Ultrapotent thrombin inhibitor combines peptide fragments from a trio of blood-sucking organisms

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Source: © Richard James Payne/The University of Sydney

Hybrid molecule featuring leech, tsetse fly and flea peptide fragments binds thrombin at three sites

Salivary peptide fragments from a leech, a tsetse fly and a rat flea have been combined to create a synthetic protein that clamps onto thrombin, the key enzyme in blood clotting, with remarkable strength. Developed by Richard Payne and Joshua Maxwell at the University of Sydney, Australia, and colleagues, they believe their hybrid molecule could inspire alternative design strategies for new anticoagulants.