Rapid screening of α-amylase inhibitors from Aloe vera based on polydopamine/L-cysteine bifunctionalized magnetic mesoporous silica immobilized α-amylase

IF 3.8 2区化学 Q1 BIOCHEMICAL RESEARCH METHODS

Analytical and Bioanalytical Chemistry Pub Date : 2025-03-25 DOI:10.1007/s00216-025-05841-z

Lei Wang, Yue Li, Sikai Wang, Lin Lv, Hongmei Liu, Guoqi Zhang, Yan Zhao

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引用次数: 0

Abstract

Diabetes mellitus is a metabolic disorder that impacts millions of individuals globally. In the treatment of this condition, it is imperative to explore natural resources for therapeutic agents that exhibit fewer adverse effects and enhanced efficacy. Currently, the methods employed for isolating anti-diabetic lead compounds from natural sources are often intricate and time-consuming. Therefore, there is an urgent need to develop efficient and rapid screening techniques. In this study, α-amylase was immobilized using a novel polydopamine/L-cysteine bifunctionalized magnetic mesoporous silica composite material (Fe₃O₄@nSiO₂@mSiO₂@PDA@L-Cys) for the first time. A ligand fishing approach utilizing the immobilized α-amylase was developed to rapidly screen for α-amylase inhibitors from Aloe vera. Characterization and property analysis of the immobilized enzyme showed that the immobilized α-amylase exhibited exceptional stability and reusability. Two ligands were successfully screened from Aloe vera and then characterized as aloin B and aloin A using ultra-high performance liquid chromatography tandem mass spectrometry. Their respective IC₅₀ values were 0.99 ± 0.09 mM and 1.14 ± 0.05 mM. Molecular docking studies confirmed the interaction of both ligands with specific amino acid residues within the active site of α-amylase. The study presents a fast and efficient approach for screening α-amylase inhibitors from intricate natural sources, thereby offering significant potential for the development of anti-diabetic agents.

Graphical Abstract

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基于聚多巴胺/ l -半胱氨酸双功能化磁性介孔二氧化硅固定α-淀粉酶的芦荟α-淀粉酶抑制剂的快速筛选。

糖尿病是一种影响全球数百万人的代谢紊乱。在这种情况的治疗中，迫切需要探索自然资源，寻找副作用少、疗效高的治疗剂。目前，从天然来源中分离抗糖尿病先导化合物的方法往往复杂且耗时。因此，迫切需要开发高效、快速的筛选技术。本研究首次采用新型聚多巴胺/ l -半胱氨酸双功能化磁性介孔硅复合材料（Fe3O4@nSiO2@mSiO2@PDA@ l -cys）固定化α-淀粉酶。为了快速筛选芦荟中α-淀粉酶抑制剂，建立了固定化α-淀粉酶的配体捕捞方法。对固定化α-淀粉酶的表征和性能分析表明，固定化α-淀粉酶具有良好的稳定性和可重复使用性。从芦荟中成功筛选出两种配体，并利用超高效液相色谱-串联质谱法对其进行鉴定，分别为芦荟素B和芦荟素A。它们的IC50值分别为0.99±0.09 mM和1.14±0.05 mM。分子对接研究证实了这两种配体与α-淀粉酶活性位点内特定氨基酸残基的相互作用。该研究为从复杂的天然来源中筛选α-淀粉酶抑制剂提供了一种快速有效的方法，从而为开发抗糖尿病药物提供了巨大的潜力。

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来源期刊

Analytical and Bioanalytical Chemistry 化学-分析化学

CiteScore

8.00

自引率

4.70%

发文量

638

审稿时长

2.1 months

期刊介绍： Analytical and Bioanalytical Chemistry’s mission is the rapid publication of excellent and high-impact research articles on fundamental and applied topics of analytical and bioanalytical measurement science. Its scope is broad, and ranges from novel measurement platforms and their characterization to multidisciplinary approaches that effectively address important scientific problems. The Editors encourage submissions presenting innovative analytical research in concept, instrumentation, methods, and/or applications, including: mass spectrometry, spectroscopy, and electroanalysis; advanced separations; analytical strategies in “-omics” and imaging, bioanalysis, and sampling; miniaturized devices, medical diagnostics, sensors; analytical characterization of nano- and biomaterials; chemometrics and advanced data analysis.