Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/7245
Título: Synergistic effects of the membrane actions of cecropin-melittin antimicrobial hybrid peptide BP100
Autor: Ferre, Rafael
Melo, Manuel N.
Correia, Ana D.
Feliu, Lidia
Bardají, Eduard
Planas, Marta
Castanho, Miguel
Data: 2009
Editora: Biophysical Society
Citação: Biophysical Journal Volume 96 March 2009 1815–1827
Resumo: BP100 (KKLFKKILKYL-NH2) is a short cecropin A-melittin hybrid peptide, obtained through a combinatorial chemistry approach, which is highly effective in inhibiting both the in vitro and in vivo growth of economically important plant pathogenic Gram-negatives. The intrinsic Tyr fluorescence of BP100 was taken advantage of to study the peptide’s binding affinity and damaging effect on phospholipid bilayers modeling the bacterial and mammalian cytoplasmic membranes. In vitro cytotoxic effects of this peptide were also studied on mammalian fibroblast cells. Results show a stronger selectivity of BP100 toward anionic bacterial membrane models as indicated by the high obtained partition constants, one order of magnitude greater than for the neutral mammalian membrane models. For the anionic systems, membrane saturation was observed at high peptide/lipid ratios and found to be related with BP100-induced vesicle permeabilization, membrane electroneutrality, and vesicle aggregation. Occurrence of BP100 translocation was unequivocally detected at both high and low peptide/lipid ratios using a novel and extremely simple method. Moreover, cytotoxicity against mammalian models was reached at a concentration considerably higher than the minimum inhibitory concentration. Our findings unravel the relationships among the closely coupled processes of charge neutralization, permeabilization, and translocation in the mechanism of action of antimicrobial peptides.
Descrição: © 2009 by the Biophysical Society
Peer review: yes
URI: http://dx.doi.org/10.1016/j.bpj.2008.11.053
http://hdl.handle.net/10451/7245
ISSN: 0006-3495
Aparece nas colecções:IMM - Artigos em Revistas Internacionais

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