用 L-酪氨酸处理的棘皮兰细胞培养物的非靶向代谢组学分析

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS
Miguel Aguilar-Camacho, Carlos E. Gómez-Sánchez, Abraham Cruz-Mendívil, Diego A Luna-Vital, José A Guerrero-Analco, Juan L. Monribot-Villanueva, Janet A. Gutiérrez-Uribe
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引用次数: 0

摘要

添加酪氨酸(Tyr)等前体可以提高植物细胞悬浮液的生物量和特殊代谢物的产量。需要对α-淀粉酶和α-葡萄糖苷酶具有抑制活性的天然化合物,以减少肠道对简单碳水化合物的吸收。以前曾有报道称,棘皮果中的可溶性黑色素能抑制α-葡萄糖苷酶的酶活性。因此,本研究的目的是分析用不同浓度的 Tyr 处理棘皮果细胞悬浮液时的代谢组谱,并评估细胞提取物对 α 淀粉酶和 α 葡萄糖苷酶的抑制活性。棘尾蛙细胞悬浮液的甲醇提取物(1 mg/mL)对α-淀粉酶活性的抑制作用与阿卡波糖(50 µM)相似。然而,没有观察到提取物对 α-葡萄糖苷酶的抑制作用。需要进一步纯化甲醇提取物,以防止化合物产生拮抗作用。通过层次聚类和主成分分析,确定了四种特定的化学特征。半乳糖代谢和淀粉/蔗糖代谢是主要的调节代谢途径。分子对接显示,化合物 Tyr_100 和 200 处理的自由结合能估计为 -2.4 至 -5.6 kcal/mol,可与与α-淀粉酶催化活性有关的关键氨基酸相互作用。向棘尾蛙细胞悬浮液中添加 Tyr 可用于生产α-淀粉酶抑制提取物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Untargeted metabolomic analysis of Randia echinocarpa cell cultures treated with L-Tyrosine

Untargeted metabolomic analysis of Randia echinocarpa cell cultures treated with L-Tyrosine

The addition of precursors, like tyrosine (Tyr), can increase the biomass and specialized metabolite production in plant cell suspensions. There is a need for natural compounds with inhibitory activity against α-amylase and α-glucosidase to decrease the intestinal absorption of simple carbohydrates. It has been previously reported that soluble melanins from the Randia echinocarpa fruit inhibit the enzymatic activity of α-glucosidase. Thus, the objective of this study was to analyze the metabolomic profiles of R. echinocarpa cell suspensions when treated with different concentrations of Tyr and to assess the inhibitory activities of the cell extracts against α-amylase and α-glucosidase. Methanolic extracts (1 mg/mL) of R. echinocarpa cell suspensions inhibited the activity of α-amylase similarly to acarbose at 50 µM. Nevertheless, no inhibition of α-glucosidase by the extracts was observed. Further purification of the methanolic extracts is required to prevent antagonist effects of the compounds. Four specific chemical profiles were determined by Hierarchical Cluster and Principal Components Analysis. Galactose metabolism and starch/sucrose metabolism were among the main modulated metabolic pathways. Molecular docking showed that compounds Tyr_100 and 200 treatments had an estimated free binding energy of -2.4 to -5.6 kcal/mol and can interact with key amino acids involved with the catalytic activity of α-amylase. The addition of Tyr to the cell suspensions of R. echinocarpa can be used to produce α-amylase inhibitory extracts.

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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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