从. 中分离得到的二萜生物碱的体外和计算研究。
In Vitro and In Silico Investigation of Diterpenoid Alkaloids Isolated from .
机构信息
Department of Pharmacy, Shaheed Benazir Bhutto University, Sheringal Dir (Upper) 18000, Khyber Pakhtunkhwa, Pakistan.
Department of Chemistry, University of Malakand, Chakdara Dir (Lower) 18550, Khyber Pakhtunkhwa, Pakistan.
出版信息
Molecules. 2022 Jul 7;27(14):4348. doi: 10.3390/molecules27144348.
This study reports the isolation of three new C diterpenoid alkaloids, Chitralinine A-C (-) from the aerial parts of . Their structures were established on the basis of latest spectral techniques and single crystal X-rays crystallographic studies of chitralinine A described basic skeleton of these compounds. All the isolated Compounds (-) showed strong, competitive type inhibition against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) in comparison to standard allanzanthane and galanthamine however, chitralinine-C remained the most potent with IC value of 11.64 ± 0.08 μM against AChE, and 24.31 ± 0.33 μM against BChE, respectively. The molecular docking reflected a binding free energy of -16.400 K Cal-mol for chitralinine-C, having strong interactions with active site residues, TYR334, ASP72, SER122, and SER200. The overall findings suggest that these new diterpenoid alkaloids could serve as lead drugs against dementia-related diseases including Alzheimer's disease.
本研究报告了三种新的 C 二萜生物碱，即 (-) 从 的地上部分分离出来。它们的结构是基于最新的光谱技术和对 chitralinine A 的单晶 X 射线晶体学研究建立的，描述了这些化合物的基本骨架。所有分离出的化合物 (-) 与标准的 allanzanthane 和 galanthamine 相比，对乙酰胆碱酯酶 (AChE) 和丁酰胆碱酯酶 (BChE) 表现出强烈的、竞争性抑制作用，但 chitralinine-C 的抑制作用最强，对 AChE 的 IC 值为 11.64 ± 0.08 μM，对 BChE 的 IC 值为 24.31 ± 0.33 μM。分子对接反映了 chitralinine-C 的结合自由能为-16.400 K Cal-mol，与活性位点残基 TYR334、ASP72、SER122 和 SER200 有很强的相互作用。总的来说，这些新的二萜生物碱可能可以作为治疗与痴呆相关疾病的药物，包括阿尔茨海默病。
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