Journal ArticleDOI
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
TLDR
In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented and several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibits protein synthesis or inhibit enzymatic activity.Abstract:
Antimicrobial peptides are an abundant and diverse group of molecules that are produced by many tissues and cell types in a variety of invertebrate, plant and animal species. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by 'barrel-stave', 'carpet' or 'toroidal-pore' mechanisms. Although these models are helpful for defining mechanisms of antimicrobial peptide activity, their relevance to how peptides damage and kill microorganisms still need to be clarified. Recently, there has been speculation that transmembrane pore formation is not the only mechanism of microbial killing. In fact several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibit protein synthesis or inhibit enzymatic activity. In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented.read more
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Antimicrobial peptides generated from milk proteins: a survey and prospects for application in the food industry. A review
TL;DR: This review attempts to study the literature pertaining to antimicrobial peptides derived from major milk proteins upon hydrolysis either by digestive proteases or by fermentation with proteolytic lactic acid bacteria.
Journal ArticleDOI
Conformation and Membrane Orientation of Amphiphilic Helical Peptides by Oriented Circular Dichroism
Jochen Bürck,Siegmar Roth,Parvesh Wadhwani,Sergii Afonin,Nathalie Kanithasen,Erik Strandberg,Anne S. Ulrich +6 more
TL;DR: Changes in peptide conformation and membrane alignment observed here by OCD seem to be functionally relevant, as they can be correlated with the membrane perturbing activities of the three antimicrobial and cell-penetrating sequences.
Journal ArticleDOI
Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?
Marlon H. Cardoso,Marlon H. Cardoso,Raquel Q. Orozco,Raquel Q. Orozco,Samilla B. Rezende,Gisele Regina Rodrigues,Karen G N Oshiro,Karen G N Oshiro,Elizabete de Souza Cândido,Elizabete de Souza Cândido,Octavio L. Franco +10 more
TL;DR: This review will focus on the main computational strategies that have generated AMPs with promising activities against pathogenic bacteria, as well as anti-infective potential in different animal models, including sepsis and cutaneous infections.
Journal ArticleDOI
Mechanism of a prototypical synthetic membrane-active antimicrobial: Efficient hole-punching via interaction with negative intrinsic curvature lipids
Lihua Yang,Vernita Gordon,Dallas R. Trinkle,Nathan W. Schmidt,Matthew A. Davis,Clarabelle DeVries,Abhigyan Som,John E. Cronan,Gregory N. Tew,Gerard C. L. Wong +9 more
TL;DR: It is shown unambiguously that bacterial membrane permeation by these antimicrobials depends on the presence of negative intrinsic curvature lipids, such as phosphatidylethanolamine (PE)lipids, found in high concentrations within bacterial membranes.
Journal ArticleDOI
Membrane Active Peptides and Their Biophysical Characterization
TL;DR: Recent advances in experimental and computational investigation of membrane active peptides are summarized with particular emphasis on two amphipathic membraneactive peptides, the AMP melittin and the CPP pVEC.
References
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Journal ArticleDOI
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