The Potential of Antimicrobial Peptides as Biocides

Laverty, Garry; Gorman, Seán; Gilmore, Brendan

doi:10.3390/ijms12106566

Cited by 149 publications

(128 citation statements)

References 225 publications

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“…They are very diverse in their sequences, length (generally short) and structures (some of them are linear while others are cyclic sometimes due to disulfide bridges, with a variety of secondary structures), but they adopt an amphipathic conformation that allows them to interact and disrupt selectively the negatively charged microbial membranes. No single mechanism can be defined for all AMPs, but despite these differences it can be concluded that they act mainly by binding to membranes and kill bacteria by disrupting membrane packing and organization, causing defects in the membrane with the consequent dissipation of transmembrane potential and leakage of important cellular contents [10][11][12]. In the case of PxB as well as cecropin and other AMPs, the proposed mechanism of action is based on the formation of periplasmic membrane contacts between outer and inner membranes.…”

Section: Introductionmentioning

confidence: 99%

Membrane interaction of a new synthetic antimicrobial lipopeptide sp-85 with broad spectrum activity

Grau-Campistany

Pujol

Marqués

et al. 2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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ARTICLE IN PRESS• Sp-85 is a new synthetic antibiotic lipopeptide with broad spectrum activity.• Pressure-area curves of mixed monolayers show non-ideal mixing.• Binding to anionic liposomes results in fusion and leakage of aqueous contents.• TEM images of antibiotic-exposed bacteria show damaged membranes.• A mechanism of action based on bacterial membrane destabilization is proposed.g r a p h i c a l a b s t r a c t a r t i c l e i n f o a b s t r a c tAntimicrobial peptides offer a new class of therapeutic agents to which bacteria may not be able to develop genetic resistance, since their main activity is in the lipid component of the bacterial cell membrane. We have developed a series of synthetic cationic cyclic lipopeptides based on natural polymyxin, and in this work we explore the interaction of sp-85, an analog that contains a C12 fatty acid at the N-terminus and two residues of arginine. This analog has been selected from its broad spectrum antibacterial activity in the micromolar range, and it has a disruptive action on the cytoplasmic membrane of bacteria, as demonstrated by TEM. In order to obtain information on the interaction of this analog with membrane lipids, we have obtained thermodynamic parameters from mixed monolayers prepared with POPG and POPE/POPG (molar ratio 6:4), as models of Gram positive and Gram negative bacteria, respectively. Langmuir-Blodgett films have been extracted on glass plates and observed by confocal microscopy, and images are consistent with a strong destabilizing effect on the membrane organization induced by sp-85. The effect of sp-85 on the membrane is confirmed with unilamelar lipid vesicles of the same composition, where biophysical experiments based on fluorescence are indicative of membrane fusion and permeabilization starting at very low concentrations of peptide and only if anionic lipids are present. Overall, results described here provide strong evidence that the mode of action of sp-85 is the alteration of the bacterial membrane permeability barrier.

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Section: Introductionmentioning

confidence: 99%

Membrane interaction of a new synthetic antimicrobial lipopeptide sp-85 with broad spectrum activity

Grau-Campistany

Pujol

Marqués

et al. 2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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“…In recent decades, they have been the focus of intensive research as a result of the development of antibiotic resistance and a growing need for highly efficient genes for disease control in crops [2,[5][6][7][8]. Unexpected abundance of AMP genes (approximately 2-3% of the protein-coding genes) in plant genomes was disclosed by bioinformatics tools [9,10], which reflects long-term plant-pathogen coevolution and highlights the role of AMPs in defence and possibly other vital functions.…”

Section: Introductionmentioning

confidence: 99%

Genes encoding 4‐Cys antimicrobial peptides in wheat Triticum kiharae Dorof. et Migush.: multimodular structural organization, instraspecific variability, distribution and role in defence

et al. 2013

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A novel family of antifungal peptides was discovered in the wheat Triticum kiharae Dorof. et Migusch. Two members of the family, designated Tk-AMP-X1 and Tk-AMP-X2, were completely sequenced and shown to belong to the a-hairpinin structural family of plant peptides with a characteristic C1XXXC2-X(n)-C3XXXC4 motif. The peptides inhibit the spore germination of several fungal pathogens in vitro. cDNA and gene cloning disclosed unique structure of genes encoding Tk-AMP-X peptides. They code for precursor proteins of unusual multimodular structure, consisting of a signal peptide, several a-hairpinin (4-Cys) peptide domains with a characteristic cysteine pattern separated by linkers and a C-terminal prodomain. Three types of precursor proteins, with five, six or seven 4-Cys peptide modules, were found in wheat. Among the predicted family members, several peptides previously isolated from T. kiharae seeds were identified. Genes encoding Tk-AMP-X precursors have no introns in the proteincoding regions and are upregulated by fungal pathogens and abiotic stress, providing conclusive evidence for their role in stress response. A combined PCR-based and bioinformatics approach was used to search for related genes in the plant kingdom. Homologous genes differing in the number of peptide modules were discovered in phylogenetically-related Triticum and Aegilops species, including polyploid wheat genome donors. Association of the Tk-AMP-X genes with A, B/G or D genomes of hexaploid wheat was demonstrated. Furthermore, Tk-AMP-X-related sequences were shown to be widespread in the Poaceae family among economically important crops, such as barley, rice and maize.

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“…The continuous increase of resistance among pathogenic microorganisms to conventional antibiotics has encouraged the development of new antimicrobial agents for the treatment of pathogenic diseases [5]. Various AMPs with broad and selective antimicrobial activity and less risk of resistance development in microbial populations are promising, new, alternative candidates for antibiotics [6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Recombinant expression of LFchimera antimicrobial peptide in a plant-based expression system and its antimicrobial activity against clinical and phytopathogenic bacteria

Chahardoli

Fazeli

Niazi‎

et al. 2018

Biotechnology & Biotechnological Equipment

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Antimicrobial peptides (AMPs) with their broad and selective antimicrobial activity and lowered risk of resistance development in microbial populations are promining as a new alternative candidate to conventional antibiotics. Plant-based expression systems can be employed as cost-effective and high scale-up capacity production hosts for recombinant expression of AMPs. LFchimera is a chimerical peptide containing LFcin and LFampin antimicrobial peptides of bovine lactoferrin, and it has stronger bactericidal activity. Here, the LFchimera sequence was codon-optimized for tobacco and fused with endoplasmic reticulum retention signals along with a CaMV 35S promoter and then transferred by agrobacterium-mediated transformation. The integration and expression of the transgene in tobacco plants were confirmed by polymerase chain reaction (PCR) and RT-PCR, respectively. Recombinant production of the peptide was confirmed by sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE), and peptide functional activity was confirmed by the antibacterial evaluation of total protein extracts against various clinical and phytopathogenic bacteria. Finally, LFchimera peptide was partially purified using an affinity column, and the antibacterial activity was shown. Taken together, these results confirmed that tobacco can be utilized for the recombinant production of antimicrobial peptides such as LFchimera.

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The Potential of Antimicrobial Peptides as Biocides

Cited by 149 publications

References 225 publications

Membrane interaction of a new synthetic antimicrobial lipopeptide sp-85 with broad spectrum activity

Membrane interaction of a new synthetic antimicrobial lipopeptide sp-85 with broad spectrum activity

Genes encoding 4‐Cys antimicrobial peptides in wheat Triticum kiharae Dorof. et Migush.: multimodular structural organization, instraspecific variability, distribution and role in defence

Recombinant expression of LFchimera antimicrobial peptide in a plant-based expression system and its antimicrobial activity against clinical and phytopathogenic bacteria

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