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

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.