Journal
COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 141, Issue -, Pages 528-536Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfb.2016.02.003
Keywords
CAMPs; Hydrophobicity; Membrane interaction
Funding
- Universidad Nacional de Quilmes
- Comision de Investigaciones Cientificas de la Provincia de Buenos Aires (CIC-BA)
- Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT-MINCyT), Argentina [PICT 2013-1481, PICT 2013-815]
- Fundacao para a Ciencia e a Tecnologia - Ministerio da Ciencia, Tecnologia e Ensino Superior (FCT-MCTES, Portugal)
- CONICET
- Fundacao para a Ciencia e Tecnologia-Ministerio da Educacao e Ciencia (FCT-MEC, Portugal) [SFRH/BD/95624/2013]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/95624/2013] Funding Source: FCT
Ask authors/readers for more resources
Cationic antimicrobial peptides (CAMPs) represent important self defense molecules in many organisms, including humans. These peptides have a broad spectrum of activities, killing or neutralizing many Gram-negative and Gram-positive bacteria. The emergence of multidrug resistant microbes has stimulated research on the development of alternative antibiotics. In the search for new antibiotics, cationic antimicrobial peptides (CAMPs) offer a viable alternative to conventional antibiotics, as they physically disrupt the bacterial membranes, leading to lysis of microbial membranes and eventually cell death. In particular, the group of linear a-helical cationic peptides has attracted increasing interest from clinical as well as basic research during the last decade. In this work, we studied the biophysical and microbiological characteristics of three new designed CAMPs. We modified a previously studied CAMP sequence, in order to increase or diminish the hydrophobic face, changing the position of two lysines or replacing three leucines, respectively. These mutations modified the hydrophobic moment of the resulting peptides and allowed us to study the importance of this parameter in the membrane interactions of the peptides. The structural properties of the peptides were also correlated with their membrane-disruptive abilities, antimicrobial activities and hemolysis of human red blood cells. (C) 2016 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available