Structural Diversity and Biological Activity of Cyanopeptolins Produced by Nostoc edaphicum CCNP1411-Reference-Cited by-同舟云学术

Structural Diversity and Biological Activity of Cyanopeptolins Produced by Nostoc edaphicum CCNP1411

Published:2023-09-26 Issue:10 Volume:21 Page:508
ISSN:1660-3397
Container-title:Marine Drugs
language:en
Short-container-title:Marine Drugs

Author:

Konkel Robert¹^ORCID,Cegłowska Marta²^ORCID,Szubert Karolina¹,Wieczerzak Ewa³^ORCID,Iliakopoulou Sofia⁴^ORCID,Kaloudis Triantafyllos⁵⁶^ORCID,Mazur-Marzec Hanna¹^ORCID

Affiliation:

1. Department of Marine Biology and Biotechnology, Faculty of Oceanography and Geography, University of Gdańsk, PL-81378 Gdynia, Poland

2. Institute of Oceanology, Polish Academy of Sciences, Powstańców Warszawy 55, PL-81712 Sopot, Poland

3. Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, PL-80308 Gdańsk, Poland

4. Department of Sustainable Agriculture, University of Patras, GR-30131 Agrinio, Greece

5. Institute of Nanoscience & Nanotechnology, NCSR Demokritos, GR-15310 Agia Paraskevi, Greece

6. Laboratory of Organic Micropollutants, Water Quality Control Department, EYDAP SA, Menidi, GR-13674 Athens, Greece

Abstract

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.

Funder

National Science Centre in Poland

Institute of Oceanology, PAN

STSM

Publisher

MDPI AG

Subject

Drug Discovery,Pharmacology, Toxicology and Pharmaceutics (miscellaneous),Pharmaceutical Science

Link

https://www.mdpi.com/1660-3397/21/10/508/pdf

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