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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Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle.
Zakhar O. Shenkarev,Kirill D. Nadezhdin,Vladimir A. Sobol,A.G. Sobol,Lars Skjeldal,Alexander S. Arseniev +5 more
TL;DR: Detailed structural analysis and comparison with other knottins revealed structural conservation of the two‐disulfide motif in cyclic and acyclic peptides and permit consideration of the cyclotides as membrane‐active cationic antimicrobial peptides.
Journal ArticleDOI
Single-cell, real-time detection of oxidative stress induced in Escherichia coli by the antimicrobial peptide CM15
TL;DR: It is demonstrated that for Escherichia coli in aerobic conditions, the peptide CM15 induces a burst of biochemically harmful reactive oxygen species within 30 s of membrane permeabilization, which may prove a significant bacteriostatic mechanism for a variety of cationic AMPs.
Journal ArticleDOI
Therapeutic antimicrobial peptides may compromise natural immunity
TL;DR: Using experimental evolution, it is demonstrated that Staphylococcus aureus rapidly evolved resistance to pexiganan, a drug-candidate for diabetic leg ulcer infections, and this unintended consequence of therapeutic use could drastically undermine the innate immune system's ability to control and clear microbial infections.
Journal ArticleDOI
Antibacterial and antiviral functional materials: Chemistry and Biological Activity toward Tackling COVID-19-like Pandemics
Bhuvaneshwari Balasubramaniam,Prateek,Sudhir Ranjan,Mohit Saraf,Prasenjit Kar,Surya Pratap Singh,Vijay Kumar Thakur,Anand Singh,Raju Kumar Gupta +8 more
TL;DR: In this paper, the authors have surveyed antibacterial and antiviral materials of various classes such as small-molecule organics, synthetic and biodegradable polymers, silver, TiO2, and copper-derived chemicals.
Journal ArticleDOI
Antimicrobial polymers prepared by ring-opening metathesis polymerization: manipulating antimicrobial properties by organic counterion and charge density variation.
TL;DR: The results suggest that, above a certain charge threshold, neither minimum inhibitory concentration (MIC90) nor hemolytic activity (HC50) is greatly affected by adding more cationic groups to the molecule.
References
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