2004
DOI: 10.1016/j.peptides.2003.12.006
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Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin

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Cited by 224 publications
(150 citation statements)
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“…Following the initial discovery of LFampin 268-284 (produced by solid-phase chemistry), a slightly longer sequence (produced by action of a single endopeptidase on bLf) was published that included an additional N-terminal helix cap region, Asp-Leu-Ile. It was found that the longer peptide LFampin 265-284 had higher activity [123]. For both peptides, the helical conformation was found to be critical for effectiveness against Gram-positive bacteria [124].…”
Section: Lf Derived Peptides: Lactoferrampinmentioning
confidence: 99%
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“…Following the initial discovery of LFampin 268-284 (produced by solid-phase chemistry), a slightly longer sequence (produced by action of a single endopeptidase on bLf) was published that included an additional N-terminal helix cap region, Asp-Leu-Ile. It was found that the longer peptide LFampin 265-284 had higher activity [123]. For both peptides, the helical conformation was found to be critical for effectiveness against Gram-positive bacteria [124].…”
Section: Lf Derived Peptides: Lactoferrampinmentioning
confidence: 99%
“…The sequence comparison of Lfampin from six different species shows a uniform preponderance of cationic amino acid residues among hydrophobic residues ( Table 5). As an antimicrobial peptide Lfampin plays a key role in membrane-mediated activities of Lf [123]. Following the initial discovery of LFampin 268-284 (produced by solid-phase chemistry), a slightly longer sequence (produced by action of a single endopeptidase on bLf) was published that included an additional N-terminal helix cap region, Asp-Leu-Ile.…”
Section: Lf Derived Peptides: Lactoferrampinmentioning
confidence: 99%
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“…The polar/nonpolar character of lactoferricin makes its structure similar to cationic peptides which exert their antimicrobial activities through membrane disruption [122]. Another bactericidal N-terminal fragment of bovine Lf has recently been described [193]. It can be hypothesized that bioactive fragments of Lf are generated in milk during infection by proteases in milk.…”
Section: Humoral Defensesmentioning
confidence: 99%
“…LPS makes these bacteria susceptible to phagocytosis by cells of immune system. There are various other mechanisms purposed for its action [11][12][13][14][15] (Table 2). …”
Section: Mechanism Of Actionmentioning
confidence: 99%