OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria

Abstract 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 pept...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Shira Mandel, Janna Michaeli, Noa Nur, Isabelle Erbetti, Jonathan Zazoun, Livia Ferrari, Antonio Felici, Moshe Cohen-Kutner, Niv Bachnoff
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
R
Q
Acceso en línea:https://doaj.org/article/83a72ed367e14c80809b6afdced28df3
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:83a72ed367e14c80809b6afdced28df3
record_format dspace
spelling oai:doaj.org-article:83a72ed367e14c80809b6afdced28df32021-12-02T16:35:56ZOMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria10.1038/s41598-021-86155-92045-2322https://doaj.org/article/83a72ed367e14c80809b6afdced28df32021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86155-9https://doaj.org/toc/2045-2322Abstract 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.Shira MandelJanna MichaeliNoa NurIsabelle ErbettiJonathan ZazounLivia FerrariAntonio FeliciMoshe Cohen-KutnerNiv BachnoffNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Shira Mandel
Janna Michaeli
Noa Nur
Isabelle Erbetti
Jonathan Zazoun
Livia Ferrari
Antonio Felici
Moshe Cohen-Kutner
Niv Bachnoff
OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria
description Abstract 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 article
author Shira Mandel
Janna Michaeli
Noa Nur
Isabelle Erbetti
Jonathan Zazoun
Livia Ferrari
Antonio Felici
Moshe Cohen-Kutner
Niv Bachnoff
author_facet Shira Mandel
Janna Michaeli
Noa Nur
Isabelle Erbetti
Jonathan Zazoun
Livia Ferrari
Antonio Felici
Moshe Cohen-Kutner
Niv Bachnoff
author_sort Shira Mandel
title 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_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_sort omn6 a novel bioengineered peptide for the treatment of multidrug resistant gram negative bacteria
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/83a72ed367e14c80809b6afdced28df3
work_keys_str_mv AT shiramandel omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT jannamichaeli omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT noanur omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT isabelleerbetti omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT jonathanzazoun omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT liviaferrari omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT antoniofelici omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT moshecohenkutner omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
AT nivbachnoff omn6anovelbioengineeredpeptideforthetreatmentofmultidrugresistantgramnegativebacteria
_version_ 1718383702151528448