期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 1, 页码 -出版社
MDPI
DOI: 10.3390/ijms23010524
关键词
ribosomal S1 protein; amyloid; antimicrobial peptides; Staphylococcus aureus; MRSA; cell-penetrating peptide; FoldAmyloid; AlphaFold 2
资金
- RUSSIAN SCIENCE FOUNDATION [18-14-00321]
- Russian Science Foundation [18-14-00321] Funding Source: Russian Science Foundation
The need to develop new antimicrobial peptides is essential due to the high resistance of pathogenic bacteria to traditional antibiotics. This study successfully creates hybrid antimicrobial peptides containing amyloidogenic regions of the ribosomal S1 protein, showing significant antimicrobial effects against both Gram-positive and Gram-negative bacteria.
The need to develop new antimicrobial peptides is due to the high resistance of pathogenic bacteria to traditional antibiotics now and in the future. The creation of synthetic peptide constructs is a common and successful approach to the development of new antimicrobial peptides. In this work, we use a simple, flexible, and scalable technique to create hybrid antimicrobial peptides containing amyloidogenic regions of the ribosomal S1 protein from Staphylococcus aureus. While the cell-penetrating peptide allows the peptide to enter the bacterial cell, the amyloidogenic site provides an antimicrobial effect by coaggregating with functional bacterial proteins. We have demonstrated the antimicrobial effects of the R23F, R23DI, and R23EI hybrid peptides against Staphylococcus aureus, methicillin-resistant S. aureus (MRSA), Pseudomonas aeruginosa, Escherichia coli, and Bacillus cereus. R23F, R23DI, and R23EI can be used as antimicrobial peptides against Gram-positive and Gram-negative bacteria resistant to traditional antibiotics.
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