Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor.
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| Autori principali: | , , , |
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| Natura: | Artículo científico |
| Lingua: | en |
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Marine drugs
2024
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| _version_ | 1868266277650300928 |
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| author | Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna |
| author_facet | Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna |
| collection | PubMed - marine biology |
| contents | Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor. Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna Serine Proteinase Inhibitors Aphanizomenon Thrombin Anticoagulants Cyanobacteria 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. |
| format | Artículo científico |
| id | pubmed_39590786 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Marine drugs |
| record_format | pubmed |
| spellingShingle | Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor. Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna Serine Proteinase Inhibitors Aphanizomenon Thrombin Anticoagulants Cyanobacteria Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor. Overlingė, Donata Cegłowska, Marta Konkel, Robert Mazur-Marzec, Hanna Serine Proteinase Inhibitors Aphanizomenon Thrombin Anticoagulants Cyanobacteria 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. |
| title | Aeruginosin 525 (AER525) from Cyanobacterium Sp. (KUCC C2): A New Serine Proteases Inhibitor. |
| topic | Serine Proteinase Inhibitors Aphanizomenon Thrombin Anticoagulants Cyanobacteria |
| url | https://pubmed.ncbi.nlm.nih.gov/39590786/ |