Work

In silico Analysis of the Stability of Ribosomal Protein S1 from Various Strains of the Pathogenic Microorganism Staphylococcus aureus.

Year: 2024

Type: article

Abstract: The pathogenic microorganism Staphylococcus aureus, one of the representatives of the staphylococcus family, is capable of developing resistance to antibiotics and antiseptics. The largest ribosomal protein, S1, from S. aureus contains four structural S1 domains, and short peptides synthesized based on its sequence have amyloidogenic and antimicrobial properties (antimicrobial peptides). In this work, in silico analysis of all available ribosomal protein S1 sequences from various S. aureus strains allowed us to identify residues that are characteristic of specific strains. Based on data from the I-Mutant service, changes in the stability of ribosomal protein S1 from various S. aureus strains were predicted. The results obtained will be used in the future for targeted mutations in the design of new antimicrobial peptides based on ribosomal protein S1.

Source: Journal Biomed

DOI: 10.33647/2074-5982-20-3-32-36

Authors: O. V. Galzitskaya, A. V. Machulin, E. I. Deryusheva

Institutions: Russian Academy of Sciences, Institute of Theoretical and Experimental Biophysics, Institute of Protein Research, G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Scientific Center for Biological Research, Institute for Biological Instrumentation

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: diamond

OpenAlex ID: W4404338349

FWCI:

Cites: 4

Cited by:

Related to: 10