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Structural Diversity and Biological Activity of Cyanopeptolins Produced by Nostoc edaphicum CCNP1411.
Konkel, Robert; Ceglowska, Marta; Szubert, Karolina; Wieczerzak, Ewa; Iliakopoulou, Sofia; Kaloudis, Triantafyllos; Mazur-Marzec, Hanna.
Affiliation
  • Konkel R; Department of Marine Biology and Biotechnology, Faculty of Oceanography and Geography, University of Gdansk, PL-81378 Gdynia, Poland.
  • Ceglowska M; Institute of Oceanology, Polish Academy of Sciences, Powstanców Warszawy 55, PL-81712 Sopot, Poland.
  • Szubert K; Department of Marine Biology and Biotechnology, Faculty of Oceanography and Geography, University of Gdansk, PL-81378 Gdynia, Poland.
  • Wieczerzak E; Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, PL-80308 Gdansk, Poland.
  • Iliakopoulou S; Department of Sustainable Agriculture, University of Patras, GR-30131 Agrinio, Greece.
  • Kaloudis T; Institute of Nanoscience & Nanotechnology, NCSR Demokritos, GR-15310 Agia Paraskevi, Greece.
  • Mazur-Marzec H; Laboratory of Organic Micropollutants, Water Quality Control Department, EYDAP SA, Menidi, GR-13674 Athens, Greece.
Mar Drugs ; 21(10)2023 Sep 26.
Article in En | MEDLINE | ID: mdl-37888443
Cyanopeptolins (CPs) are one of the most commonly occurring class of cyanobacterial nonribosomal peptides. For the majority of these compounds, protease inhibition has been reported. In the current work, the structural diversity of cyanopeptolins produced by Nostoc edaphicum CCNP1411 was explored. As a result, 93 CPs, including 79 new variants, were detected and structurally characterized based on their mass fragmentation spectra. CPs isolated in higher amounts were additionally characterized by NMR. To the best of our knowledge, this is the highest number of cyanopeptides found in one strain. The biological assays performed with the 34 isolated CPs confirmed the significance of the amino acid located between Thr and the unique 3-amino-6-hydroxy-2-piperidone (Ahp) on the activity of the compounds against serine protease and HeLa cancer cells.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Nostoc Language: En Journal: Mar Drugs Journal subject: BIOLOGIA / FARMACOLOGIA Year: 2023 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Nostoc Language: En Journal: Mar Drugs Journal subject: BIOLOGIA / FARMACOLOGIA Year: 2023 Document type: Article Affiliation country: Country of publication: