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

Autor: Vitale GA; Department of Eco-Sustainable Marine Biotechnology, Stazione Zoologica Anton Dohrn, Via A.F. Acton, Molosiglio, 80133 Naples, Italy., Scarpato S; Department of Pharmacy, University of Naples 'Federico II', 80131 Naples, Italy.; GEOMAR Centre for Marine Biotechnology (GEOMAR-Biotech), Research Unit Marine Natural Products Chemistry, GEOMAR Helmholtz Centre for Ocean Research Kiel, Am Kiel-Kanal 44, 24106 Kiel, Germany., Mangoni A; Department of Pharmacy, University of Naples 'Federico II', 80131 Naples, Italy., D'Auria MV; Department of Pharmacy, University of Naples 'Federico II', 80131 Naples, Italy., Della Sala G; Department of Eco-Sustainable Marine Biotechnology, Stazione Zoologica Anton Dohrn, Via A.F. Acton, Molosiglio, 80133 Naples, Italy., de Pascale D; Department of Eco-Sustainable Marine Biotechnology, Stazione Zoologica Anton Dohrn, Via A.F. Acton, Molosiglio, 80133 Naples, Italy.
Jazyk: angličtina
Zdroj: Marine drugs [Mar Drugs] 2023 Apr 21; Vol. 21 (4). Date of Electronic Publication: 2023 Apr 21.
DOI: 10.3390/md21040256
Abstrakt: 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 CO 2 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.
Databáze: MEDLINE