ArticleFolia microbiologica2017
Antimicrobial peptide isolated from Bacillus amyloliquefaciens K14 revitalizes its use in combinatorial drug therapy.
Article in Folia microbiologica, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- A Review on cLF36, a Novel Recombinant Antimicrobial Peptide-Derived Camel Lactoferrin.Probiotics and antimicrobial proteins · 2024Review
- Membrane-Active Cyclic Amphiphilic Peptides: Broad-Spectrum Antibacterial Activity Alone and in Combination with Antibiotics.Journal of medicinal chemistry · 2022Article
- Alternatives to Fight Vancomycin-ResistantAntibiotics (Basel, Switzerland) · 2021Review
- Biomedical Relevance of Novel Anticancer Peptides in the Sensitive Treatment of Cancer.Biomolecules · 2021Review
- Antimicrobial Peptides with Antibacterial Activity against Vancomycin-ResistantInternational journal of molecular sciences · 2021Review
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- Article
- Reduction of Oxidative Stress through Activating the Nrf2 mediated HO-1 Antioxidant Efficacy Signaling Pathway by MS15, an Antimicrobial Peptide fromAntioxidants (Basel, Switzerland) · 2020Article
- Evaluation of the Antibacterial Material Production in the Fermentation ofMarine drugs · 2020Article
- The Practical Potential of Bacilli and Their Enzymes for Industrial Production.Frontiers in microbiology · 2020Review
- Synergistic Antibacterial Activity of Designed Trp-Containing Antibacterial Peptides in Combination With Antibiotics Against Multidrug-ResistantFrontiers in microbiology · 2019Article
- Two novel cationic antifungal peptides isolated from Bacillus pumilus HN-10 and their inhibitory activity against Trichothecium roseum.World journal of microbiology & biotechnology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The present study was performed to evaluate the antibacterial activities of an antimicrobial peptide (CSpK14) and the synergies thereof with β-lactams against vancomycin-resistant Staphylococcus aureus (VRSA) and Enterococci (VRE). Our strain was isolated from fermented food (kimchi), which is 99.79 % homologous with Bacillus amyloliquefaciens subsp. plantarum FZB42(T). CSpK14 was purified to homogeneity by diammonium sulfate precipitation, concentration, dialysis, and followed by two-stage chromatographic separation, i.e., Sepharose Cl-6B and Sephadex G-25 chromatography, and had a molar mass of ~4.6 kDa via Tricine SDS-PAGE and in situ examination. It was stable at pH 6.0-11.5 and temperature up to 80 °C. In addition, it was also stable with various metal ions, solvents, and proteases. The N-terminal amino acid sequence was H-Y-D-P-G-D-D-S-G-N-T-G and did not show any significant homology with reported peptides. However, it shows some degrees of identity with alpha-2-macroglobulin and ligand-gated channel protein from different microorganisms. CSpK14 significantly reduced the minimum inhibitory concentrations (MICs) of β-lactams and had no effect on non-β-lactams against VRSA and VRE. MICs of CSpK14/oxacillin and CSpK14/ampicillin were reduced by 8- to 64-fold and 2- to 16-fold, respectively. The time killing assay between CSpK14/oxacillin (2.29-2.37 Δlog
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.