UCL School of Pharmacy, University College London, London WC1N 1AX, UK.
Department of Pharmacognosy, Faculty of Pharmacy, Umm Al-Qura University, Makkah 21955, Saudi Arabia.
Molecules. 2021 Oct 15;26(20):6229. doi: 10.3390/molecules26206229.
This study investigated the in vitro inhibitory potential of different solvent extracts of leaves of on key enzymes related to type 2 diabetes mellitus (α-glucosidase and α-amylase) in combination with an aggregation assay (using 0.01% Triton X-100 detergent) to assess the specificity of action. The methanol extract was the most active in inhibiting α-glucosidase and α-amylase, with IC values of 6.67 ± 0.30 and 25.62 ± 4.12 µg/mL, respectively. However, these activities were significantly attenuated in the presence of 0.01% Triton X-100. The chemical analysis of the methanol extract was conducted utilizing a dereplication approach combing LC-ESI-MS/MS and database searching. The chemical analysis detected 27 major peaks in the negative ion mode, and 24 phenolic compounds, predominantly tannins and flavonol glycosides derivatives, were tentatively identified. Our data indicate that the enzyme inhibitory activity was probably due to aggregation-based inhibition, perhaps linked to polyphenols.
本研究调查了不同溶剂提取物对 2 型糖尿病相关关键酶(α-葡萄糖苷酶和α-淀粉酶)的体外抑制潜力,并结合聚集测定(使用 0.01% Triton X-100 清洁剂)来评估作用的特异性。甲醇提取物对α-葡萄糖苷酶和α-淀粉酶的抑制活性最强,IC 值分别为 6.67 ± 0.30 和 25.62 ± 4.12 µg/mL。然而,在 0.01% Triton X-100 的存在下,这些活性显著减弱。甲醇提取物的化学成分分析采用结合 LC-ESI-MS/MS 和数据库搜索的去重复方法进行。负离子模式下检测到 27 个主要峰,初步鉴定出 24 种酚类化合物,主要为单宁和黄酮醇糖苷衍生物。我们的数据表明,酶抑制活性可能归因于基于聚集的抑制,可能与多酚有关。