| 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 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]
References
- ^ a b 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): 2703–2710. PMID 12529985.
- ^ Bruni N, Capucchio MT, Biasibetti E, Pessione E, Cirrincione S, Giraudo L, et al. (June 2016). "Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine". Molecules. 21 (6): 752. doi: 10.3390/molecules21060752. PMC 6273662. PMID 27294909.
- ^ 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): 2588–2598. doi: 10.1007/s00018-005-5373-z. PMC 11139180. 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): 3387–3395. doi: 10.1128/AAC.49.8.3387-3395.2005. PMC 1196233. PMID 16048952.
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |
| 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 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]
References
- ^ a b 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): 2703–2710. PMID 12529985.
- ^ Bruni N, Capucchio MT, Biasibetti E, Pessione E, Cirrincione S, Giraudo L, et al. (June 2016). "Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine". Molecules. 21 (6): 752. doi: 10.3390/molecules21060752. PMC 6273662. PMID 27294909.
- ^ 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): 2588–2598. doi: 10.1007/s00018-005-5373-z. PMC 11139180. 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): 3387–3395. doi: 10.1128/AAC.49.8.3387-3395.2005. PMC 1196233. PMID 16048952.
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| This biochemistry article is a stub. You can help Wikipedia by expanding it. |