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- W1489969108 abstract "Two lactoferrampin (LFampin) peptides derived from bovine lactoferrin were compared with respect to their bactericidal activities. LFampin 265–284 killed a set of Gram-positive bacteria that were resistant to LFampin 268–284. The presence of 265 Asp-Leu- 267 Ile did not simply lead to an overall increased potency, since higher concentrations of LFampin 265–284 than LFampin 268–284 were needed to kill the Gram-negative bacteria that were tested. The Asp-Leu-Ile sequence enhances the propensity of LFampin to adopt an α-helix, as shown by circular dichroism spectroscopy. These results suggest that the helical conformation of the peptide is an important determinant of the susceptibility of Gram-positive bacteria." @default.
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- W1489969108 date "2006-06-01" @default.
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- W1489969108 title "Distinct bactericidal activities of bovine lactoferrin peptides LFampin 268–284 and LFampin 265–284: Asp-Leu-Ile makes a differenceThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal's usual peer review process." @default.
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- W1489969108 doi "https://doi.org/10.1139/o06-042" @default.
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