Evaluation of the epinecidin-1 peptide as an active ingredient in cleaning solutions against pathogens

Pan, Chieh Yu; Rajanbabu, Venugopal; Chen, Jyh-Yih; Her, Guor Mour; Nan, Fan-Hua

doi:10.1016/j.peptides.2010.05.011

Cited by 21 publications

(16 citation statements)

References 30 publications

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“…Epinecidin-1 showed to be a potential candidate for topical application that can prevent vaginal or skin infections due to the synergistic effect that possess with commercial cleaning solutions, where such effect was not affected by low pH or after being stored at room temperature and at 4 °C for up to 14 days [211]. The synergistic effect of pleurocidin and several antibiotics [212], bacteroricin [213] and histone-derived [214] has also been shown [212,213].…”

Section: Therapeuticsmentioning

confidence: 99%

Antimicrobial Peptides from Fish

2014

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Antimicrobial peptides (AMPs) are found widely distributed through Nature, and participate in the innate host defense of each species. Fish are a great source of these peptides, as they express all of the major classes of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and a fish-specific class of the cecropin family, called piscidins. As with other species, the fish peptides exhibit broad-spectrum antimicrobial activity, killing both fish and human pathogens. They are also immunomodulatory, and their genes are highly responsive to microbes and innate immuno-stimulatory molecules. Recent research has demonstrated that some of the unique properties of fish peptides, including their ability to act even in very high salt concentrations, make them good potential targets for development as therapeutic antimicrobials. Further, the stimulation of their gene expression by exogenous factors could be useful in preventing pathogenic microbes in aquaculture.

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Section: Therapeuticsmentioning

confidence: 99%

Antimicrobial Peptides from Fish

2014

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“…The synthesised peptide was dissolved in 0.1 M sterile PBS (pH 7.3), and its antimicrobial activities were monitored on the basis of minimum inhibitory concentrations (MICs). The inhibitory property of XLAsp-P2 on chloramphenicol-resistant Staphylococcus aureus RN4200, S. aureus ATCC29213, Staphylococcus sciuri ATCC29062, Rothia nasimurium ATCC19426, Aerococcus viridans ATCC700406, S. aureus ATCC25922, Escherichia coli BL21, Klebsiella pneumoniae ATCC23356 and Aeruginosus bacillus ATCC47085 was examined in accordance with standard protocols and clinical and laboratory standard institute guidelines [14], and with broth dilution method [15]. The microorganisms were grown for 18 h at 37°C on their respective media: E. coli and S. aureus in Mueller-Hinton (MH) broth, Candida albicans in YPD diluted to a cell final concentration of 10 5 colony-forming units (CFU) per millilitre.…”

Section: Antimicrobial Activity Assay and Bactericidal Kinetics Assaymentioning

confidence: 99%

Novel short antimicrobial peptide isolated fromXenopus laevisskin

Liu

Cheng

et al. 2017

J. Pept. Sci.

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A rich source of bioactive peptides, including a large number of antimicrobial peptides, has been found in amphibian skin. In this study, a novel short antimicrobial peptide was purified from Xenopus laevis skin and characterised through reversed-phase high-performance liquid chromatography, Edman degradation and matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. The peptide was composed of six amino acids with a sequence of DEDLDE and thus named X. laevis antibacterial peptide-P2 (XLAsp-P2). Transmission electron microscopy revealed that this peptide showed potential antimicrobial abilities against bacteria by damaging the bacterial cell membrane. XLAsp-P2 maybe inhibit bacterial growth by binding to the microbial genomic DNA. The peptide also exhibited a weak haemolytic activity against rabbit red blood cells. Therefore, XLAsp-P2 is a novel short anionic antibacterial peptide with broad activities. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

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“…This strain is resistant to ampicillin, methicillin, oxacillin, and ciprofloxacin. The culture and quantification were performed as previously described [21, 22]. …”

Section: Methodsmentioning

confidence: 99%

Antimicrobial peptide Epinecidin-1 promotes complete skin regeneration of methicillin-resistant Staphylococcus aureus-infected burn wounds in a swine model

Huang

Pan

et al. 2017

Oncotarget

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This report shows that the antimicrobial peptide (AMP) Epinecidin-1 (Epi-1) efficiently heals MRSA-infected heat burn injuries and provides protection from infection in a pig model. The presence of an optimal level of Epi-1 induces cell proliferation by promoting cell cycle progression through an increase in S-phase cells. Epi-1 also induces proliferation to cover the wounded region in an in vitro cell proliferation assay using immortalized human epithelial HaCaT cells. Next, the in vivo wound healing efficiency of Epi-1 was tested in heat-burned pig skin infected with MRSA under in vivo conditions. Treatment of the injury with Epi-1 for 1 h at six hours post-infection completely healed the wound within 25 days. Conversely, the injury in the untreated control was not healed 25 days post-infection. Histological staining of wound sections with H&E showed that Epi-1 enhanced vascularization and increased epithelial activities in the wound region. Neutrophil recruitment to the wounded region in the Epi-1-treated sections was visualized by Giemsa staining. Additionally, Masson's trichrome staining of wound sections confirmed that Epi-1 enhanced extracellular collagen compound formation. The induction of sepsis-associated blood C-reactive protein (CRP) and the pro-inflammatory cytokine IL-6 in response to MRSA infection was also suppressed in pigs that received Epi-1. Taken together, the results demonstrate that the biomaterial Epi-1 heals wounds through increasing epithelial cell proliferation, vascularization, and the formation of collagen and controls MRSA infection-mediated sepsis in pigs.

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Evaluation of the epinecidin-1 peptide as an active ingredient in cleaning solutions against pathogens

Cited by 21 publications

References 30 publications

Antimicrobial Peptides from Fish

Antimicrobial Peptides from Fish

Novel short antimicrobial peptide isolated fromXenopus laevisskin

Antimicrobial peptide Epinecidin-1 promotes complete skin regeneration of methicillin-resistant Staphylococcus aureus-infected burn wounds in a swine model

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