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Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide–membrane interactions of three related antimicrobial peptides
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Orientador(es)
Resumo(s)
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 -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.
Descrição
© 2016 Elsevier B.V. All rights reserved.
Palavras-chave
CAMPs Hydrophobicity Membrane interaction
Contexto Educativo
Citação
Colloids and Surfaces B: Biointerfaces 141 (2016) 528–536
Editora
Elsevier