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Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.
Galzitskaya, Oxana V; Kurpe, Stanislav R; Panfilov, Alexander V; Glyakina, Anna V; Grishin, Sergei Y; Kochetov, Alexey P; Deryusheva, Evgeniya I; Machulin, Andrey V; Kravchenko, Sergey V; Domnin, Pavel A; Surin, Alexey K; Azev, Viacheslav N; Ermolaeva, Svetlana A.
Afiliación
  • Galzitskaya OV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Kurpe SR; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Panfilov AV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Glyakina AV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Grishin SY; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Kochetov AP; Institute of Mathematical Problems of Biology, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Deryusheva EI; Keldysh Institute of Applied Mathematics, Russian Academy of Sciences, 125047 Moscow, Russia.
  • Machulin AV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Kravchenko SV; The Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.
  • Domnin PA; Institute for Biological Instrumentation, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences", 142290 Pushchino, Russia.
  • Surin AK; Skryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Science", 142290 Pushchino, Russia.
  • Azev VN; Institute of Environmental and Agricultural Biology (X-BIO), Tyumen State University, 625003 Tyumen, Russia.
  • Ermolaeva SA; Gamaleya Research Centre of Epidemiology and Microbiology, 123098 Moscow, Russia.
Int J Mol Sci ; 23(10)2022 May 13.
Article en En | MEDLINE | ID: mdl-35628272
Antibiotic-resistant bacteria are recognized as one of the leading causes of death in the world. We proposed and successfully tested peptides with a new mechanism of antimicrobial action "protein silencing" based on directed co-aggregation. The amyloidogenic antimicrobial peptide (AAMP) interacts with the target protein of model or pathogenic bacteria and forms aggregates, thereby knocking out the protein from its working condition. In this review, we consider antimicrobial effects of the designed peptides on two model organisms, E. coli and T. thermophilus, and two pathogenic organisms, P. aeruginosa and S. aureus. We compare the amino acid composition of proteomes and especially S1 ribosomal proteins. Since this protein is inherent only in bacterial cells, it is a good target for studying the process of co-aggregation. This review presents a bioinformatics analysis of these proteins. We sum up all the peptides predicted as amyloidogenic by several programs and synthesized by us. For the four organisms we studied, we show how amyloidogenicity correlates with antibacterial properties. Let us especially dwell on peptides that have demonstrated themselves as AMPs for two pathogenic organisms that cause dangerous hospital infections, and in which the minimal inhibitory concentration (MIC) turned out to be comparable to the MIC of gentamicin sulfate. All this makes our study encouraging for the further development of AAMP. The hybrid peptides may thus provide a starting point for the antibacterial application of amyloidogenic peptides.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Catiónicos Antimicrobianos / Péptidos Antimicrobianos Tipo de estudio: Prognostic_studies Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Suiza
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Catiónicos Antimicrobianos / Péptidos Antimicrobianos Tipo de estudio: Prognostic_studies Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Suiza