Antimicrobial Peptides 2013
DOI: 10.1002/9783527652853.ch2
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Cationic Antimicrobial Peptides

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Cited by 8 publications
(2 citation statements)
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“…As to why these AHDPs possess the capacity for anticancer activity is unclear as, self-evidently, this capacity has no relevance to plant survival [85]. However, it has been suggested that this anticancer activity may result from the general ability of these peptides to interact with membranes [86], which appears to have evolved to kill microorganisms in line with the role of most HDPs as endogenous antimicrobials [39]. This review has shown that the anticancer actions used by plant AHPDs are based on membrane interaction, which at least in some cases, appears to involve the use of PE as a lipid receptor (Fig.…”
Section: Discussionmentioning
confidence: 99%
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“…As to why these AHDPs possess the capacity for anticancer activity is unclear as, self-evidently, this capacity has no relevance to plant survival [85]. However, it has been suggested that this anticancer activity may result from the general ability of these peptides to interact with membranes [86], which appears to have evolved to kill microorganisms in line with the role of most HDPs as endogenous antimicrobials [39]. This review has shown that the anticancer actions used by plant AHPDs are based on membrane interaction, which at least in some cases, appears to involve the use of PE as a lipid receptor (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…In this conformation, Cn-AMP2 exhibited a strongly hydrophobic region, formed by the C-terminal eight residues of the peptide, YFVFSVGM, which was flanked by a short anionic segment, TES [36,37]. This residue arrangement endows Cn-AMP2 with primary amphiphilicity [36,37], which has been reported for other anticancer peptides such as indolicidin [38,39] and is known to mediate the ability of these peptides to traverse membranes [40]. By analogy to indolicidin, it was suggested that the ability of Cn-AMP2 to traverse cancer cell membranes may be hydrophobicity driven by a mechanism involving the peptide's C-terminal region [36,37].…”
Section: Please Provide Corresponding Author(s) Photograph Size Shoulmentioning
confidence: 99%