Lactoferricin

Lactoferricin
Lactoferricin
Identifiers
Symbol	N/A
OPM superfamily	203
OPM protein	1lfc

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.

Lactoferricin is the most studied AMP derived from milk protein. The complete sequence of lactoferricin corresponds to lactoferrin fragment 17-41 (FKCRRWQWRM KKLGAPSITCVRRAF; LFB0084) 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.^[3] In humans, lactoferricin corresponds to lactoferrin fragment 1-47 but consists of two subunits, namely fragments 1-11 and 12-47 (LFH0009), connected by a disulfide bridge.

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]

References[]

^ Wakabayashi H, Takase M, Tomita M (2003). "Lactoferricin derived from milk protein lactoferrin" (PDF). Current Pharmaceutical Design. 9 (16): 1277–1287. doi:10.1007/s13594-013-0153-2. PMID 12769736. S2CID 85279971.
^ Eliassen LT, Berge G, Sveinbjørnsson B, Svendsen JS, Vorland LH, Rekdal Ø (2002). "Evidence for a direct antitumor mechanism of action of bovine lactoferricin". Anticancer Research. 22 (5): 2703–10. PMID 12529985.
^ Théolier J, Fliss I, Jean J, Hammami R (2013). "MilkAMP: a comprehensive database of antimicrobial peptides of dairy origin" (PDF). Dairy Science & Technology. 94 (2): 181–193. doi:10.1007/s13594-013-0153-2. PMID 12769736. S2CID 85279971.
^ Gifford JL, Hunter HN, Vogel HJ (November 2005). "Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties". Cellular and Molecular Life Sciences. 62 (22): 2588–98. doi:10.1007/s00018-005-5373-z. PMID 16261252.
^ Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ (August 2005). "Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent". Antimicrobial Agents and Chemotherapy. 49 (8): 3387–95. doi:10.1128/AAC.49.8.3387-3395.2005. PMC 1196233. PMID 16048952.

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[pmid12769736-1] Wakabayashi H, Takase M, Tomita M (2003). "Lactoferricin derived from milk protein lactoferrin" (PDF). Current Pharmaceutical Design. 9 (16): 1277–1287. doi:10.1007/s13594-013-0153-2. PMID 12769736. S2CID 85279971.

[pmid12529985-2] Eliassen LT, Berge G, Sveinbjørnsson B, Svendsen JS, Vorland LH, Rekdal Ø (2002). "Evidence for a direct antitumor mechanism of action of bovine lactoferricin". Anticancer Research. 22 (5): 2703–10. PMID 12529985.

[3] Théolier J, Fliss I, Jean J, Hammami R (2013). "MilkAMP: a comprehensive database of antimicrobial peptides of dairy origin" (PDF). Dairy Science & Technology. 94 (2): 181–193. doi:10.1007/s13594-013-0153-2. PMID 12769736. S2CID 85279971.

[pmid16261252-4] Gifford JL, Hunter HN, Vogel HJ (November 2005). "Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties". Cellular and Molecular Life Sciences. 62 (22): 2588–98. doi:10.1007/s00018-005-5373-z. PMID 16261252.

[pmid16048952-5] Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ (August 2005). "Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent". Antimicrobial Agents and Chemotherapy. 49 (8): 3387–95. doi:10.1128/AAC.49.8.3387-3395.2005. PMC 1196233. PMID 16048952.

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