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
Leptoglycin: a new Glycine/Leucine-rich antimicrobial peptide isolated from the skin secretion of the South American frog Leptodactylus pentadactylus (Leptodactylidae)
Juliana Carvalho de Sousa,Raquel F. Berto,Elicélia A. Gois,Nauíla C. Fontenele-Cardi,José E.R. Honório-Júnior,Katsuhiro Konno,Michael K. Richardson,Marcos Fábio Gadelha Rocha,Antonio Camargo,Daniel C. Pimenta,Bruno A. Cardi,Krishnamurti M. Carvalho +11 more
TL;DR: The amino acid sequence of leptoglycin with high level of glycine and leucine containing an unusual central proline suggests the existence of a new class of Gly/Leu-rich antimicrobial peptides.
Journal ArticleDOI
The First Gene-encoded Amphibian Neurotoxin *
Dewen You,Dewen You,Jing Hong,Mingqiang Rong,Haining Yu,Songping Liang,Yufang Ma,Yufang Ma,Hailong Yang,Hailong Yang,Jing Wu,Jing Wu,Donghai Lin,Ren Lai +13 more
TL;DR: A novel 60-residue neurotoxin peptide (anntoxin) that inhibited tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channel (VGSC) was purified and characterized from the skin secretions of the tree frog Hyla annectans, the first gene-encoded neurotoxin found in amphibians.
Journal ArticleDOI
The antibacterial activity of 4,4'-bipyridinium amphiphiles with conventional, bicephalic and gemini architectures.
Melissa C. Grenier,Robert W. Davis,Kelsey L. Wilson-Henjum,Jade E. LaDow,Jacob W. Black,Kevin L. Caran,Kyle Seifert,Kevin P. C. Minbiole +7 more
TL;DR: A series of mono- and bis-alkylated analogs of 4,4'-bipyridinium compounds were prepared to investigate structure-activity relationships in their inhibition of a battery of Gram positive and Gram negative bacteria, and the most bioactive compounds were gemini in structure.
Journal ArticleDOI
TRC40 can deliver short secretory proteins to the Sec61 translocon
TL;DR: Two human secretory protein precursors, apelin and statherin, are identified as bona fide substrates for post-translational translocation across the mammalian endoplasmic reticulum (ER) membrane, and it is speculated that the post- Transformer translocation of secretory proteins in higher eukaryotes is more prevalent than previously acknowledged.
Journal ArticleDOI
Ubiquitously expressed Human Beta Defensin 1 (hBD1) forms bacteria-entrapping nets in a redox dependent mode of action.
Judith Raschig,Daniela Mailänder-Sánchez,Anne Berscheid,Jürgen Berger,Adam A. Strömstedt,L Courth,Nisar P. Malek,Heike Brötz-Oesterhelt,Jan Wehkamp +8 more
TL;DR: Surprisingly, using electron microscopy, a so far unknown net-like structure surrounding bacteria is detected, which were treated with the reduced but not the oxidized form of hBD1.
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