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| Main Authors: | , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Marine life science & technology
2025
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| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41322256/ |
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| _version_ | 1868266119877361665 |
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| author | Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming |
| author_facet | Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming |
| collection | PubMed - marine biology |
| contents | Antibacterial dimeric phenazine derivatives from a marine-derived sp. OUCMDZ-4923. Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming Phenazine derivatives, a class of naturally occurring antibiotics primarily produced by bacteria, are regarded as promising scaffolds for developing new antibiotics. In this study, eight new dimeric phenazine derivatives, phenazostains K‒R (‒), along with two reported dimeric analogues, phenazostains B () and C (), were isolated from the fermentation broth of the marine-derived sp. OUCMDZ-4923. Their structures were elucidated through spectroscopic analysis, primarily using NMR and HRESIMS spectra, ECD calculations, and the modified Mosher's method. Compounds ‒ feature the 12-deoxysaphenate unit linked to various sites on methyl saphenate, phenazine, or methyl phenazine-1-carboxylate. Notably, compounds and represent the first dimeric phenazines linked by a 12,12'-oxy bridge. Our experimental results suggest that these dimers could be formed from methyl saphenate () through a nonenzymatic pathway. Moreover, the analysis of gene roles within their biosynthetic gene cluster revealed that phenazostains ‒ are formed through a nonenzymatic process. Additionally, all dimers were evaluated for their antibacterial activity; compounds , ‒, and exhibited inhibitory activities against both and its methicillin-resistant strain (MRSA), with MIC values ranging from 1.56 to 25.0 μg/mL. The online version contains supplementary material available at 10.1007/s42995-025-00328-3. |
| format | Artículo científico |
| id | pubmed_41322256 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Marine life science & technology |
| record_format | pubmed |
| spellingShingle | Antibacterial dimeric phenazine derivatives from a marine-derived sp. OUCMDZ-4923. Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming Antibacterial dimeric phenazine derivatives from a marine-derived sp. OUCMDZ-4923. Wang, Dongyang Liu, Peipei Xia, Yuwei Wang, Liping Li, Ning Zhu, Weiming Phenazine derivatives, a class of naturally occurring antibiotics primarily produced by bacteria, are regarded as promising scaffolds for developing new antibiotics. In this study, eight new dimeric phenazine derivatives, phenazostains K‒R (‒), along with two reported dimeric analogues, phenazostains B () and C (), were isolated from the fermentation broth of the marine-derived sp. OUCMDZ-4923. Their structures were elucidated through spectroscopic analysis, primarily using NMR and HRESIMS spectra, ECD calculations, and the modified Mosher's method. Compounds ‒ feature the 12-deoxysaphenate unit linked to various sites on methyl saphenate, phenazine, or methyl phenazine-1-carboxylate. Notably, compounds and represent the first dimeric phenazines linked by a 12,12'-oxy bridge. Our experimental results suggest that these dimers could be formed from methyl saphenate () through a nonenzymatic pathway. Moreover, the analysis of gene roles within their biosynthetic gene cluster revealed that phenazostains ‒ are formed through a nonenzymatic process. Additionally, all dimers were evaluated for their antibacterial activity; compounds , ‒, and exhibited inhibitory activities against both and its methicillin-resistant strain (MRSA), with MIC values ranging from 1.56 to 25.0 μg/mL. The online version contains supplementary material available at 10.1007/s42995-025-00328-3. |
| title | Antibacterial dimeric phenazine derivatives from a marine-derived sp. OUCMDZ-4923. |
| url | https://pubmed.ncbi.nlm.nih.gov/41322256/ |