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Lactoferricin

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Lactoferricin is an amphipathic, cationic peptide with anti-microbial[1] and anti-cancer[2] properties. It can be generated by the pepsin-mediated digestion of lactoferrin.

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Lactoferricin is the most studied AMP derived from milk protein. The complete sequence of lactoferricin corresponds to lactoferrin fragment 17-41 (FKCRRWQWRM KKLGAPSITCVRRAF; LFB0084 Archived 2018-11-03 at the Wayback Machine) and sequences from within this fragment are also antimicrobial. The MilkAMP database contains a total of 111 peptides (natural, synthetic and modified) comprising or derived from the complete lactoferricin.[1] In humans, lactoferricin corresponds to lactoferrin fragment 1-47 but consists of two subunits, namely fragments 1-11 and 12-47 (LFH0009 Archived 2017-01-13 at the Wayback Machine), connected by a disulfide bridge.[3]

Human Lactoferricin and Bovine Lactoferricin are two greatly studied forms of Lactoferricin. These two forms have great sequence differences. Bovine Lactoferricin contains 25 residues, while Human Lactoferricin contains 49 residues.[4] Also, when placed in solution Bovine Lactoferricin forms a β-pleated sheet, while Human Lactoferricin forms a coiled structure.[5]

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