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

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Jan G M Bolscher (Author) Other; Regina Adao (Author) Other; Kamran Nazmi (Author) Other; Petra A M van den Keybus (Author) Other; Wim van't Hof (Author) Other; Arie Nieuw N Amerongen (Author) Other; Margarida Bastos (Author) FCUP; Enno C I Veerman (Author) Other

Journal

Title: Biochimie

Vol. 91

Pages: 123-132

ISSN: 0300-9084

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 80 Citations

Scopus - 86 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-003-P8E

DOI: 10.1016/j.biochi.2008.05.019

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10