Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein from Staphylococcus aureus

• Published in: International journal of molecular sciences Vol. 23; no. 1; p. 524
• Main Authors: Kravchenko, Sergey V, Domnin, Pavel A, Grishin, Sergei Y, Panfilov, Alexander V, Azev, Viacheslav N, Mustaeva, Leila G, Gorbunova, Elena Y, Kobyakova, Margarita I, Surin, Alexey K, Glyakina, Anna V, Fadeev, Roman S, Ermolaeva, Svetlana A, Galzitskaya, Oxana V
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 04-01-2022; MDPI
• Subjects: Algorithms; Amino Acid Sequence; Amino acids; amyloid; Amyloidogenesis; Amyloidogenic Proteins - chemistry; Antibiotics; Antiinfectives and antibacterials; Antimicrobial agents; Antimicrobial Cationic Peptides - chemical synthesis; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - pharmacology; Antimicrobial peptides; Antimicrobial Peptides - chemical synthesis; Antimicrobial Peptides - chemistry; Antimicrobial Peptides - pharmacology; Bacteria; Bacterial infections; Bacterial Proteins - chemistry; Cell Survival - drug effects; cell-penetrating peptide; Cell-Penetrating Peptides - chemical synthesis; Cell-Penetrating Peptides - chemistry; Cell-Penetrating Peptides - pharmacology; Dose-Response Relationship, Drug; Drug resistance; E coli; Fibroblasts; Gram-negative bacteria; Gram-positive bacteria; High resistance; Humans; Methicillin; Methicillin-Resistant Staphylococcus aureus - drug effects; Microbial Sensitivity Tests; Microorganisms; Models, Molecular; MRSA; Peptides; Physiology; Protein Conformation; Protein Interaction Domains and Motifs; Proteins; Pseudomonas aeruginosa; Ribosomal Proteins - chemistry; ribosomal S1 protein; Staphylococcus aureus; Staphylococcus aureus - drug effects; Staphylococcus infections; amyloid; ribosomal S1 protein; AlphaFold 2; MRSA; FoldAmyloid; cell-penetrating peptide; Staphylococcus aureus; antimicrobial peptides
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms23010524

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
. 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
, methicillin-resistant
(MRSA),
,
, and
. R23F, R23DI, and R23EI can be used as antimicrobial peptides against Gram-positive and Gram-negative bacteria resistant to traditional antibiotics.