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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Journal ArticleDOI
High potency and broad-spectrum antimicrobial peptides synthesized via ring-opening polymerization of alpha-aminoacid-N-carboxyanhydrides.
Chuncai Zhou,Xiaobao Qi,Peng Li,Wei Ning Chen,Lamrani Mouad,Matthew Wook Chang,Susanna Su Jan Leong,Mary B. Chan-Park +7 more
TL;DR: This method offers high potential for inexpensive synthesis of substantial quantities of AMPs via ring-opening polymerization of alpha-amino acid N-carboxyanhydrides (NCA) using a transition metal initiator and includes membrane disruption, which is likely to inhibit rapid induction of AMP-resistance in pathogens
Journal ArticleDOI
The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism
David I. Fernandez,Anton P. Le Brun,Thomas C. Whitwell,Marc-Antoine Sani,Michael James,Michael James,Frances Separovic +6 more
TL;DR: The antimicrobial peptide interaction is consistent with the carpet mechanism for aurein 1.2 with discrete structural changes depending on the type of phospholipid membrane, with subtle changes in membrane structure caused by the peptide.
Journal ArticleDOI
Zwitterionic Phospholipids and Sterols Modulate Antimicrobial Peptide-Induced Membrane Destabilization
TL;DR: It is shown how sterols can protect even negatively charged membranes from the disruptive effects of antimicrobial peptides, thereby providing a molecular view of the differences in sensitivity of various target membranes to linear cationic antibiotic peptides.
Journal ArticleDOI
Nisin and other antimicrobial peptides: Production, mechanisms of action, and application in active food packaging
Johnson Clay Santos,Rita de Cássia Superbi de Sousa,Caio G. Otoni,Allan Robledo Fialho e Moraes,Victor Gomes Lauriano Souza,Eber Antonio Alves Medeiros,Paula J.P. Espitia,Ana Clarissa dos Santos Pires,Jane Sélia dos Reis Coimbra,Nilda de Fátima Ferreira Soares +9 more
TL;DR: A comprehensive review of antimicrobial peptides, from synthesis procedures to mechanisms of action, with an emphasis on nisin is presented, and a historical outlook and the current perspectives of their potential applications in food packaging systems are addressed.
Journal ArticleDOI
“Doubly Selective” Antimicrobial Polymers: How Do They Differentiate between Bacteria?
TL;DR: The molecular-weight-dependent antimicrobial activity of the SMAMPs was shown to be a sieving effect: while the 3000 g mol(-1) SMAMP was able to penetrate the peptidoglycan layer of the Gram-positive S. aureus bacteria, the 50000 g mol−1 SMAMP got stuck and consequently did not have antimicrobialActivity.
References
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