AI Article Synopsis
- Cyanopeptolins (CPs) are a common type of nonribosomal peptide found in cyanobacteria, known primarily for their ability to inhibit proteases.
- The study identified 93 distinct CPs from the cyanobacterial strain CCNP1411, including 79 new variants, characterized using mass spectrometry and NMR techniques.
- Biological assays revealed that a specific amino acid between Thr and Ahp plays a crucial role in the compounds' effectiveness against serine protease and HeLa cancer cells.
Article 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 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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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10608790 | PMC |
| http://dx.doi.org/10.3390/md21100508 | DOI Listing |
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