Academic Journal
Grifolamine A, a novel bis-γ-butyrolactone from Grifola frondosa exerted inhibitory effect on α-glucosidase and their binding interaction: Affinity and molecular dynamics simulation
| العنوان: | Grifolamine A, a novel bis-γ-butyrolactone from Grifola frondosa exerted inhibitory effect on α-glucosidase and their binding interaction: Affinity and molecular dynamics simulation |
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| المؤلفون: | Shaodan Chen, Zhenqiang Mu, Tianqiao Yong, Jiangyong Gu, Yifan Zhang, Xiong Gao, Yizhen Xie, Chun Xiao, Huiping Hu, Xiaobing Yang, Xiangmin Li, Manjun Cai, Qingping Wu |
| المصدر: | Current Research in Food Science, Vol 5, Iss , Pp 2045-2052 (2022) |
| بيانات النشر: | Elsevier, 2022. |
| سنة النشر: | 2022 |
| المجموعة: | LCC:Nutrition. Foods and food supply LCC:Food processing and manufacture |
| مصطلحات موضوعية: | Grifolamine A, Bis-γ-butyrolactone, α-glucosidase, Grifola frondosa, Absolute configuration, Surface plasmon resonance, Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456 |
| الوصف: | A novel bis-γ-butyrolactone grifolamine A (1), the first γ-butyrolactone dimer from nature, together with three known γ-butyrolactones (2–4), was isolated from the byproduct from Grifola frondosa polysaccharides preparation process. The structure and stereochemistry of grifolamine A (1) were elucidated by extensive spectroscopic analysis combined with quantum chemical calculation. The biosynthetic origin of compound 1, as well as 2–4 was proposed. Grifolamine A (1) showed an intense inhibition against α-glucosidase in vitro. The underlying inhibitory mechanism was revealed by surface plasmon resonance (SPR), molecular docking, molecular dynamics (MD) simulation and binding free energy calculation. SPR revealed that grifolamine A exhibited a strong affinity to α-glucosidase with an equilibrium dissociation constant (KD) value of 1.178 × 10−4 M. Molecular docking manifested that grifolamine A sat at the active pocket of α-glucosidase by van der Waals force, alkyl interaction and carbon hydrogen bonds, and consequently changed the micro-environmental structure of α-glucosidase. MD simulation revealed that grifolamine A had high binding affinity to α-glucosidase with average free energy of −25.2 ± 3.2 kcal/mol. Free energy decomposition indicated amino acid residues including PHE298, PHE308, PHE309, PHE155 and ARG310 at the binding pocket played a strongly positive effect on the interaction between grifolamine A and α-glucosidase. Our findings provide valuable information for the design and development of novel α-glucosidase inhibitors based on γ-butyrolactone skeleton. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2665-9271 |
| Relation: | http://www.sciencedirect.com/science/article/pii/S2665927122001964; https://doaj.org/toc/2665-9271 |
| DOI: | 10.1016/j.crfs.2022.10.026 |
| URL الوصول: | https://doaj.org/article/b5f067173c1447f98316b956f91d313d |
| رقم الانضمام: | edsdoj.b5f067173c1447f98316b956f91d313d |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 26659271 |
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| DOI: | 10.1016/j.crfs.2022.10.026 |