Displaying publications 1 - 20 of 33 in total

Abstract:
Sort:
  1. α-glucosidase inhibitors isolated from Mimosa pudica L
    Tasnuva ST, Qamar UA, Ghafoor K, Sahena F, Jahurul MHA, Rukshana AH, et al.
    Nat Prod Res, 2019 May;33(10):1495-1499.
    PMID: 29281898 DOI: 10.1080/14786419.2017.1419224
    The aim of the study was to isolate digestive enzymes inhibitors from Mimosa pudica through a bioassay-guided fractionation approach. Repeated silica gel and sephadex LH 20 column chromatographies of bioactive fractions afforded stigmasterol, quercetin and avicularin as digestive enzymes inhibitors whose IC50 values as compared to acarbose (351.02 ± 1.46 μg mL-1) were found to be as 91.08 ± 1.54, 75.16 ± 0.92 and 481.7 ± 0.703 μg mL-1, respectively. In conclusion, M. pudica could be a good and safe source of digestive enzymes inhibitors for the management of diabetes in future.
    Matched MeSH terms: Acarbose/pharmacology
  2. Fulltext Triazoloquinazolines as a new class of potent α-glucosidase inhibitors: in vitro evaluation and docking study
    Abuelizz HA, Anouar EH, Ahmad R, Azman NIIN, Marzouk M, Al-Salahi R
    PLoS One, 2019;14(8):e0220379.
    PMID: 31412050 DOI: 10.1371/journal.pone.0220379
    Previously, we synthesized triazoloquinazolines 1-14 and characterized their structure. In this study, we aimed to evaluate the in vitro activity of the targets 1-14 as α-glucosidase inhibitors using α-glucosidase enzyme from Saccharomyces cerevisiae type 1. Among the tested compounds, triazoloquinazolines 14, 8, 4, 5, and 3 showed the highest inhibitory activity (IC50 = 12.70 ± 1.87, 28.54 ± 1.22, 45.65 ± 4.28, 72.28 ± 4.67, and 83.87 ± 5.12 μM, respectively) in relation to that of acarbose (IC50 = 143.54 ± 2.08 μM) as a reference drug. Triazoloquinazolines were identified herein as a new class of potent α-glucosidase inhibitors. Molecular docking results envisaged the plausible binding interaction between the target triazoloquinazolines and α-glucosidase enzyme and indicated considerable interaction with the active site residues.
    Matched MeSH terms: Acarbose
  3. Treatment Options for Patients with Type 2 Diabetes Mellitus during the Fasting Month of Ramadan
    Loh HH, Kamaruddin NA
    Ann Acad Med Singap, 2020 Jul;49(7):468-476.
    PMID: 33000110
    During Ramadan, Muslims fast from sunrise (Sahur) to sunset (Iftar) and are required to abstain from food and fluids, including oral and injectable medications. Patients with diabetes who fast during Ramadan are at risk of developing hyperglycemia with increased risk of ketoacidosis, hypoglycemia, dehydration and thrombosis. Pre-Ramadan education and preparation of a fasting patient are essential to reduce severe complications. This review paper summarizes studies to date on oral and injectable medications available for patients with type 2 diabetes during Ramadan fasting, as well as recommendations on management of these patients during Ramadan. Although there is limited data on the use of Metformin, Acarbose and Thiazolidinedione in Ramadan, they appear to be safe. Sulphonylurea, especially Glibenclamide, is associated with higher risk of hypoglycemia during Ramadan fasting, hence may need adjustment in dosing and timing. The incretin group and SGLT2 inhibitor use during Ramadan fasting is associated with low risk of hypoglycemia with no increased adverse events. Insulin regimes need to be individualized for patients who fast during Ramadan.
    Matched MeSH terms: Acarbose
  4. Synthesis, α-amylase inhibitory potential and molecular docking study of indole derivatives
    Taha M, Baharudin MS, Ismail NH, Imran S, Khan MN, Rahim F, et al.
    Bioorg Chem, 2018 10;80:36-42.
    PMID: 29864686 DOI: 10.1016/j.bioorg.2018.05.021
    In search of potent α-amylase inhibitor we have synthesized eighteen indole analogs (1-18), characterized by NMR and HR-EIMS and screened for α-amylase inhibitory activity. All analogs exhibited a variable degree of α-amylase inhibition with IC50 values ranging between 2.031 ± 0.11 and 2.633 ± 0.05 μM when compared with standard acarbose having IC50 values 1.927 ± 0.17 μM. All compounds showed good α-amylase inhibition. Compound 14 was found to be the most potent analog among the series. Structure-activity relationship has been established for all compounds mainly based on bringing about the difference of substituents on phenyl ring. To understand the binding interaction of the most active analogs molecular docking study was performed.
    Matched MeSH terms: Acarbose
  5. Synthesis, in vitro evaluation and molecular docking studies of thiazole derivatives as new inhibitors of α-glucosidase
    Rahim F, Ullah H, Javid MT, Wadood A, Taha M, Ashraf M, et al.
    Bioorg Chem, 2015 Oct;62:15-21.
    PMID: 26162519 DOI: 10.1016/j.bioorg.2015.06.006
    A series of thiazole derivatives 1-21 were prepared, characterized by EI-MS and (1)H NMR and evaluated for α-glucosidase inhibitory potential. All twenty one derivatives showed good α-glucosidase inhibitory activity with IC50 value ranging between 18.23±0.03 and 424.41±0.94μM when compared with the standard acarbose (IC50, 38.25±0.12μM). Compound (8) (IC50, 18.23±0.03μM) and compound (7) (IC50=36.75±0.05μM) exhibited outstanding inhibitory potential much better than the standard acarbose (IC50, 38.25±0.12μM). All other analogs also showed good to moderate enzyme inhibition. Molecular docking studies were carried out in order to find the binding affinity of thiazole derivatives with enzyme. Studies showed these thiazole analogs as a new class of α-glucosidase inhibitors.
    Matched MeSH terms: Acarbose/pharmacology
  6. Synthesis, in vitro evaluation and molecular docking studies of biscoumarin thiourea as a new inhibitor of α-glucosidases
    Zawawi NK, Taha M, Ahmat N, Ismail NH, Wadood A, Rahim F, et al.
    Bioorg Chem, 2015 Dec;63:36-44.
    PMID: 26432614 DOI: 10.1016/j.bioorg.2015.09.004
    Biscoumarin analogs 1-18 have been synthesized, characterized by EI-MS and (1)H NMR and evaluated for α-glucosidase inhibitory potential. All compounds showed variety of α-glucosidase inhibitory potential ranging in between 13.5±0.39 and 104.62±0.3μM when compared with standard acarbose having IC50 value 774.5±1.94μM. The binding interactions of the most active analogs were confirmed through molecular docking. The compounds showed very good interactions with enzyme. All synthesized compounds 1-18 are new. Our synthesized compounds can further be studied to developed lead compounds.
    Matched MeSH terms: Acarbose
  7. Synthesis, in vitro alpha-glucosidase inhibitory potential of benzimidazole bearing bis-Schiff bases and their molecular docking study
    Rahim F, Zaman K, Taha M, Ullah H, Ghufran M, Wadood A, et al.
    Bioorg Chem, 2020 01;94:103394.
    PMID: 31699396 DOI: 10.1016/j.bioorg.2019.103394
    Voglibose and acarbose are distinguished α-glucosidase inhibitors used for controlling of diabetes mellitus. Unfortunately, these distinguished and clinically used inhibitors have also numerous side effects. Subsequently, there is still needed to develop safer therapy. Despite of a broad spectrum of biological importance of benzimidazole, it is occasionally evaluated for α-glucosidase activity. Current study deals with the synthesis and biological screening of benzimidazole bearing bis-Schiff bases (1-19) for their α-glucosidase inhibitory activity. All analogues exhibited excellent to good inhibitory potential (IC50 = 2.20 ± 0.1to 88.60 ± 1.70 µM) when compared with standard drug acarbose (IC50 = 38.45 ± 0.80 µM). A structure activity relationship has been established on the basis of electronic effects and position of different substituents present on phenyl ring. In order to rationalize the binding interactions of most active analogues with the active site of α-glucosidase enzyme, molecular docking study was conducted.
    Matched MeSH terms: Acarbose
  8. Fulltext Synthesis, biological activity and molecular docking of new tricyclic series as α-glucosidase inhibitors
    Abuelizz HA, Iwana NANI, Ahmad R, Anouar EH, Marzouk M, Al-Salahi R
    BMC Chem, 2019 Dec;13(1):52.
    PMID: 31384800 DOI: 10.1186/s13065-019-0560-4
    Diabetes is an emerging metabolic disorder. α-Glucosidase inhibitors, such as acarbose, delay the hydrolysis of carbohydrates by interfering with the digestive enzymes. This action decreases the glucose absorption and the postprandial glucose level. We have synthesized 25 tricyclic 2-phenoxypyrido[3,2-e][1,2,4]triazolo[1,5-a]pyrimidin-5(4H)-ones hybrids and evaluated their α-glucosidase inhibitory activity. Compounds 6h and 6d have shown stronger activity than that of acarbose. Compound 6h exhibited the highest inhibition with an IC50 of 104.07 µM. Molecular modelling studies revealed that compound 6h inhibits α-glucosidase due to the formation of a stable ligand-α-glucosidase complex and extra hydrogen bond interactions, and directed in the binding site by Trp329.25 tricyclic 2-phenoxypyrido[3,2-e][1,2,4]triazolo[1,5-a]pyrimidin-5(4H)-ones hybrids have been synthesized and evaluated their α-glucosidase inhibitory activity. Compounds 6h have shown stronger activity than that of acarbose.
    Matched MeSH terms: Acarbose
  9. Synthesis of new indazole based dual inhibitors of α-glucosidase and α-amylase enzymes, their in vitro, in silico and kinetics studies
    Rafique R, Khan KM, Arshia, Kanwal, Chigurupati S, Wadood A, et al.
    Bioorg Chem, 2020 01;94:103195.
    PMID: 31451297 DOI: 10.1016/j.bioorg.2019.103195
    The current study describes the discovery of novel inhibitors of α-glucosidase and α-amylase enzymes. For that purpose, new hybrid analogs of N-hydrazinecarbothioamide substituted indazoles 4-18 were synthesized and fully characterized by EI-MS, FAB-MS, HRFAB-MS, 1H-, and 13C NMR spectroscopic techniques. Stereochemistry of the imine double bond was established by NOESY measurements. All derivatives 4-18 with their intermediates 1-3, were evaluated for in vitro α-glucosidase and α-amylase enzyme inhibition. It is worth mentioning that all synthetic compounds showed good inhibition potential in the range of 1.54 ± 0.02-4.89 ± 0.02 µM for α-glucosidase and for α-amylase 1.42 ± 0.04-4.5 ± 0.18 µM in comparison with the standard acarbose (IC50 value of 1.36 ± 0.01 µM). In silico studies were carried out to rationalize the mode of binding interaction of ligands with the active site of enzymes. Moreover, enzyme inhibitory kinetic characterization was also performed to understand the mechanism of enzyme inhibition.
    Matched MeSH terms: Acarbose
  10. Fulltext Synthesis of Novel Triazinoindole-Based Thiourea Hybrid: A Study on α-Glucosidase Inhibitors and Their Molecular Docking
    Taha M, Alshamrani FJ, Rahim F, Hayat S, Ullah H, Zaman K, et al.
    Molecules, 2019 Oct 23;24(21).
    PMID: 31652777 DOI: 10.3390/molecules24213819
    A new class of triazinoindole-bearing thiosemicarbazides (1-25) was synthesized and evaluated for α-glucosidase inhibitory potential. All synthesized analogs exhibited excellent inhibitory potential, with IC50 values ranging from 1.30 ± 0.01 to 35.80 ± 0.80 µM when compared to standard acarbose (an IC50 value of 38.60 ± 0.20 µM). Among the series, analogs 1 and 23 were found to be the most potent, with IC50 values of 1.30 ± 0.05 and 1.30 ± 0.01 µM, respectively. The structure-activity relationship (SAR) was mainly based upon bringing about different substituents on the phenyl rings. To confirm the binding interactions, a molecular docking study was performed.
    Matched MeSH terms: Acarbose
  11. Synthesis of Bis-indolylmethane sulfonohydrazides derivatives as potent α-Glucosidase inhibitors
    Gollapalli M, Taha M, Ullah H, Nawaz M, AlMuqarrabun LMR, Rahim F, et al.
    Bioorg Chem, 2018 10;80:112-120.
    PMID: 29894890 DOI: 10.1016/j.bioorg.2018.06.001
    In search of better α-glucosidase inhibitors, a series of bis-indolylmethane sulfonohydrazides derivatives (1-14) were synthesized and evaluated for their α-glucosidase inhibitory potential. All derivatives exhibited outstanding α-glucosidase inhibition with IC50 values ranging between 0.10 ± 0.05 to 5.1 ± 0.05 μM when compared with standard drug acarbose having IC50 value 856.28 ± 3.15 μM. Among the series, analog 7 (0.10 ± 0.05 μM) with tri-chloro substitution on phenyl ring was identified as the most potent inhibitor of α-glucosidase (∼ 8500 times). The structure activity relationship has been also established. Molecular docking studies were also performed to help understand the binding interaction of the most active analogs with receptors. From the docking studies, it was observed that all the active bis-indolylmethane sulfonohydrazides derivatives showed considerable binding interactions within the active site (acarbose inhibition site) of α-glucosidase. We also evaluated toxicity of all derivatives and found none of them are toxic.
    Matched MeSH terms: Acarbose
  12. Selection, purification, and evaluation of acarbose-an α-glucosidase inhibitor from Actinoplanes sp
    Tuyen DT, Yew GY, Cuong NT, Hoang LT, Yen HT, Hong Thao PT, et al.
    Chemosphere, 2021 Feb;265:129167.
    PMID: 33307502 DOI: 10.1016/j.chemosphere.2020.129167
    Actinoplanes sp. A1094 strain had been selected for its high production of acarbose from 20 different strains of Actinoplanes sp. can be found in wild. The content for glucosidase inhibitor of acarbose concentration was recorded at 1.12 g/L. The conducted analysis of 16S rRNA sequence of Actinoplanes sp. A1094 showed 99% similar identity to the corresponding sequence of Actinoplanes hulinensis. Acarbose was purified from Actinoplanes hulinensis 1094 with a yield of 8.48%, purity of 98% and further identified by LC/MS and NMR methods (C25H43NO18; m/z: 645.6 g/mol). The purified acarbose was used to evaluate the hypoglycemia in streptozotocin (STZ)-induced diabetic mice model. The purified acarbose reduced postprandial blood glucose level in comparison with Glucobay® as medication for control type 2 diabetes in a combination therapy. Notably, the outcomes of native acarbose on fasting blood glucose levels in mice resemble akin to the commercial product and the acarbose accumulating fermentation and metabolic engineering from the cell gene in which would reduce in production cost. Therefore, acarbose from Actinoplanes hulinensis 1094 could be potentially used to make products for the treatment of type II diabetes.
    Matched MeSH terms: Acarbose
  13. Proposed molecular mechanism of non-competitive inhibition using molecular dynamics simulations between α-glucosidase enzyme and mangostin compound as antidiabetic
    Maulana AF, Maksum IP, Sriwidodo S, Rukayadi Y
    J Mol Model, 2024 Apr 18;30(5):136.
    PMID: 38634946 DOI: 10.1007/s00894-024-05934-z
    CONTEXT: Further understanding of the molecular mechanisms is necessary since it is important for designing new drugs. This study aimed to understand the molecular mechanisms involved in the design of drugs that are inhibitors of the α-glucosidase enzyme. This research aims to gain further understanding of the molecular mechanisms underlying antidiabetic drug design. The molecular docking process yielded 4 compounds with the best affinity energy, including γ-Mangostin, 1,6-dimethyl-ester-3-isomangostin, 1,3,6-trimethyl-ester-α-mangostin, and 3,6,7-trimethyl-ester-γ-mangostin. Free energy calculation with molecular mechanics with generalized born and surface area solvation indicated that the 3,6,7-trimethyl-γ-mangostin had a better free energy value compared to acarbose and simulated maltose together with 3,6,7-trimethyl-γ-mangostin compound. Based on the analysis of electrostatic, van der Waals, and intermolecular hydrogen interactions, 3,6,7-trimethyl-γ-mangostin adopts a noncompetitive inhibition mechanism, whereas acarbose adopts a competitive inhibition mechanism. Consequently, 3,6,7-trimethyl-ester-γ-mangostin, which is a derivative of γ-mangostin, can provide better activity in silico with molecular docking approaches and molecular dynamics simulations.

    METHOD: This research commenced with retrieving protein structures from the RCSB database, generating the formation of ligands using the ChemDraw Professional software, conducting molecular docking with the Autodock Vina software, and performing molecular dynamics simulations using the Amber software, along with the evaluation of RMSD values and intermolecular hydrogen bonds. Free energy, electrostatic interactions, and Van der Waals interaction were calculated using MM/GBSA. Acarbose, used as a positive control, and maltose are simulated together with test compound that has the best free energy. The forcefields used for molecular dynamics simulations are ff19SB, gaff2, and tip3p.

    Matched MeSH terms: Acarbose
  14. Fulltext Prevention of type 2 diabetes
    Lai LC
    Malays J Pathol, 2002 Dec;24(2):71-6.
    PMID: 12887163
    The prevalence of diabetes is increasing worldwide. The World Health Organisation has estimated that there will be around 300 million diabetics by 2025. The largest increase will occur in Asia. The prevalence of type 2 diabetes is increasing due to a combination of factors: increasing lifespan, sedentary lifestyle, excessive intake of high energy foods, increasing prevalence of overweight/obese people. The Finnish Diabetes Prevention Study Group has clearly shown that changes in the lifestyle of both overweight men and women with impaired glucose tolerance can reduce the incidence of type 2 diabetes by 58%. This finding was confirmed by the Diabetes Prevention Programme which found that lifestyle intervention in individuals with impaired fasting glucose or impaired glucose tolerance reduced the risk of developing type 2 diabetes by 58%, whereas treatment with metformin reduced the risk of type 2 diabetes by only 31%. Both acarbose and troglitazone have also been shown to reduce the progression to diabetes in individuals who are at high risk of developing type 2 diabetes. Since the cure for diabetes remains some way off our concerted efforts should be directed at prevention of diabetes in order to curb the increasing prevalence of diabetes worldwide. Lifestyle changes are more beneficial than long term drug therapy in the prevention of diabetes and should be actively promoted.
    Matched MeSH terms: Acarbose/therapeutic use
  15. Fulltext Phytochemical screening and enzymatic and antioxidant activities of Erythrina suberosa (Roxb) bark
    Ahmed Z, Aziz S, Hanif M, Mohiuddin SG, Ali Khan SH, Ahmed R, et al.
    J Pharm Bioallied Sci, 2020 04 10;12(2):192-200.
    PMID: 32742119 DOI: 10.4103/jpbs.JPBS_222_19
    Background: This study aimed to evaluate the phytochemicals screening of Erythrina suberosa (Roxb) bark and to analyze the enzymatic activities of its various organic fractions.

    Materials and Methods: Crude methanolic fraction of E. suberosa (Roxb) bark and its respective fractions were screened for the presence of different phytochemicals with different reagents. On the basis of increasing order of polarity, different organic solvents were used to obtain different fractions. Enzymatic studies were performed on crude methanolic extract of the plant. All the assays were performed under standard in vitro conditions.

    Results: The phytochemical analysis shows the presence of alkaloids, phenols, triterpenoids, phytosterols, and flavonoids. Phenolic compounds and flavonoids are the major constituents of the plant. In anticholinesterase assay, the percent inhibition of standard drug (eserine) was 91.27 ± 1.17 and the half maximal inhibitory concentration (IC50) was 0.04 ± 0.0001. For α-glucosidase inhibition, the IC50 value for Dichloromethane fraction was 8.45 ± 0.13, for Methanol fraction it was 64.24 ± 0.15, and for aqueous fraction it was 42.62 ± 0.17 as compared with standard IC50 that is 37.42 (acarbose). Furthermore, results show that all fractions have potential against anti-urease enzyme, but DCM fraction of crude aqueous extract has significant IC50 value (45.26 ± 0.13) than other fractions.

    Conclusion: Keeping in view all the results, it is evident that the plant can be used in future for formulating effective drugs against many ailments. Secondary metabolites and their derivatives possess different biological activities, for example, .g. flavonoids in cancer, asthma, and Alzheimer. Furthermore, the extracts of this plant can be used in their crude form, which is an addition to the complementary and alternative treatment strategies.

    Matched MeSH terms: Acarbose
  16. Fulltext Perilla frutescens Leaf Extract and Fractions: Polyphenol Composition, Antioxidant, Enzymes (α-Glucosidase, Acetylcholinesterase, and Tyrosinase) Inhibitory, Anticancer, and Antidiabetic Activities
    Wang Z, Tu Z, Xie X, Cui H, Kong KW, Zhang L
    Foods, 2021 Feb 03;10(2).
    PMID: 33546380 DOI: 10.3390/foods10020315
    This study aims to evaluate the bioactive components, in vitro bioactivities, and in vivo hypoglycemic effect of P. frutescens leaf, which is a traditional medicine-food homology plant. P. frutescens methanol crude extract and its fractions (petroleum ether, chloroform, ethyl acetate, n-butanol fractions, and aqueous phase residue) were prepared by ultrasound-enzyme assisted extraction and liquid-liquid extraction. Among the samples, the ethyl acetate fraction possessed the high total phenolic (440.48 μg GAE/mg DE) and flavonoid content (455.22 μg RE/mg DE), the best antioxidant activity (the DPPH radical, ABTS radical, and superoxide anion scavenging activity, and ferric reducing antioxidant power were 1.71, 1.14, 2.40, 1.29, and 2.4 times higher than that of control Vc, respectively), the most powerful α-glucosidase inhibitory ability with the IC50 value of 190.03 μg/mL which was 2.2-folds higher than control acarbose, the strongest proliferative inhibitory ability against MCF-7 and HepG2 cell with the IC50 values of 37.92 and 13.43 μg/mL, which were considerable with control cisplatin, as well as certain inhibition abilities on acetylcholinesterase and tyrosinase. HPLC analysis showed that the luteolin, rosmarinic acid, rutin, and catechin were the dominant components of the ethyl acetate fraction. Animal experiments further demonstrated that the ethyl acetate fraction could significantly decrease the serum glucose level, food, and water intake of streptozotocin-induced diabetic SD rats, increase the body weight, modulate their serum levels of TC, TG, HDL-C, and LDL-C, improve the histopathology and glycogen accumulation in liver and intestinal tissue. Taken together, P. frutescens leaf exhibits excellent hypoglycemic activity in vitro and in vivo, and could be exploited as a source of natural antidiabetic agent.
    Matched MeSH terms: Acarbose
  17. Molecular dynamics simulations reveal the inhibitory mechanism of Withanolide A against α-glucosidase and α-amylase
    Oyewusi HA, Wu YS, Safi SZ, Wahab RA, Hatta MHM, Batumalaie K
    J Biomol Struct Dyn, 2023;41(13):6203-6218.
    PMID: 35904027 DOI: 10.1080/07391102.2022.2104375
    Diabetes mellitus (DM) is a global chronic disease characterized by hyperglycemia and insulin resistance. The unsavory severe gastrointestinal side-effects of synthetic drugs to regulate hyperglycemia have warranted the search for alternative treatments to inhibit the carbohydrate digestive enzymes (e.g. α-amylase and α-glucosidase). Certain phytochemicals recently captured the scientific community's attention as carbohydrate digestive enzyme inhibitors due to their low toxicity and high efficacy, specifically the Withanolides-loaded extract of Withania somnifera. That said, the present study evaluated in silico the efficacy of Withanolide A in targeting both α-amylase and α-glucosidase in comparison to the synthetic drug Acarbose. Protein-ligand interactions, binding affinity, and stability were characterized using pharmacological profiling, high-end molecular docking, and molecular-dynamic simulation. Withanolide A inhibited the activity of α-glucosidase and α-amylase better, exhibiting good pharmacokinetic properties, absorption, and metabolism. Also, Withanolide A was minimally toxic, with higher bioavailability. Interestingly, Withanolide A bonded well to the active site of α-amylase and α-glucosidase, yielding the lowest binding free energy of -82.144 ± 10.671 kcal/mol and -102.1043 ± 11.231 kcal/mol compared to the Acarbose-enzyme complexes (-63.220 ± 13.283 kcal/mol and -82.148 ± 10.671 kcal/mol). Hence, the findings supported the therapeutic potential of Withanolide A as α-amylase and α-glucosidase inhibitor for DM treatment.Communicated by Ramaswamy H. Sarma.
    Matched MeSH terms: Acarbose/pharmacology
  18. Inhibitory effects of edible seaweeds, polyphenolics and alginates on the activities of porcine pancreatic α-amylase
    Zaharudin N, Salmeán AA, Dragsted LO
    Food Chem, 2018 Apr 15;245:1196-1203.
    PMID: 29287342 DOI: 10.1016/j.foodchem.2017.11.027
    Edible seaweeds are valuable because of their organoleptic properties and complex polysaccharide content. A study was conducted to investigate the potential of dried edible seaweed extracts, its potential phenolic compounds and alginates for α-amylase inhibitory effects. The kinetics of inhibition was assessed in comparison with acarbose. The methanol extract of Laminaria digitata and the acetone extract of Undaria pinnatifida showed inhibitory activity against α-amylase, IC50 0.74 ± 0.02 mg/ml and 0.81 ± 0.03 mg/ml, respectively; both showed mixed-type inhibition. Phenolic compound, 2,5-dihydroxybenzoic acid was found to be a potent inhibitor of α-amylase with an IC50 value of 0.046 ± 0.004 mg/ml. Alginates found in brown seaweeds appeared to be potent inhibitors of α-amylase activity with an IC50 of (0.075 ± 0.010-0.103 ± 0.017) mg/ml, also a mixed-type inhibition. Overall, the findings provide information that crude extracts of brown edible seaweeds, phenolic compounds and alginates are potent α-amylase inhibitors, thereby potentially retarding glucose liberation from starches and alleviation of postprandial hyperglycaemia.
    Matched MeSH terms: Acarbose/pharmacology
  19. Indole acrylonitriles as potential anti-hyperglycemic agents: Synthesis, α-glucosidase inhibitory activity and molecular docking studies
    Solangi M, Kanwal, Mohammed Khan K, Saleem F, Hameed S, Iqbal J, et al.
    Bioorg Med Chem, 2020 Nov 01;28(21):115605.
    PMID: 33065441 DOI: 10.1016/j.bmc.2020.115605
    One of the most prevailing metabolic disorder diabetes mellitus has become the global health issue that has to be addressed and cured. Different marketed drugs have been made available for the treatment of diabetes but there is still a need of introducing new therapeutic agents that are economical and have lesser or no side effects. The current study deals with the synthesis of indole acrylonitriles (3-23) and the evaluation of these compounds for their potential for α-glucosidase inhibition. The structures of these synthetic molecules were deduced by using different spectroscopic techniques. Acarbose (IC50 = 2.91 ± 0.02 μM) was used as standard in this study and the synthetic molecules (3-23) have shown promising α-glucosidase inhibitory activity. Compounds 4, 8, 10, 11, 14, 18, and 21 displayed superior inhibition of α-glucosidase enzyme in the range of (IC50 = 0.53 ± 0.01-1.36 ± 0.04 μM) as compared to the standard acarbose. Compound 10 (IC50 = 0.53 ± 0.01 μM) was the most effective inhibitor of this library and displayed many folds enhanced activity in contrast to the standard. Molecular docking of synthetic compounds was performed to verify the binding interactions of ligand with the active site of enzyme. This study had identified a number of potential α-glucosidase inhibitors that can be used for further research to identify a potent therapeutic agent against diabetes.
    Matched MeSH terms: Acarbose
  20. Fulltext Health utilities in Chinese patients with coronary heart disease and impaired glucose tolerance (ACE): A longitudinal analysis of a randomized, double-blind, placebo-controlled trial
    Leal J, Becker F, Lim LL, Holman RR, Gray AM
    J Diabetes, 2022 Jul;14(7):455-464.
    PMID: 35876124 DOI: 10.1111/1753-0407.13294
    BACKGROUND: We estimate health-related quality of life and the impact of four cardiovascular events (myocardial infarction [MI], stroke, congestive heart failure, angina) and gastrointestinal events in 6522 Chinese patients with coronary heart disease (CHD) and impaired glucose tolerance (IGT) participating in the Acarbose Cardiovascular Evaluation (ACE) trial.

    METHODS: Health-related quality of life was captured using the EuroQol-5 Dimension-3 Level (EQ-5D-3L), with data collected at baseline and throughout the trial. Multilevel mixed-effects linear regression with random effects estimated health-related quality of life over time, capturing variation between hospital sites and individuals, and a fixed-effects linear model estimated the impact of cardiovascular and gastrointestinal events.

    RESULTS: Patients were followed for a median of 5 years (interquartile range 3.4-6.0). The average baseline EQ-5D score of 0.930 (SD 0.104) remained relatively unchanged over the trial period with no evidence of statistically significant differences in EQ-5D score between randomized treatment groups. The largest decrement in the year of an event was estimated for stroke (-0.107, P 

    Matched MeSH terms: Acarbose/therapeutic use
Related Terms
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links