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
Citations
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Journal ArticleDOI
Peptides and Peptidomimetics for Antimicrobial Drug Design
Biljana Mojsoska,Håvard Jenssen +1 more
TL;DR: The purpose of this paper is to introduce and highlight a few classes of traditional antimicrobial peptides with a focus on structure-activity relationship studies, and the contributions of individual amino acids with respect to the peptides antibacterial properties.
Journal ArticleDOI
Synthesis, Self-Assembly, and Biomedical Applications of Antimicrobial Peptide–Polymer Conjugates
TL;DR: This Perspective seeks to highlight the state-of-the-art strategy for the synthesis, self-assembly, and biomedical applications of AMP-polymer conjugates and explore the promising directions for future research ranging from synthetic strategies, multistage and stimuli-responsive antibacterial activities, antifungi applications, and potentials in elimination of inflammation during medical treatment.
Journal ArticleDOI
Sequence Requirements and an Optimization Strategy for Short Antimicrobial Peptides
Kai Hilpert,Melissa Elliott,Rudolf Volkmer-Engert,Peter Henklein,Oreola Donini,Qun Zhou,Dirk F. H. Winkler,Robert E. W. Hancock +7 more
TL;DR: Short antimicrobial host-defense peptides represent a possible alternative as lead structures to fight antibiotic resistant bacterial infections by providing a cost and time effective enrichment of new candidates for drug development, increasing the chances of finding pharmacologically relevant peptides.
Journal ArticleDOI
On the mechanism of pore-formation by melittin
TL;DR: It is shown that in membranes composed of zwitterionic lipids, i.e. phosphatidylcholine, melittin not only forms pores but also inhibits pore formation, and proposes that these two modes of action are the result of two competing reactions: direct insertion into the membrane and binding parallel to the membrane surface.
Journal ArticleDOI
Road to clinical efficacy: challenges and novel strategies for antimicrobial peptide development
TL;DR: As peptide synthesis and recombinant production methodologies improve, and more relevant bioassays become available, it becomes increasingly likely that AMPs will break the regulatory barrier and enter the marketplace as valuable antimicrobial weapons in the next 10 years.
References
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