Molecular Diversity in Gene-Encoded, Cationic Antimicrobial Polypeptides

Tossi, Alessandro; Sandri, Luca

doi:10.2174/1381612023395475

Cited by 132 publications

(90 citation statements)

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“…Gram positive bacteria do have a relatively high BLIS production. Biochemical (net charge) and/ or structural features (linear/circular/amino acid composition) are major criteria for classification of antimicrobial peptides (Tossi and Sandri, 2002;Zasloff, 2002). Jack et al(1995) suggested that the presence of disulphide and monosulphide (lanthionine) bonds be the basis for bacterioicin classification and it can be used as a benchmark to denote r their spectrum activity, since presence of higher number of the disulphide bonds in a bacteriocin enhances the activity spectrum .…”

Section: Classification Of Bacteriocinsmentioning

confidence: 99%

Microbial defense systems in foods and feeds

Fatima¹

2017

JBC

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Bacteriocins are proteinaceous substances having antigenic and developed by some microbial strains having the ability and effectiveness against pathogenic bacteria and spoilage, harmless to the consumer, and have no adverse effect on the organoleptic product quality. Bacteriocins are rendered inactive by the action of proteolytic enzymes present in the gastrointestinal tract, thy can resist high temperatures, are non-toxic and does not compromise the immune system in experimental animals. Bacteriocins as microbial defense systems has been widely researched and documented. However, though the diversity and abundance of bactrocins is very high, indicating their use as microbial weapons, research on ecological and evolutionary significance needs elaborate studies. More advanced studies are needed to unfold reasons for their success as toxins.

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Section: Classification Of Bacteriocinsmentioning

confidence: 99%

Microbial defense systems in foods and feeds

Fatima¹

2017

JBC

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“…24 Excellent reviews cover many aspects of the field of gene-enconded, ribosomally synthesized antimicrobial peptides. [25][26][27][28][29][30][31] The molecular diversity of antimicrobial peptide is immense and almost a thousand of structures have already been characterized. Plenty of information can also be retrieved from specialized databases like AMSDb (http://www.bbcm.univ.trieste.it/~tossi/amsdb/html) and ANTIMIC (http://research.i2r.a-star.edu.sg/Templar/DB/ ANTIMIC/).…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

Section: Antimicrobial Peptidesmentioning

confidence: 99%

“…In terms of amino acid composition and net surface charge, they may be rich in one type of amino acid residues (Pro-rich, Pro/ Gly-rich, Trp-rich, His-rich, His/Gly-rich, and Lys-or Arg-rich), confering variable indexes of hydrophobicity, amphipathicity, net positive charge and, in minor cases, net negative charge to these molecules. 25,27 Fragments of protein domains can also present antimicrobial properties.For instance, the carboxyl terminal thirty amino acids of the -subunit of human hemoglobin, which forms a cationic -helix is active against Escherichia coli, Staphylococcus aureus and Candida albicans.32 Antimicrobial peptides are also generated by cleavage of -casein by strains of Lactobacillus acidophilus. Three casein-derived AMPs (IKHQGLPQE, VLNENLLR, and SDIPNPIGSENSEK) showed antibacterial activity against pathogenic strains of Enterobacter sakazakii and Escherichia coli.…”

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confidence: 99%

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Membrane-translocating peptides and toxins: from nature to bedside

Baptista¹,

Kerkis

Silva³

et al. 2008

J. Braz. Chem. Soc.

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Atualmente, diferentes classes funcionais de peptídeos e toxinas biologicamente ativas isolados de diversos organismos são conhecidas. Em medicina, esses polipeptídios podem ser diretamente utilizados ou podem servir como modelos para a geração de moléculas derivadas. Aqui, nós fazemos referência a três classes de peptídeos e toxinas que agem sobre membranas celulares ou sobre sistemas de transporte por membranas: (i) toxinas binárias; (ii) peptídeos antimicrobianos; (iii) peptídeos penetradores de células. As toxinas binárias têm sido geneticamente manipuladas para gerar imunotoxinas específicas, enquanto os peptídeos antimicrobianos são usados como agentes alternativos contra células tumorais e microbianas resistentes. Os peptídeos penetradores de células têm aplicações que vão desde a transfecção celular quanto ao transporte intracelular de nanopartículas. Nosso grupo vem investigando a capacidade da crotamina, um peptídeo do veneno de cascavel, em translocar membranas celulares, bem como de utilizar a crotamina como sistema de transporte molecular e de análise de imagens.Today, different functional classes of bioactive peptides and toxins isolated from diverse sources of living organisms are known. In medicine, these polypeptides present the potential to be used structurally unmodified or to serve as templates for molecular design of improved derivatives. Here, we refer to members of three classes of remarkable peptides and toxins that act at the cell membranes level and membrane trafficking systems: (i) the binary toxins (ii) the antimicrobial peptides and (iii) the cell penetrating peptides. Binary toxins have been genetically manipulated to generate specific immunotoxins, while antimicrobial peptides are in use as alternative agents against resistant microbes and tumor cells. Cell penetrating peptides have applications as diverse as cell transfection and transport of nanomaterials. Our group is dissecting the capacity of crotamine, a peptide from rattlesnake venom, to translocate cell membranes and use it as a delivery system in the transducing technology and molecular imaging.Keywords: cytolysin, binary toxin, antimicrobial peptide, cell-penetrating peptide, animal toxin, nanobiotechnology Binary Bacterial ToxinsA wide variety of bacterial toxins that has the cell membrane as a target is presently known. Indeed the molecular diversity of bacterial toxins is so remarkable that a large number of microorganisms secret several toxic peptides and polypeptides devoid of or having catalytic activity. All these toxins are capable of intoxicating eucaryotic cells by interfering directly with cytoplasmic membrane or by using membrane systems to gain access Membrane-translocating Peptides and Toxins: from Nature to Bedside J. Braz. Chem. Soc. 212 to the interior of cells for the delivery of their active domain.In the first case, single chain proteins or composed of two separate water-soluble proteins -which oligomerize during their action on phospholipid membrane and form pores or channels -encompass the cytoly...

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“…Among them, histatin recovered from saliva from humans and primates and primarily directed against fungal pathogens, outstands for its distinctive mechanism of action which does not involve channel formation in the fungal cytoplasmic membrane but rather translocates efficiently into the cell and targets the mitochondrion (Tsai and Bobek, 1998). Those enriched in histidine and glycine are quite large, also affecting fungal pathogens and a distinctive feature is that their residues are arranged in approximately regular but different structural repeats (Tossi and Sandri, 2002). Finally, only two peptides enriched in tryptophan residues have been described, both derived from porcine cathelicidin precursors (Schibli et al 2002).…”

Section: From Eukaryotesmentioning

confidence: 99%