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Journal ArticleDOI

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Kim A. Brogden
- 01 Mar 2005 - 
- Vol. 3, Iss: 3, pp 238-250
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.

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Citations
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Acinetobacter baumannii: Emergence of a Successful Pathogen

TL;DR: This review details the significant advances that have been made in understanding of this remarkable organism over the last 10 years, including current taxonomy and species identification, issues with susceptibility testing, mechanisms of antibiotic resistance, global epidemiology, clinical impact of infection, host-pathogen interactions, and infection control and therapeutic considerations.
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Antifouling coatings: recent developments in the design of surfaces that prevent fouling by proteins, bacteria, and marine organisms.

TL;DR: The major strategies for designing surfaces that prevent fouling due to proteins, bacteria, and marine organisms are reviewed and ongoing research in this area should result in the development of even better antifouling materials in the future.
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Peptide Antimicrobial Agents

TL;DR: The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides.
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Inflammatory bowel disease: cause and immunobiology

TL;DR: How environmental factors, infectious microbes, ethnic origin, genetic susceptibility, and a dysregulated immune system can result in mucosal inflammation are discussed.
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Designing antimicrobial peptides: form follows function

TL;DR: In this article, advanced computer assisted design strategies that address the difficult problem of relating primary sequence to peptide structure, and are delivering more potent, cost-effective, broad-spectrum peptides as potential next-generation antibiotics.
References
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Journal ArticleDOI

Cutting edge: IFN-inducible ELR- CXC chemokines display defensin-like antimicrobial activity.

TL;DR: Members of the IFN-γ-inducible tripeptide motif Glu-Leu-Arg− CXC chemokines were antimicrobial against Escherichia coli and Listeria monocytogenes and suggest that, in tissues with mononuclear cell infiltration, IFN -γ-Inducible chemokine may reach concentrations necessary for microbicidal activity.
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Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family

TL;DR: Genetic and biochemical evidence is reported that gonococcal susceptibility to the lethal action of PG-1 and other structurally unrelated antibacterial peptides, including a peptide that is expressed constitutively by human granulocytes and testis and inducibly by keratinocytes, is modulated by an energy-dependent efflux system termed mtr.
Journal ArticleDOI

Electrically gated ionic channels in lipid bilayers.

TL;DR: The generation of action potentials in nerve and muscle requires cell membranes with steeply voltage-dependent ionic permeabilities, and the process of activating ionic pathways by some stimulus, such as a change in membrane potential, is called gating.
Journal ArticleDOI

The Lantibiotic Mersacidin Inhibits Peptidoglycan Synthesis by Targeting Lipid II

TL;DR: The interaction of mersacidin with lipid II apparently occurs via a binding site which is not targeted by any antibiotic currently in use, and in contrast to the glycopeptide antibiotics, complex formation does not involve the C-terminald-alanyl–d-alanine moiety of the lipid intermediate.
Journal ArticleDOI

Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics.

TL;DR: A few cationic antimicrobial peptides have entered clinical trials to date, with mixed success, but their diverse portfolio of structures, activity spectra, biological activities, and modes of action, provide substantial potential.
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