Hirudin Hirudin Hirudin is a naturally occurring peptide in the salivary glands of blood-sucking leeches (such as "Hirudo medicinalis") that has a blood anticoagulant property. This is fundamental for the leeches’ alimentary habit of hematophagy, since it keeps the blood flowing after the initial phlebotomy performed by the worm on the host’s skin. During his years in Birmingham and Edinburgh, John Berry Haycraft had been actively engaged in research and published papers on the coagulation of blood, and in 1884, he discovered that the leech secreted a powerful anticoagulant, which he named hirudin, although it was not isolated until the 1950s,
Cell-penetrating peptide process by which peptide bonds are hydrolyzed to amino acids. Unnatural acid insertion in the peptide chain has multiple advantages. It facilitates the formation of stable foldamers with distinct secondary structure. β-Peptides are conformationally more stable in aqueous solution than naturally occurring peptides, especially for small chains. The secondary structure is reinforced by the presence of a rigid β-amino acid, which contains cyclohexane or cyclopentane fragments. These fragments generate a more rigid structure and influence the opening angle of the foldamer. These features are very important for new peptide design. Helical β-peptides mimic antimicrobial activities of host defense peptides. A