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Discovery of Acyl-Surugamide A2 from Marine Streptomyces albidoflavus RKJM-0023-A New Cyclic Nonribosomal Peptide Containing an N-ε-acetyl-L-lysine Residue.
Maw, Zacharie A; Haltli, Bradley; Guo, Jason J; Baldisseri, Donna M; Cartmell, Christopher; Kerr, Russell G.
Afiliação
  • Maw ZA; Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE C1A 4P3, Canada.
  • Haltli B; Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE C1A 4P3, Canada.
  • Guo JJ; Nautilus Biosciences, Croda Canada Limited, Charlottetown, PE C1A 4P3, Canada.
  • Baldisseri DM; Department of Chemistry & Chemical Biology, Barnett Institute for Chemical and Biological Analysis, Northeastern University, Boston, MA 02115, USA.
  • Cartmell C; Bruker Biospin Corp., 15 Fortune Drive, Billerica, MA 01821, USA.
  • Kerr RG; Department of Pharmacology, Comprehensive Center for Pain & Addiction, College of Medicine, University of Arizona, Tucson, AZ 85724, USA.
Molecules ; 29(7)2024 Mar 27.
Article em En | MEDLINE | ID: mdl-38611762
ABSTRACT
We report the discovery of a novel cyclic nonribosomal peptide (NRP), acyl-surugamide A2, from a marine-derived Streptomyces albidoflavus RKJM-0023 (CP133227). The structure of acyl-surugamide A2 was elucidated using a combination of NMR spectroscopy, MS2 fragmentation analysis, and comparative analysis of the sur biosynthetic gene cluster. Acyl-surugamide A2 contains all eight core amino acids of surugamide A, with a modified N-ε-acetyl-L-lysine residue. Our study highlights the potential of marine Streptomyces strains to produce novel natural products with potential therapeutic applications. The structure of cyclic peptides can be solved using MS2 spectra and analysis of their biosynthetic gene clusters.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Lisina Idioma: En Revista: Molecules Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Lisina Idioma: En Revista: Molecules Ano de publicação: 2024 Tipo de documento: Article