Journal
BIOCHIMIE
Volume 91, Issue 1, Pages 123-132Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2008.05.019
Keywords
Antimicrobial peptide; Bovine lactoferrin; Lactoferricin; Lactoferrampin; Lfchimera; DSC; CD
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Funding
- Dutch Digestive Foundation [WS 01-42]
- FCT
- [SFRH/BD/24055/2005]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/24055/2005] Funding Source: FCT
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The innate immunity factor lactoferrin harbours two antimicrobial moieties, lactoferricin and lactoferrampin, situated in close proximity in the NI domain of the molecule. Most likely they cooperate in many of the beneficial activities of lactoferrin. To investigate whether chimerization of both peptides forms a functional unit we designed a chimerical structure containing lactoferricin amino acids 17-30 and lactoferrampin amino acids 265-284. The bactericidal activity of this LFchimera was found to be drastically stronger than that of the constituent peptides, as was demonstrated by the need for lower dose, shorter incubation time and less ionic strength dependency. Likewise, strongly enhanced interaction with negatively charged model membranes was found for the LFchimera relative to the constituent peptides. Thus, chimerization of the two antimicrobial peptides resembling their structural orientation in the native molecule strikingly improves their biological activity. (C) 2008 Elsevier Masson SAS. All rights reserved.
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