Defense peptides: recent developments

Cytryńska, Małgorzata; Zdybicka-Barabas, Agnieszka

doi:10.1515/bmc-2015-0014

Cited by 20 publications

(17 citation statements)

References 130 publications

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“…Due to the unique properties of AMPs, they can and should be used for the benefit of humanity in the face of the antibiotic resistance catastrophe (Ventola, 2015). Existing efforts of scientific research are directed toward searching for more effective bactericides and studying of their mode of action (Cytryńska and Zdybicka-Barabas, 2015). Even though such investigations are necessary, there are some aspects of this problem that are poorly addressed by research.…”

Section: Introductionmentioning

confidence: 99%

Sub-inhibitory Effects of Antimicrobial Peptides

Vasilchenko

Рогожин

2019

Front. Microbiol.

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Antimicrobials, and particularly antimicrobial peptides (AMPs), have been thoroughly studied due to their therapeutic potential. The research on their exact mode of action on bacterial cells, especially at under sublethal concentrations, has resulted in a better understanding of the unpredictable nature of bacterial behavior under stress conditions. In this review, we were aiming to gather the wide yet still under-investigated knowledge about various AMPs and their subinhibition effects on cellular and molecular levels. We describe how AMP action is non-linear and unpredictable, also showing that exposure to AMP can lead to antimicrobial resistance via triggering various regulatory systems. Being one of the most known types of antimicrobials, bacteriocins have dual action and can also be utilized by microorganisms as signaling molecules at naturally achievable sub-inhibitory concentrations. The unpredictable nature of AMP action and the pathogenic response triggered by them remains an area of knowledge that requires further investigation.

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Section: Introductionmentioning

confidence: 99%

Sub-inhibitory Effects of Antimicrobial Peptides

Vasilchenko

Рогожин

2019

Front. Microbiol.

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“…Several models have been proposed to explain the interactions of AMPs with microbial membranes, including the barrel-stave, carpet-like, aggregate, and toroidal pore model. Nevertheless, irrespective of the model, it is generally accepted that the initial step of the binding is mediated by electrostatic interactions between the cationic peptide and negatively charged membrane components followed by hydrophobic interactions between amphipathic domains in the peptide molecule and lipid components of the membrane (Nguyen et al 2011;Scocchi et al 2011;Cytryńska and Zdybicka-Barabas 2015).…”

Section: Introductionmentioning

confidence: 99%

Studies on the interactions of neutral Galleria mellonella cecropin D with living bacterial cells

et al. 2018

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Cecropins constitute an important family of insect antimicrobial peptides involved in humoral innate immune response. In comparison with the highly basic cecropins A and B, cecropins D are less cationic and more hydrophobic. Interestingly, cecropins D were described only in lepidopteran insects, e.g., the greater wax moth Galleria mellonella. In the present study, interactions of neutral cecropin D (pI 6.47) purified from hemolymph of G. mellonella with living Escherichia coli cells were investigated. Fluorescence lifetime imaging microscopy using fluorescein isothiocyanate-labeled cecropin D revealed very fast binding of the peptide to E. coli cells. Fourier transform infrared spectroscopy analyses showed that G. mellonella cecropin D interacted especially with E. coli LPS and probably other lipid components of the bacterial cell envelope and exhibited an ordering effect with regard to lipid chains. This effect is consistent with the peptide binding mechanism based upon its incorporation into the lipid phase of the cell membrane. The interaction resulted in permeabilization of the bacterial cell membrane. Upon cecropin D binding, the cells lost characteristic surface topography, which was accompanied by altered nanomechanical properties, as revealed by atomic force microscopy. The interaction of the peptide with the bacterial cells also led to intracellular damage, i.e., loss of the cell envelope multilayer structure, formation of membrane vesicles, and enlargement of periplasmic space, which eventually caused death of the bacteria. In summary, it can be concluded that amphipathic character of α-helices, exposure of small positively charged patches on their polar surfaces and hydrophobic interactions are important physicochemical characteristics related to effective binding to E. coli cells and antibacterial activity of neutral G. mellonella cecropin D.

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“…These investigations have also shown that there are a number of major drivers in the membrane interactions of AMPs of which the most important are charge, hydrophobicity and amphiphilicity [9,18,19]. The vast majority of AMPs are cationic to help facilitate the targeting of microbes through direct electrostatic interaction with anionic components of their membranes [19,20].…”

Section: Introductionmentioning

confidence: 99%

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

et al. 2016

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Antimicrobial peptides (AMPs) are potent antibiotics of the innate immune system that have been extensively investigated as a potential solution to the global problem of infectious diseases caused by pathogenic microbes. A group of AMPs that are increasingly being reported are those that utilise pH dependent antimicrobial mechanisms, and here we review research into this area. This review shows that these antimicrobial molecules are produced by a diverse spectrum of creatures, including vertebrates and invertebrates, and are primarily cationic, although a number of anionic examples are known. Some of these molecules exhibit high pH optima for their antimicrobial activity but in most cases, these AMPs show activity against microbes that present low pH optima, which reflects the acidic pH generally found at their sites of action, particularly the skin. The modes of action used by these molecules are based on a number of major structure/function relationships, which include metal ion binding, changes to net charge and conformational plasticity, and primarily involve the protonation of histidine, aspartic acid and glutamic acid residues at low pH. The pH dependent activity of pore forming antimicrobial proteins involves mechanisms that generally differ fundamentally to those used by pH dependent AMPs, which can be described by the carpet, toroidal pore and barrel-stave pore models of membrane interaction. A number of pH dependent AMPs and antimicrobial proteins have been developed for medical purposes and have successfully completed clinical trials, including kappacins, LL-37, histatins and lactoferrin, along with a number of their derivatives. Major examples of the therapeutic application of these antimicrobial molecules include wound healing as well as the treatment of multiple cancers and infections due to viruses, bacteria and fungi. In general, these applications involve topical administration, such as the use of mouth washes, cream formulations and hydrogel delivery systems. Nonetheless, many pH dependent AMPs and antimicrobial proteins have yet to be fully characterized and these molecules, as a whole, represent an untapped source of novel biologically active agents that could aid fulfillment of the urgent need for alternatives to conventional antibiotics, helping to avert a return to the pre-antibiotic era.

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Defense peptides: recent developments

Cited by 20 publications

References 130 publications

Sub-inhibitory Effects of Antimicrobial Peptides

Sub-inhibitory Effects of Antimicrobial Peptides

Studies on the interactions of neutral Galleria mellonella cecropin D with living bacterial cells

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

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