نتایج جستجو برای: antimicrobial cationic peptides

تعداد نتایج: 175492  

Journal: :Physical review letters 2007
Sattar Taheri-Araghi Bae-Yeun Ha

Antimicrobial peptides are known to selectively disrupt (highly charged) microbial membranes by asymmetrical incorporation into the outer layers. We present a physical basis for membrane-charge selectivity of cationic antimicrobial peptides. In particular, we provide a clear picture of how peptide-charge Q influences the asymmetrical insertion--one salient feature is the existence of an optimal...

Journal: :Antimicrobial Agents and Chemotherapy 2010

Journal: :Antimicrobial agents and chemotherapy 2009
Ilknur Senyürek Maren Paulmann Tobias Sinnberg Hubert Kalbacher Martin Deeg Thomas Gutsmann Marina Hermes Thomas Kohler Fritz Götz Christiane Wolz Andreas Peschel Birgit Schittek

Dermcidin (DCD) is an antimicrobial peptide which is constitutively expressed in eccrine sweat glands. By postsecretory proteolytic processing in sweat, the DCD protein gives rise to anionic and cationic DCD peptides with a broad spectrum of antimicrobial activity. Many antimicrobial peptides induce membrane permeabilization as part of their killing mechanism, which is accompanied by a loss of ...

Journal: :Antimicrobial Agents and Chemotherapy 1999

Journal: :Proceedings. Biological sciences 2006
Gabriel G Perron Michael Zasloff Graham Bell

A novel class of antibiotics based on the antimicrobial properties of immune peptides of multicellular organisms is attracting increasing interest as a major weapon against resistant microbes. It has been claimed that cationic antimicrobial peptides exploit fundamental features of the bacterial cell so that resistance is much less likely to evolve than in the case of conventional antibiotics. P...

2017
Annabelle Mouammine Sylvie Pages Anne Lanois Sophie Gaudriault Gregory Jubelin Maurine Bonabaud Stéphane Cruveiller Emeric Dubois David Roche Ludovic Legrand Julien Brillard Alain Givaudan

Some of the bacterial cells in isogenic populations behave differently from others. We describe here how a new type of phenotypic heterogeneity relating to resistance to cationic antimicrobial peptides (CAMPs) is determinant for the pathogenic infection process of the entomopathogenic bacterium Photorhabdus luminescens. We demonstrate that the resistant subpopulation, which accounts for only 0....

Journal: :Journal of the American Chemical Society 2009
Riqiang Fu Eric D Gordon Daniel J Hibbard Myriam Cotten

High-resolution two-dimensional (2D) (1)H-(15)N heteronuclear correlation (HETCOR) spectroscopy has been used to characterize the structure and dynamics of (15)N-backbone labeled antimicrobial piscidin 1 (p1) oriented in "native-like" hydrated lipid bilayers. Piscidin belongs to a family of amphipatic cationic antimicrobial peptides, which are membrane-active and have broad spectrum antimicrobi...

2012
Reinaldo Ramos Lucília Domingues Miguel Gama

Cationic antimicrobial peptides (AMPs) represent the first line of defense against many invading pathogens. These small amphipathic peptides are part of the innate immune system and have a broad-spectrum activity against bacteria, fungi and viruses. In mammals, at least two distinct groups of AMPs are found. Defensins are the more representatives and cathelicidins form the second group. The hCA...

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