Facile constructed meroterpenoids with novel hexadecahydroacephenanthrylene carbon skeleton using the biotransformation and chemical synthesis method.

IF 4.7 2区医学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Bioorganic Chemistry Pub Date : 2024-12-01 Epub Date: 2024-10-06 DOI:10.1016/j.bioorg.2024.107871

Die Yan, Binglin Chang, Qingcui Li, Yuqian Tang, Jingxin He, Yena Liu, Hui Cui

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Abstract

Bioaspermeroterpenoid A (1), the first meroterpenoid with an unprecedented hexadecahydroacephenanthrylene carbon skeleton, together with two analogues bioaspermeroterpenoids B and C (2 and 3) were co-isolated from the biotransformation extract of aspermeroterpene C by the fungus Penicillium herquei GZU-31-6. On the other hand, bioaspermeroterpenoid Aa (1a) featuring the same hexadecahydroacephenanthrylene carbon skeleton was synthesized from the precursor aspermeroterpene C by the nucleophilic addition reaction in the presence of CH₃ONa. Furthermore, bioaspermeroterpenoids A and C showed good inhibitory activities against lipopolysaccharide (LPS)-induced nitric oxide (NO) production in RAW 264.7 cells with IC₅₀ values of 26.08 and 7.50 µM, respectively, compared to the positive control (Indomethacin, IC₅₀ 24.1 µM). Especially, bioaspermeroterpenoids A and C also significantly suppressed the protein expression of iNOS and COX-2 at the concentration of 12.5 μM.

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用生物转化和化学合成法简便构建具有新型十六氢菲碳骨架的美拉特萜类化合物。

通过真菌 Penicillium herquei GZU-31-6，从天冬萜 C 的生物转化提取物中共同分离出了生物天冬萜 A（1）、生物天冬萜 B 和生物天冬萜 C 的两个类似物（2 和 3）。另一方面，在 CH3ONa 的存在下，通过亲核加成反应，从前体天冬萜 C 合成了具有相同十六氢杂菲碳架的生物天冬萜 Aa（1a）。此外，与阳性对照（吲哚美辛，IC50 24.1 µM）相比，生物高分子萜 A 和 C 对 RAW 264.7 细胞中脂多糖（LPS）诱导的一氧化氮（NO）产生具有良好的抑制活性，IC50 值分别为 26.08 µM 和 7.50 µM。特别是，在 12.5 μM 的浓度下，生物萜 A 和 C 还能显著抑制 iNOS 和 COX-2 的蛋白表达。

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来源期刊

Bioorganic Chemistry 生物-生化与分子生物学

CiteScore

9.70

自引率

3.90%

发文量

679

审稿时长

31 days

期刊介绍： Bioorganic Chemistry publishes research that addresses biological questions at the molecular level, using organic chemistry and principles of physical organic chemistry. The scope of the journal covers a range of topics at the organic chemistry-biology interface, including: enzyme catalysis, biotransformation and enzyme inhibition; nucleic acids chemistry; medicinal chemistry; natural product chemistry, natural product synthesis and natural product biosynthesis; antimicrobial agents; lipid and peptide chemistry; biophysical chemistry; biological probes; bio-orthogonal chemistry and biomimetic chemistry. For manuscripts dealing with synthetic bioactive compounds, the Journal requires that the molecular target of the compounds described must be known, and must be demonstrated experimentally in the manuscript. For studies involving natural products, if the molecular target is unknown, some data beyond simple cell-based toxicity studies to provide insight into the mechanism of action is required. Studies supported by molecular docking are welcome, but must be supported by experimental data. The Journal does not consider manuscripts that are purely theoretical or computational in nature. The Journal publishes regular articles, short communications and reviews. Reviews are normally invited by Editors or Editorial Board members. Authors of unsolicited reviews should first contact an Editor or Editorial Board member to determine whether the proposed article is within the scope of the Journal.