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
Novel Apidaecin 1b Analogs with Superior Serum Stabilities for Treatment of Infections by Gram-Negative Pathogens
Nicole Berthold,Patricia Czihal,Stefanie Fritsche,Ute Sauer,Guido Schiffer,Daniel Knappe,Gottfried Alber,Ralf Hoffmann +7 more
TL;DR: It is shown that Api88 is degraded relatively fast upon incubation with mouse serum, by cleavage of the C-terminal leucine residue, and Api137 appears to be a very promising lead compound that should be even more efficient in vivo than Api 88.
Journal ArticleDOI
Melittin-lipid bilayer interactions and the role of cholesterol.
TL;DR: Comparison of microscopy and leakage data suggests that melittin-induced leakage occurs via different mechanisms in the cholesterol-free and cholesterol-supplemented systems, and it is significant that the presence of cholesterol does not increase the amount of membrane-associatedmelittin needed to cause maximum leakage from, or major structural rearrangements of, the liposomes.
Journal ArticleDOI
Real-time attack of LL-37 on single Bacillus subtilis cells.
TL;DR: Time-lapse fluorescence microscopy of single, growing Bacillus subtilis cells with 2-12s time resolution reveals the mechanisms of antimicrobial peptide (AMP) action on a Gram-positive species with unprecedented detail.
Journal ArticleDOI
Antimicrobial peptides from different plant sources: Isolation, characterisation, and purification.
Swee-Seong Tang,Zakaria Hossain Prodhan,Sudhangshu Kumar Biswas,Cheng Foh Le,Shamala Devi Sekaran +4 more
TL;DR: New and different approaches to the selection, characterisation, isolation, purification, mode of action and bioactivity assessment of a range of AMPs collected from plant sources are highlighted.
Journal ArticleDOI
dbAMP: an integrated resource for exploring antimicrobial peptides with functional activities and physicochemical properties on transcriptome and proteome data
Jhih-Hua Jhong,Yu-Hsiang Chi,Wen-Chi Li,Tsai-Hsuan Lin,Kai-Yao Huang,Tzong-Yi Lee,Tzong-Yi Lee +6 more
TL;DR: The dbAMP database as mentioned in this paper is a database of antimicrobial peptides (AMPs) from the public domain and manually curated literature, including 12, 389 unique entries, including 4271 experimentally verified AMPs and 8118 putative AMPs along with their functional activities, supported by 1924 articles.
References
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