Cargando…
OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria
New antimicrobial agents are urgently needed, especially to eliminate multidrug resistant Gram-negative bacteria that stand for most antibiotic-resistant threats. In the following study, we present superior properties of an engineered antimicrobial peptide, OMN6, a 40-amino acid cyclic peptide based...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7988117/ https://www.ncbi.nlm.nih.gov/pubmed/33758343 http://dx.doi.org/10.1038/s41598-021-86155-9 |
_version_ | 1783668727580983296 |
---|---|
author | Mandel, Shira Michaeli, Janna Nur, Noa Erbetti, Isabelle Zazoun, Jonathan Ferrari, Livia Felici, Antonio Cohen-Kutner, Moshe Bachnoff, Niv |
author_facet | Mandel, Shira Michaeli, Janna Nur, Noa Erbetti, Isabelle Zazoun, Jonathan Ferrari, Livia Felici, Antonio Cohen-Kutner, Moshe Bachnoff, Niv |
author_sort | Mandel, Shira |
collection | PubMed |
description | New antimicrobial agents are urgently needed, especially to eliminate multidrug resistant Gram-negative bacteria that stand for most antibiotic-resistant threats. In the following study, we present superior properties of an engineered antimicrobial peptide, OMN6, a 40-amino acid cyclic peptide based on Cecropin A, that presents high efficacy against Gram-negative bacteria with a bactericidal mechanism of action. The target of OMN6 is assumed to be the bacterial membrane in contrast to small molecule-based agents which bind to a specific enzyme or bacterial site. Moreover, OMN6 mechanism of action is effective on Acinetobacter baumannii laboratory strains and clinical isolates, regardless of the bacteria genotype or resistance-phenotype, thus, is by orders-of-magnitude, less likely for mutation-driven development of resistance, recrudescence, or tolerance. OMN6 displays an increase in stability and a significant decrease in proteolytic degradation with full safety margin on erythrocytes and HEK293T cells. Taken together, these results strongly suggest that OMN6 is an efficient, stable, and non-toxic novel antimicrobial agent with the potential to become a therapy for humans. |
format | Online Article Text |
id | pubmed-7988117 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-79881172021-03-25 OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria Mandel, Shira Michaeli, Janna Nur, Noa Erbetti, Isabelle Zazoun, Jonathan Ferrari, Livia Felici, Antonio Cohen-Kutner, Moshe Bachnoff, Niv Sci Rep Article New antimicrobial agents are urgently needed, especially to eliminate multidrug resistant Gram-negative bacteria that stand for most antibiotic-resistant threats. In the following study, we present superior properties of an engineered antimicrobial peptide, OMN6, a 40-amino acid cyclic peptide based on Cecropin A, that presents high efficacy against Gram-negative bacteria with a bactericidal mechanism of action. The target of OMN6 is assumed to be the bacterial membrane in contrast to small molecule-based agents which bind to a specific enzyme or bacterial site. Moreover, OMN6 mechanism of action is effective on Acinetobacter baumannii laboratory strains and clinical isolates, regardless of the bacteria genotype or resistance-phenotype, thus, is by orders-of-magnitude, less likely for mutation-driven development of resistance, recrudescence, or tolerance. OMN6 displays an increase in stability and a significant decrease in proteolytic degradation with full safety margin on erythrocytes and HEK293T cells. Taken together, these results strongly suggest that OMN6 is an efficient, stable, and non-toxic novel antimicrobial agent with the potential to become a therapy for humans. Nature Publishing Group UK 2021-03-23 /pmc/articles/PMC7988117/ /pubmed/33758343 http://dx.doi.org/10.1038/s41598-021-86155-9 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Mandel, Shira Michaeli, Janna Nur, Noa Erbetti, Isabelle Zazoun, Jonathan Ferrari, Livia Felici, Antonio Cohen-Kutner, Moshe Bachnoff, Niv OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title | OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title_full | OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title_fullStr | OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title_full_unstemmed | OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title_short | OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria |
title_sort | omn6 a novel bioengineered peptide for the treatment of multidrug resistant gram negative bacteria |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7988117/ https://www.ncbi.nlm.nih.gov/pubmed/33758343 http://dx.doi.org/10.1038/s41598-021-86155-9 |
work_keys_str_mv | AT mandelshira omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT michaelijanna omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT nurnoa omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT erbettiisabelle omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT zazounjonathan omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT ferrarilivia omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT feliciantonio omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT cohenkutnermoshe omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria AT bachnoffniv omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria |