To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities
Authors
Galzitskaya, O.V.Grishin, S.Yu.
Glyakina, A.V.
Slizen, M.V.
Panfilov, A.V.
Domnin, P.A.
Kochetov, A.P.
Surin, A.A
Kravchenko, S.V.
Surin, A.K.
Ermolaeva, S.A.
Contributors
Morić, Ivana![](/themes/Mirageimagine/images/orcid.png)
Đorđević, Valentina
![](/themes/Mirageimagine/images/orcid.png)
Conference object (Published version)
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© 2023 Institute of Molecular Genetics and Genetic Engineering, University of Belgrade
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One of the reasons for the mortal danger to humans is the ability of pathogenic bacteria
to form biofilms. The formation of biofilms is an evolutionarily conservative defense
mechanism against adverse conditions. The use of this protection by pathogenic bacteria
reduces the effectiveness of the main means of combating them - antibiotics, which
complicates the production of new types of drugs. There are two types of antimicrobial
agents that are not known antibiotics: nanoparticles and antimicrobial peptides. We
demonstrated that peptides synthesized based on the amino acid sequence of proteins
and capable of amyloid formation and coaggregation with the whole protein exhibit
antimicrobial activity. The ability of peptides to coaggregate with target proteins can help
combat biofilm-forming bacterial communities.
We evaluated the antimicrobial effects of ten synthesized hybrid peptides, which were
obtained based on the sequences of the S1 ribosomal protein of P. aeruginosa and ...S.
aureus. It is important that some peptides demonstrated high antimicrobial activity
comparable to the antibiotic gentamicin sulfate against pathogenic strains of MRSA, S.
aureus, and P. aeruginosa. These peptides showed no toxicity to eukaryotic cells. Our study
demonstrates the promise of hybrid peptides based on the amyloidogenic regions of the
S1 ribosomal protein for the development of new antimicrobials against Gram-positive
and Gram-negative bacteria resistant to traditional antibiotic.
Keywords:
amyloid / coaggregation / antimicrobial peptidesSource:
4th Belgrade Bioinformatics Conference, 2023, 4, 35-35Publisher:
- Belgrade : Institute of molecular genetics and genetic engineering
Funding / projects:
- This research was funded by the Russian science foundation, Grant Number 18-14-00321
Note:
- Belgrade : Institute of molecular genetics and genetic engineering
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Institution/Community
Institut za molekularnu genetiku i genetičko inženjerstvoTY - CONF AU - Galzitskaya, O.V. AU - Grishin, S.Yu. AU - Glyakina, A.V. AU - Slizen, M.V. AU - Panfilov, A.V. AU - Domnin, P.A. AU - Kochetov, A.P. AU - Surin, A.A AU - Kravchenko, S.V. AU - Surin, A.K. AU - Ermolaeva, S.A. PY - 2023 UR - https://belbi.bg.ac.rs/ UR - https://imagine.imgge.bg.ac.rs/handle/123456789/1970 AB - One of the reasons for the mortal danger to humans is the ability of pathogenic bacteria to form biofilms. The formation of biofilms is an evolutionarily conservative defense mechanism against adverse conditions. The use of this protection by pathogenic bacteria reduces the effectiveness of the main means of combating them - antibiotics, which complicates the production of new types of drugs. There are two types of antimicrobial agents that are not known antibiotics: nanoparticles and antimicrobial peptides. We demonstrated that peptides synthesized based on the amino acid sequence of proteins and capable of amyloid formation and coaggregation with the whole protein exhibit antimicrobial activity. The ability of peptides to coaggregate with target proteins can help combat biofilm-forming bacterial communities. We evaluated the antimicrobial effects of ten synthesized hybrid peptides, which were obtained based on the sequences of the S1 ribosomal protein of P. aeruginosa and S. aureus. It is important that some peptides demonstrated high antimicrobial activity comparable to the antibiotic gentamicin sulfate against pathogenic strains of MRSA, S. aureus, and P. aeruginosa. These peptides showed no toxicity to eukaryotic cells. Our study demonstrates the promise of hybrid peptides based on the amyloidogenic regions of the S1 ribosomal protein for the development of new antimicrobials against Gram-positive and Gram-negative bacteria resistant to traditional antibiotic. PB - Belgrade : Institute of molecular genetics and genetic engineering C3 - 4th Belgrade Bioinformatics Conference T1 - To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities EP - 35 SP - 35 VL - 4 UR - https://hdl.handle.net/21.15107/rcub_imagine_1970 ER -
@conference{ author = "Galzitskaya, O.V. and Grishin, S.Yu. and Glyakina, A.V. and Slizen, M.V. and Panfilov, A.V. and Domnin, P.A. and Kochetov, A.P. and Surin, A.A and Kravchenko, S.V. and Surin, A.K. and Ermolaeva, S.A.", year = "2023", abstract = "One of the reasons for the mortal danger to humans is the ability of pathogenic bacteria to form biofilms. The formation of biofilms is an evolutionarily conservative defense mechanism against adverse conditions. The use of this protection by pathogenic bacteria reduces the effectiveness of the main means of combating them - antibiotics, which complicates the production of new types of drugs. There are two types of antimicrobial agents that are not known antibiotics: nanoparticles and antimicrobial peptides. We demonstrated that peptides synthesized based on the amino acid sequence of proteins and capable of amyloid formation and coaggregation with the whole protein exhibit antimicrobial activity. The ability of peptides to coaggregate with target proteins can help combat biofilm-forming bacterial communities. We evaluated the antimicrobial effects of ten synthesized hybrid peptides, which were obtained based on the sequences of the S1 ribosomal protein of P. aeruginosa and S. aureus. It is important that some peptides demonstrated high antimicrobial activity comparable to the antibiotic gentamicin sulfate against pathogenic strains of MRSA, S. aureus, and P. aeruginosa. These peptides showed no toxicity to eukaryotic cells. Our study demonstrates the promise of hybrid peptides based on the amyloidogenic regions of the S1 ribosomal protein for the development of new antimicrobials against Gram-positive and Gram-negative bacteria resistant to traditional antibiotic.", publisher = "Belgrade : Institute of molecular genetics and genetic engineering", journal = "4th Belgrade Bioinformatics Conference", title = "To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities", pages = "35-35", volume = "4", url = "https://hdl.handle.net/21.15107/rcub_imagine_1970" }
Galzitskaya, O.V., Grishin, S.Yu., Glyakina, A.V., Slizen, M.V., Panfilov, A.V., Domnin, P.A., Kochetov, A.P., Surin, A.A, Kravchenko, S.V., Surin, A.K.,& Ermolaeva, S.A.. (2023). To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities. in 4th Belgrade Bioinformatics Conference Belgrade : Institute of molecular genetics and genetic engineering., 4, 35-35. https://hdl.handle.net/21.15107/rcub_imagine_1970
Galzitskaya O, Grishin S, Glyakina A, Slizen M, Panfilov A, Domnin P, Kochetov A, Surin A, Kravchenko S, Surin A, Ermolaeva S. To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities. in 4th Belgrade Bioinformatics Conference. 2023;4:35-35. https://hdl.handle.net/21.15107/rcub_imagine_1970 .
Galzitskaya, O.V., Grishin, S.Yu., Glyakina, A.V., Slizen, M.V., Panfilov, A.V., Domnin, P.A., Kochetov, A.P., Surin, A.A, Kravchenko, S.V., Surin, A.K., Ermolaeva, S.A., "To be folded, to be unfolded or to be aggregated with important functions: application of the directed coaggregation mechanism to combat bacterial communities" in 4th Belgrade Bioinformatics Conference, 4 (2023):35-35, https://hdl.handle.net/21.15107/rcub_imagine_1970 .