English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Antimicrobial peptides (AMPs), low-molecular-weight proteins with broad-spectrum antimicrobial activity, are the most promising candidates for the development of novel antimicrobials. A powerful cationic glycine-rich AMP YD1 (MW ~ 1.0 kDa) was purified from  Bacillus amyloliquefaciens CBSYD1  isolated from traditional Korean fermented food kimchi, for the treatment of multidrug-resistant (MDR) bacteria. Strain  CBSYD1  was identified 99.79% similar to  Bacillus amyloliquefaciens  subsp.  plantarum FZB42(T)  by 16S rRNA sequence analysis. The amino acid sequence residues of YD1 were determined to be Ala-Pro-Lys-Gly-Val-Gln-Gly-Pro-Asn-Gly by Edman degradation method. After the analysis and comparison of YD1 peptide sequence using several bioinformatic servers, peptide sequence has been considered to be unique. YD1 displayed antimicrobial activity against gram-positive and gram-negative bacteria. The minimal inhibitory concentrations (MIC) of YD1 for  Escherichia coli KCTC1923 (E. coli), methicillin - resistant Staphylococcus aureus B15 (MRSA) , and  vancomycin - resistant enterococci (VRE)  ranged from 8 to 64 µg/mL, representing greater potency than commercial reference antibiotics. The antimicrobial mechanism of YD1 was determined to involve cell-penetrating translocation inside the cell and interaction with the DNA leading ultimately to bacterial cell death. Analogously, Gly-Pro-Asn-Gly is the likely expected cell-penetrating motif for YD1. YD1 could be a promising antimicrobial agent for the clinical application.   Electronic supplementary material  The online version of this article (doi:10.1186/s13568-016-0315-8) contains supplementary material, which is available to authorized users.

Glycin-rich antimicrobial peptide YD1 from B. amyloliquefaciens, induced morphological alteration in and showed affinity for plasmid DNA of E. coli