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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An antifungal mechanism of curcumin lies in membrane-targeted action within Candida albicans
Won-Young Lee,Dong Gun Lee +1 more
TL;DR: It is suggested that curcumin exerts antifungal activity via inducing disruption of fungal plasma membrane through leakage of intracellular component through the flappy membrane.
Journal ArticleDOI
Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR.
TL;DR: The recent solid state (2)H NMR studies of the orientation of PGLa in lipid membranes alone and in the presence of magainin 2 are described in detail, and some new data from 3,3,3-( 2)H(3)-L-alanine labeled P GLa are included in the analysis.
Journal ArticleDOI
Engineering Antimicrobial Peptides with Improved Antimicrobial and Hemolytic Activities
TL;DR: The most active mutants with the balanced substitutions of positively charged Arg and hydrophobic Trp residues at specific positions were discovered to achieve the improved antimicrobial activity while minimizing red blood cell lysis.
Journal ArticleDOI
The role of antimicrobial peptides in plant immunity
Marcelo Lattarulo Campos,Marcelo Lattarulo Campos,Camila Maurmann de Souza,Kamila Botelho Sampaio de Oliveira,Simoni Campos Dias,Simoni Campos Dias,Octavio L. Franco,Octavio L. Franco +7 more
TL;DR: It is demonstrated that the capacity of plant AMPs to act against a large spectrum of enemies relies on their diverse mechanism of action and remarkable structural stability.
Journal ArticleDOI
Developing Antibacterial Nanocrystalline Cellulose Using Natural Antibacterial Agents.
TL;DR: It is suggested that antibacterial SNCC is a promising candidate for the development of antibacterial wound dressings after successful attachment of both nisin and lysozyme onto the SNCC.
References
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Journal ArticleDOI
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