Journal
BIOCHEMISTRY AND CELL BIOLOGY
Volume 84, Issue 3, Pages 358-362Publisher
CANADIAN SCIENCE PUBLISHING, NRC RESEARCH PRESS
DOI: 10.1139/O06-042
Keywords
alpha-helix; antimicrobial peptides; Gram-negative bacteria; Gram-positive bacteria; lactoferrampin; lactoferrin
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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-IIe sequence enhances the propensity of LFampin to adopt an alpha-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.
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