Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor.

Mar Drugs

Department of Marine Biology and Biotechnology, University of Gdańsk, M. J. Piłsudskiego 46, PL-81378 Gdynia, Poland.

Published: November 2024

Aeruginosins (AERs) are one of the most common classes of cyanobacterial peptides synthesised through a hybrid non-ribosomal peptide synthase/polyketide synthase pathway. They have been found in , , /, and The presence of AER in isolated from the Curonian Lagoon was reported for the first time in our previous work. Here, the structure of aeruginosin 525 (AER525), isolated from sp. KUCC C2, was characterised based on high-resolution mass spectrometry. This new AER variant shows potent activity against thrombin. It also inhibits trypsin and carboxypeptidase A but has no effect on elastase and chymotrypsin. In terms of the -terminal residue and biological activity, AER525 displaces some similarity to dysinosins, which belongs to the most potent inhibitors of thrombin among AERs. The findings underline the potential of AER525 as a new anticoagulant agent.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11595689PMC
http://dx.doi.org/10.3390/md22110506DOI Listing

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Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor.

Mar Drugs

November 2024

Department of Marine Biology and Biotechnology, University of Gdańsk, M. J. Piłsudskiego 46, PL-81378 Gdynia, Poland.

Aeruginosins (AERs) are one of the most common classes of cyanobacterial peptides synthesised through a hybrid non-ribosomal peptide synthase/polyketide synthase pathway. They have been found in , , /, and The presence of AER in isolated from the Curonian Lagoon was reported for the first time in our previous work. Here, the structure of aeruginosin 525 (AER525), isolated from sp.

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