Discovery of Acyl-Surugamide A2 from Marine <i>Streptomyces albidoflavus</i> RKJM-0023—A New Cyclic Nonribosomal Peptide Containing an N-ε-acetyl-L-lysine Residue
Zacharie A. Maw,
Bradley Haltli,
Jason J. Guo,
Donna M. Baldisseri,
Christopher Cartmell,
Russell G. Kerr
Affiliations
Zacharie A. Maw
Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE C1A 4P3, Canada
Bradley Haltli
Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE C1A 4P3, Canada
Jason J. Guo
Department of Chemistry & Chemical Biology, Barnett Institute for Chemical and Biological Analysis, Northeastern University, Boston, MA 02115, USA
Donna M. Baldisseri
Bruker Biospin Corp., 15 Fortune Drive, Billerica, MA 01821, USA
Christopher Cartmell
Department of Pharmacology, Comprehensive Center for Pain & Addiction, College of Medicine, University of Arizona, Tucson, AZ 85724, USA
Russell G. Kerr
Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE C1A 4P3, Canada
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.
