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

Sergey V Kravchenko,Elena Y Gorbunova,Alexey K Surin,Anna V Glyakina,Oxana V Galzitskaya,Alexander V Panfilov,Viacheslav N Azev,Sergei Y Grishin,Margarita I Kobyakova,Pavel A Domnin,Svetlana A Ermolaeva,Roman S Fadeev,Leila G Mustaeva

doi:10.3390/ijms23010524

Abstract

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.

Highlights

IntroductionIt is necessary to develop peptides that, under nearly physiological conditions in vitro (neutral pH, medium ionic strength, temperature 37 ◦ C), form ordered structures, since the ability to self-assemble is important for the manifestation of action of antimicrobial substances [10]
S1 proteins, we suggest that amyloidogenic propensity may significantly contribute to the antimicrobial effect of synthetic antimicrobial peptides [29]
We found that peptides synthesized based on the ribosomal S1 protein sequence from S. aureus have significant antimicrobial activity against Staphylococcus aureus, methicillin-resistant S. aureus (MRSA), Bacillus cereus, Escherichia coli, and Pseudomonas aeruginosa, and their antimicrobial effect is manifested at the level of the antibiotic gentamicin sulfate

Summary

Introduction

It is necessary to develop peptides that, under nearly physiological conditions in vitro (neutral pH, medium ionic strength, temperature 37 ◦ C), form ordered structures, since the ability to self-assemble is important for the manifestation of action of antimicrobial substances [10]. These properties are possessed by amyloidogenic peptides, some of which have been described as efficient antimicrobial agents [11,12,13]

Methods

Results

Conclusion