Meroterpenoids Isolated from <i>Avicennia marina</i> Fruit Fungal Strain Aspergillus sp.

High Resolution Image Download MS PowerPoint Slide 3 new diisoprenyl cyclohexene-type meroterpenoids, aspergienynes R -T ( 1 – 3 ), one new natural product ( 9 ), and six known compounds ( 4–8 and 10 ), were obtained from Avicennia marina (Forssk.) Vierh. fruit fungal strain Aspergillus sp. YLNU-Q11. These new compounds’ structures were elucidated using spectroscopic analyses, NMR/DP4+ calculations, and ECD studies. In the acetylcholinesterase (AChE) inhibitory assay, compound 8 showed moderate inhibitory activity (IC 50 = 9.54 μM). Further molecular docking analysis suggested that hydrogen bonding interactions with residues TYR374, GLY79, and GLY150 are crucial for the binding of 8 to AChE.

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Publication Details

Journal
ACS Omega
Published
2026-06-25
DOI
https://doi.org/10.1021/acsomega.5c12372
Primary Topic
Microbial Natural Products and Biosynthesis
Type
article
Field-Weighted Citation Impact
0.00

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article

Meroterpenoids Isolated from Avicennia marina Fruit Fungal Strain Aspergillus sp.

Fan‐Fan Wang, Jiwen Wu, Pingfang Tao, Zhongqing Wen et al.
ACS Omega
Microbial Natural Products and Biosynthesis
article

Meroterpenoids Isolated from Avicennia marina Fruit Fungal Strain Aspergillus sp.

Fan‐Fan Wang, Jiwen Wu, Pingfang Tao, Zhongqing Wen, Xiaoxia Liu, Feng Qin, Jingjing Tao, Li-Ping Mo, Xin-Xiu Nong, Xuefeng Jin
article en

Abstract

High Resolution Image Download MS PowerPoint Slide 3 new diisoprenyl cyclohexene-type meroterpenoids, aspergienynes R -T ( 1 – 3 ), one new natural product ( 9 ), and six known compounds ( 4–8 and 10 ), were obtained from Avicennia marina (Forssk.) Vierh. fruit fungal strain Aspergillus sp. YLNU-Q11. These new compounds’ structures were elucidated using spectroscopic analyses, NMR/DP4+ calculations, and ECD studies. In the acetylcholinesterase (AChE) inhibitory assay, compound 8 showed moderate inhibitory activity (IC 50 = 9.54 μM). Further molecular docking analysis suggested that hydrogen bonding interactions with residues TYR374, GLY79, and GLY150 are crucial for the binding of 8 to AChE.

ACS Omega
Guangxi University (CN), Yulin Normal University (CN), The People's Hospital of Guangxi Zhuang Autonomous Region (CN)
Natural Science Foundation of Guangxi Zhuang Autonomous Region
Life below water
Openalex Percentile: Top 9%
Microbial Natural Products and Biosynthesis
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