Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides

J.G.M. Bolscher, R. Adão, K. Nazmi, P.A.M. van den Keijbus, W. van 't Hof, A. van Nieuw Amerongen, M. Bastos, E.C.I. Veerman

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    Abstract

    The innate immunity factor lactoferrin harbours two antimicrobial moieties, lactoferricin and lactoferrampin, situated in close proximity in the N1 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.
    Original languageUndefined/Unknown
    Pages (from-to)123-132
    JournalBiochimie
    Volume91
    Issue number1
    DOIs
    Publication statusPublished - 2009

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