directly illustrates the medicinal-leech-secretome drug-discovery story: a single natural leech molecule has seeded a family of engineered anticoagulant therapeutics. The caveat is that this is a narrative review of others' research and an account of engineered fusion proteins rather than whole-leech therapy, so it reports design rationale and progress, not pooled clinical outcomes.
Citation
[Research progress in hirudin fusion protein--review].
Zhang C et al. · Zhongguo shi yan xue ye xue za zhi, 2007
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