Peptide antibiotics: An alternative and effective antimicrobial strategy to circumvent fungal infections

Ajesh, K.; Sreejith, K.

doi:10.1016/j.peptides.2009.01.026

Cited by 57 publications

(35 citation statements)

References 158 publications

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“…Bacteria and fungi could synthesize a wide variety of metabolites with antimicrobial activity, which have been widely exploited in the pharmaceutical sector [1]. Several Bacillus subtilis (B. subtilis) strains have the potential to produce a range of antimicrobial cyclic lipopeptides, including iturins, fengycins and surfactins [2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Analysis of free amino acids during fermentation by Bacillus subtilis using capillary electrophoresis

Ren

Zhou

Zhang

et al. 2012

Biotechnol Bioproc E

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A high performance capillary electrophoresis (HPCE) method was presented to identify and quantitate free amino acids during fermentation by Bacillus subtilis. Amino acids, pre-column derivatized with phenylisothicyanate, were separated and characterized by HPCE. In order to optimize separation conditions, the assay was developed by varying the β-cyclodextrin concentration and pH of the background electrolyte. A buffer system comprising 30 mM phosphate and 3 mM β-cyclodextrin at pH 7.0, voltage of 20 kV and detection wavelength of 254 nm showed the best results, with 17 out of 20 phenylthioncarbamyl amino acids in a solution adequately separated. For quantification, p-aminobenzoic acid was added as an internal standard. Analysis of free amino acids in Bacillus subtilis culture medium using this method revealed good consistency with the values obtained using conventional ninhydrin-based amino acid analyzer. Four free amino acids (aspartic acid, glutamic acid, proline, and tyrosine) concentration in an extracellular matrix during fermentation by Bacillus subtilis were mainly monitored using this method.

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Section: Introductionmentioning

confidence: 99%

Analysis of free amino acids during fermentation by Bacillus subtilis using capillary electrophoresis

Ren

Zhou

Zhang

et al. 2012

Biotechnol Bioproc E

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“…Although the precise mechanism of AMPs action is still not known, it is generally accepted that these positivelycharged peptides target the anionic bacterial membrane surface, integrate into the lipid bilayer and disrupt its structure, which leads to the leakage of cytoplasmic components and cell death [6][7][8][9][10][11][12]16,17]. Recently, a few papers have appeared that address the mechanism of action of AMPs (melittin, lactoferrin, dermaseptins, plant defensin) on C. albicans and other kinds of yeast showing that the peptides at low concentrations act via an apoptotic mechanism [18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

The antifungal effect of peptides from hymenoptera venom and their analogs

et al. 2011

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As the occurrence of Candida species infections increases, so does resistance against commonly-used antifungal agents. It is therefore necessary to look for new antifungal drugs. This study investigated the antifungal activity of recently isolated, synthesized and characterized antimicrobial α-helical amphipathic peptides (12–18 amino acids long) from the venom of hymenoptera (melectin, lasioglossins I, II, and III, halictines I and II) as well as a whole series of synthetic analogs. The minimal inhibitory concentrations (MICs) against different Candida species (C. albicans, C. krusei, C. glabrata, C. tropicalis and C. parapsilosis) of the natural peptides amounted to 4–20 µM (7–40 mg/l). The most active were the synthetic analog all-D-lasioglossin III and lasioglossin III analog KNWKK-Aib-LGK-Aib-IK-Aib-VK-NH2. As shown using a) colony forming unit determination on agar plates, b) the efflux of the dye from rhodamine 6B-loaded cells, c) propidium iodide and DAPI staining, and d) fluorescently labeled antimicrobial peptide (5(6)-carboxyfluorescein lasioglossin-III), the killing of fungi by the peptides studied occurs within minutes and might be accompanied by a disturbance of all membrane barriers. The peptides represent a promising lead for the development of new, effective antifungal drugs.

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“…Antimicrobial peptides exhibit a broad spectrum of activity mainly against bacteria and fungi but also against viruses, parasites, and tumor cells (2,13,15,17,26,40,53). Most of them are cationic and have the ability to adopt an amphipathic conformation, properties that govern their antibacterial activity.…”

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confidence: 99%

Improvement of the Efficacy of Linear Undecapeptides against Plant-Pathogenic Bacteria by Incorporation of d -Amino Acids

Güell¹,

Cabrefiga

Badosa

et al. 2011

Appl Environ Microbiol

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A set of 31 undecapeptides, incorporating 1 to 11 D-amino acids and derived from the antimicrobial peptide BP100 (KKLFKKILKYL-NH 2 ), was designed and synthesized. This set was evaluated for inhibition of growth of the plant-pathogenic bacteria Erwinia amylovora, Pseudomonas syringae pv. syringae, and Xanthomonas axonopodis pv. vesicatoria, hemolysis, and protease degradation. Two derivatives were as active as BP100, and 10 peptides displayed improved activity, with the all-D isomer being the most active. Twenty-six peptides were less hemolytic than BP100, and all peptides were more stable against protease degradation. Plant extracts inhibited the activity of BP100 as well as that of the D-isomers. Ten derivatives incorporating one D-amino acid each were tested in an infectivity inhibition assay with the three plant-pathogenic bacteria by using detached pear and pepper leaves and pear fruits. All 10 peptides studied were active against E. amylovora, 6 displayed activity against P. syringae pv. syringae, and 2 displayed activity against X. axonopodis pv. vesicatoria. Peptides BP143 (KKLFKKILKYL-NH 2 ) and BP145 (KKLFKKILKYL-NH 2 ), containing one D-amino acid at positions 4 and 2 (underlined), respectively, were evaluated in whole-plant assays for the control of bacterial blight of pepper and pear and fire blight of pear. Peptide BP143 was as effective as streptomycin in the three pathosystems, was more effective than BP100 against bacterial blight of pepper and pear, and equally effective against fire blight of pear.

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Peptide antibiotics: An alternative and effective antimicrobial strategy to circumvent fungal infections

Cited by 57 publications

References 158 publications

Analysis of free amino acids during fermentation by Bacillus subtilis using capillary electrophoresis

Analysis of free amino acids during fermentation by Bacillus subtilis using capillary electrophoresis

The antifungal effect of peptides from hymenoptera venom and their analogs

Improvement of the Efficacy of Linear Undecapeptides against Plant-Pathogenic Bacteria by Incorporation of d -Amino Acids

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