Abstract

Bovine lactoferricin is an antimicrobial, cationic peptide generated upon gastric pepsin cleavage of bovine lactoferrin. We investigated the bactericidal effects of native lactoferricin [Lfcin B(17-41)], a shortened derivative [Lfcin B(17-31)] and the all-D-amino acid counterpart of Lfcin B(17-31) against Escherichia coli and Staphylococcus aureus. The results revealed different activities for the peptides against Gram-positive and -negative bacteria. D-Lfcin B(17-31) was the most efficient peptide against E. coli. The same peptide showed improved activity against S. aureus, D-Lfcin B(17-31) showed a significant better efficacy when compared to the L-form, but not when compared to Lfcin B(17-41). There was no correlation between the bactericidal concentrations and the time needed to achieve maximum effect. This indicates the importance of structural differences between the peptides and/or bacteria and implies that the simple thesis of I antibacterial target is not valid for lactoferricin.

Keywords

LactoferrinEscherichia coliStaphylococcus aureusAntimicrobialMicrobiologyPeptideAntibacterial activityBiologyAntibacterial agentBacteriaAntibioticsBiochemistry

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Publication Info

Year
2001
Type
article
Volume
33
Issue
7
Pages
507-511
Citations
47
Access
Closed

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Hilde Ulvatne, Lars H. Vorland (2001). Bactericidal Kinetics of 3 Lactoferricins Against Staphylococcus aureus and Escherichia coli. Scandinavian Journal of Infectious Diseases , 33 (7) , 507-511. https://doi.org/10.1080/00365540110026692

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DOI
10.1080/00365540110026692