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Peptoid-Peptide Hybrid Analogs of the Enterococcus faecalis Fsr Auto-Inducing Peptide (AIP) Reveal Crucial Structure-Activity Relationships.
McBrayer, Dominic N; Ghosh, Uttam; Lella, Muralikrishna; Cameron, Crissey D; Tal-Gan, Yftah.
Afiliación
  • McBrayer DN; Department of Chemistry, University of Nevada, Reno, 1664 N. Virginia Street, Reno, NV-89557, USA.
  • Ghosh U; Department of Chemistry, University of Nevada, Reno, 1664 N. Virginia Street, Reno, NV-89557, USA.
  • Lella M; Department of Chemistry, University of Nevada, Reno, 1664 N. Virginia Street, Reno, NV-89557, USA.
  • Cameron CD; Department of Chemistry, University of Nevada, Reno, 1664 N. Virginia Street, Reno, NV-89557, USA.
  • Tal-Gan Y; Department of Chemistry, University of Nevada, Reno, 1664 N. Virginia Street, Reno, NV-89557, USA.
Chembiochem ; 24(1): e202200527, 2023 01 03.
Article en En | MEDLINE | ID: mdl-36376247
As multidrug-resistant bacteria become a more pressing risk to human health, alternate approaches to treating bacterial infections are being increasingly investigated. Enterococcus faecalis is an opportunistic pathogen responsible for a large percentage of secondary enterococci infections. Its pathogenicity has been shown to be largely dependent on a cell-density communication mechanism, termed quorum sensing. In this study, we conducted a systematic investigation of the lactone-containing macrocyclic signaling peptide used by E. faecalis for Fsr-mediated communication, termed gelatinase biosynthesis activating pheromone (GBAP). Specifically, through a combination of the on-resin sub-monomer and solution phase peptoid building block synthesis approaches, we successfully synthesized a library of peptoid-peptide hybrid analogs of GBAP and determined the biological effects associated with the introduction of the peptoid (N-alkyl glycine derivative) modifications. Within the macrocycle region of the peptide, as have been seen with other modifications, the F7 site was unusually tolerant toward peptoid modification, compared with other macrocyclic sites. Interestingly, within the exocyclic tail, peptoid modification at the N2 site completely abolished activity, a first for a single tail modification.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enterococcus faecalis / Peptoides Límite: Humans Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enterococcus faecalis / Peptoides Límite: Humans Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos