α-Glucosidase
(Synonyms: α-葡萄糖苷酶; α-D-Glucosidase) 目录号 : GC63270
α-葡萄糖苷酶是一种碳水化合物水解酶，催化从底物的非还原端释放α-葡萄糖苷酶。
Cas No.:9001-42-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
α-Glucosidase is a carbohydrate hydrolase that catalyzes the release of alpha-glucosidase from the non-reducing end of the substrate. Inhibition of α-Glucosidase is an effective method for non-insulin-dependent diabetes mellitus (NIDDM) [1-2]. Partial or complete deficiency of alpha-glucosidase can cause Pompe disease[3-4].
References:
[1]. Kumar S, Narwal S,et,al. α-glucosidase inhibitors from plants: A natural approach to treat diabetes. Pharmacogn Rev. 2011 Jan;5(9):19-29. doi: 10.4103/0973-7847.79096. PMID: 22096315; PMCID: PMC3210010.
[2]. van de Laar FA, Lucassen PL, ,et,al. Alpha-glucosidase inhibitors for patients with type 2 diabetes: results from a Cochrane systematic review and meta-analysis. Diabetes Care. 2005 Jan;28(1):154-63. doi: 10.2337/diacare.28.1.154. PMID: 15616251.
[3]. Kohler L, Puertollano R, ,et,al. Pompe Disease: From Basic Science to Therapy. Neurotherapeutics. 2018 Oct;15(4):928-942. doi: 10.1007/s13311-018-0655-y. PMID: 30117059; PMCID: PMC6277280.
[4]. Morales A, Anilkumar AC. Glycogen Storage Disease Type II. [Updated 2023 Aug 8]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2023 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK470558/
α-葡萄糖苷酶是一种碳水化合物水解酶，催化从底物的非还原端释放α-葡萄糖苷酶。抑制α-葡萄糖苷酶是治疗非胰岛素依赖型糖尿病(NIDDM)的有效方法[1-2]。部分或完全缺乏α -葡萄糖苷酶可引起Pompe病[3-4]。
| Cas No. | 9001-42-7 | SDF | |
| 别名 | α-葡萄糖苷酶; α-D-Glucosidase | ||
| 分子式 | 分子量 | ||
| 溶解度 | 储存条件 | Store at 2-8°C,protect from light | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Identification of raloxifene as a novel α-Glucosidase inhibitor using a systematic drug repurposing approach in combination with cross molecular docking-based virtual screening and experimental verification
Carbohydr Res 2022 Jan;511:108478.PMID:34801925DOI:10.1016/j.carres.2021.108478.
α-Glucosidase is a promising target for the treatment of diabetes. Drug repurposing can increase the chances of discovering an active inhibitor. Therefore, this study aimed to identify potential α-Glucosidase inhibitor using drug repurposing and in silico strategies. We identified critical amino acid residues of the three α-Glucosidase proteins. Based on cross molecular docking studies of three α-Glucosidase proteins and drugs in the FDA database, we screened hits with the favorable binding affinities and modes targeting the three proteins. Subsequently, an in vitro activity assay showed that raloxifene was an excellent inhibitor of α-Glucosidase. Moreover, molecular dynamics simulations of raloxifene and three proteins were performed to assess the stability of the protein-hit systems in physiological conditions and clarify protein-hit interactions. We also performed the binding free energy calculation, Hirshfeld surface and alanine scanning mutagenesis analyses. These results demonstrated that binding between raloxifene and the three proteins was stable, and the critical amino acid residues of the three proteins formed stable contacts with raloxifene. The molecular mechanisms agree well with its activity, reinforcing that raloxifene is a candidate α-Glucosidase inhibitor. Our study smoothes the path for the development of novel a-glucosidase inhibitors with high efficacy and low toxicity for the treatment of diabetes.
Antioxidant, Acetylcholinesterase, Butyrylcholinesterase, and α-Glucosidase Inhibitory Activities of Corchorus depressus
Pharmacogn Mag 2017 Oct-Dec;13(52):647-651.PMID:29200727DOI:10.4103/pm.pm_95_17.
Background: Corchorus depressus (Cd) commonly known as Boa-phalee belonging to the family Tiliaceae having 50 genera and 450 species. Cd is not among the studied medicinal agent despite its potential in ethnopharmacology. Objectives: The present study investigated antioxidant, acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-Glucosidase inhibitory activities of Cd. The dichloromethane and methanolic extracts of the Cd were evaluated for biological activities such as antioxidant and enzyme inhibitory activities of AChE, BChE, and α-Glucosidase. Materials and methods: Antioxidant activity was evaluated by measuring free radical scavenging potential of Cd using 1,1-diphenyl-2-picrylhydrazyl. Enzyme inhibition activities were done by measuring optical density. Results: The methanol extract of roots of Cd showed potential free radical scavenging activity 99% at concentration 16.1 μg/ml. AChE was inhibited by aerial part of dichloromethane fraction by 46.07% ± 0.45% while dichloromethane extracts of roots of Cd possessed significant activity against BChE with 86% inhibition compared with standard drug Eserine at concentration 0.5 mg/ml. The dichloromethane extract of roots of Cd showed 79% inhibition against α-Glucosidase enzyme activity with IC50 62.8 ± 1.5 μg/ml. Conclusion: These findings suggest Cd as useful therapeutic option as antioxidant and inhibition of AChE, BChE, and α-Glucosidase activities. Summary: The aerial parts and roots of Corchorus depressus (Cd) were extracted in dichloromethane and methanolThe extract of roots of Cd showed free radical scavenging activity 99% at concentration 16.1 mg/ml, Ach inhibition by aerial parts of dichloromethane fraction by 46.07%, and 79% inhibition against a-glucosidase enzyme activity with IC50 62.8 ± 1.5 mg/mlThe dichloromethane and methanolic extracts of Cd exhibited antioxidant inhibition of acetyl cholinesterase, butyrylcholinesterase, and a-glucosidase activities. Abbreviations used: DPPH: 1,1-diphenyl-2-picrylhydrazyl, Cd: Corchorus depressus, AChE: Acetylcholinesterase, BChE: Butyrylcholinesterase, AD: Alzheimer's disease.
PTP1B and α-Glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Phytochemistry 2022 May;197:113100.PMID:35144153DOI:10.1016/j.phytochem.2022.113100.
In this study, we present the first investigation of Hedera rhombea Bean fruit, which led to the isolation of six undescribed compounds including two megastigmane glucosides, two rare 1,4-dioxane neolignanes, and two quinic acid derivatives, together with 26 known compounds. Their structures and absolute configurations were elucidated by extensive analysis of NMR spectroscopic data, HRMS, and ECD calculations. This is the first report on the isolation of methyl 3-O-caffeoyl-5-O-p-coumaroylquinate from a natural source. Among the isolated compounds, falcarindiol and caffeoyltryptophan showed significant PTP1B inhibition with IC50 values of 7.32 and 16.99 μM, respectively, compared to those of the positive controls [sodium orthovanadate (IC50 = 17.96 μM) and ursolic acid (IC50 = 4.53 μM)]. These two compounds along with several other compounds displayed significant α-Glucosidase inhibitions with IC50 values ranging from 12.88 to 91.89 μM, stronger than that of the positive control (acarbose, IC50 = 298.07 μM). Enzyme kinetic analysis indicated that caffeoyltryptophan and falcarindiol displayed competitive and mixed-type PTP1B inhibition, respectively, whereas the α-Glucosidase inhibition type was mixed-type for caffeoyltryptophan and uncompetitive (rarely reported for a-glucosidase inhibitors) for falcarindiol. In addition, molecular docking results showed that these active compounds exhibited good binding affinities toward both PTP1B and α-Glucosidase with negative binding energies. The results of the present study demonstrate that these active compounds might be beneficial in the treatment of type 2 diabetes.
Identification of major α-Glucosidase inhibitors in Radix Astragali and its human microsomal metabolites using ultrafiltration HPLC-DAD-MS(n.)
J Pharm Biomed Anal 2015 Feb;104:31-7.PMID:25474715DOI:10.1016/j.jpba.2014.09.029.
Radix Astragali is one of the most popular traditional medicinal herbs with α-Glucosidase inhibitory activity, however, more comprehensive information regarding α-Glucosidase inhibition of Radix Astragali and its metabolites is yet unknown. Here, an ultrafiltration HPLC-DAD-MS(n) was developed to rapidly and selectively screen and identify major α-Glucosidase ligands from Radix Astragali and its human microsomal metabolites. The developed method showed high selectivity and specificity to directly screen α-Glucosidase ligands from complex system by testing mixtures of positive ((+)-catechin) and negative (salicylic acid) controls in the optimized conditions. As a result, thirteen prototype isoflavonoids and one monohydroxylated metabolic isoflavonoid with α-Glucosidase binding activity were observed. Their structures were elucidated by combination of high-resolution MS, linear ion trap MS(n), in-source collision-induced dissociation (CID) fragmentation and NMR data. Particularly, except for calycosin and formononetin, the other twelve isoflavonoids were found as new α-Glucosidase ligands. The activity of eight aglycones among fourteen ligands (glycosides were almost deglycosylated in vivo) was evaluated and confirmed using in vitro enzymatic assay. The results indicated that the proposed ultrafiltration HPLC-DAD-MS(n) method was a powerful tool for the discovery of α-Glucosidase inhibitors from complex matrix, and these findings would enhance understanding of the real biochemical profiles of Radix Astragali.
Pistagremic acid, a glucosidase inhibitor from Pistacia integerrima
Fitoterapia 2012 Dec;83(8):1648-52.PMID:23022534DOI:10.1016/j.fitote.2012.09.017.
Pistacia integerrima Stewart in traditionally used as folk remedy for various pathological conditions including diabetes. In order to identify the bioactive compound responsible for its folk use in diabetes, a phytochemical and biological study was conducted. Pistagremic acid (PA) was isolated from the dried galls extract of P. integerrima. Strong α-Glucosidase inhibitory potential of PA was predicted using its molecular docking simulations against yeast α-Glucosidase as a therapeutic target. Significant experimental α-Glucosidase inhibitory activity of PA confirmed the computational predictions. PA showed potent enzyme inhibitory activity both against yeast (IC(50): 89.12±0.12μM) and rat intestinal (IC(50): 62.47±0.09μM) α-glucosidases. Interestingly, acarbose was found to be more than 12 times more potent an inhibitor against mammalian (rat intestinal) enzyme (having IC(50) value 62.47±0.09μM), as compared to the microbial (yeast) enzyme (with IC(50) value 780.21μM). Molecular binding mode was explored via molecular docking simulations, which revealed hydrogen bonding interactions between PA and important amino acid residues (Asp60, Arg69 and Asp 70 (3.11Å)), surrounding the catalytic site of the α-Glucosidase. These interactions could be mainly responsible for their role in potent inhibitory activity of PA. PA has a strong potential to be further investigated as a new lead compound for better management of diabetes.