Enhanced Molecular Networking Shows Microbacterium sp. V1 as a Factory of Antioxidant Proline-Rich Peptides

Mar Drugs. 2023 Apr 21;21(4):256. doi: 10.3390/md21040256.

Abstract

Two linear proline-rich peptides (1-2), bearing an N-terminal pyroglutamate, were isolated from the marine bacterium Microbacterium sp. V1, associated with the marine sponge Petrosia ficiformis, collected in the volcanic CO2 vents in Ischia Island (South Italy). Peptide production was triggered at low temperature following the one strain many compounds (OSMAC) method. Both peptides were detected together with other peptides (3-8) via an integrated, untargeted MS/MS-based molecular networking and cheminformatic approach. The planar structure of the peptides was determined by extensive 1D and 2D NMR and HR-MS analysis, and the stereochemistry of the aminoacyl residues was inferred by Marfey's analysis. Peptides 1-8 are likely to arise from Microbacterium V1 tailor-made proteolysis of tryptone. Peptides 1 and 2 were shown to display antioxidant properties in the ferric-reducing antioxidant power (FRAP) assay.

Keywords: OSMAC; antioxidant; bioactive peptides; marine bacteria; molecular networking; proline-rich peptides; structure elucidation.

MeSH terms

  • Animals
  • Antioxidants*
  • Bacteria
  • Microbacterium
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides
  • Peptides, Cyclic* / chemistry
  • Proline
  • Tandem Mass Spectrometry

Substances

  • Antioxidants
  • Peptides, Cyclic
  • Proline
  • Peptides