Displaying publications 1 - 20 of 43 in total

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  1. 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: Glycoside Hydrolase Inhibitors/pharmacology
  2. Sivasothy Y, Loo KY, Leong KH, Litaudon M, Awang K
    Phytochemistry, 2016 Feb;122:265-269.
    PMID: 26712615 DOI: 10.1016/j.phytochem.2015.12.007
    A dimeric acylphenol and a potent α-glucosidase inhibitor, giganteone D (IC50 5.05μM), was isolated and characterized from the bark of Myristica cinnamomea King. The bark also yielded an acylphenol with an unprecedented skeleton for which the name cinnamomeone A (IC50 358.80μM) was proposed. Their structures were established by means of NMR and MS spectrometric analyses. The Lineweaver-Burk plot of giganteone D indicated that it was a mixed-type inhibitor. This is the first report on the α-glucosidase inhibiting potential of acylphenols.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  3. Hashim SE, Sirat HM, Yen KH, Ismail IS, Matsuki SN
    Nat Prod Commun, 2015 Sep;10(9):1561-3.
    PMID: 26594759
    Seven compounds were isolated from the n-hexane and chloroform extracts of the flowers and leaves of four Hornstedtia species and their structures were identified using spectroscopic techniques as 3,7,4'-trimethylkaempferol (1), 3,7-dimethylkaempferol (2), 7,4'-dimethylkaempferol (3), 3,5-dimethylkaempferol (4), 3-methylkaempferol (5), stigmast-4-en-3-one (6), and 6-hydroxy-stigmast-4-en-3-one (7). Compounds 1 to 7 were isolated from these species for the first time. They were assayed for free radical scavenging and α-glucosidase inhibition activities. The DPPH assay showed that 3-methylkaempferol (5) was the most potent antioxidant agent with an IC50 value 78.6 µM, followed by 7,4'-dimethylkaempferol (3) (IC50 = 86.1 µM). For α-glucosidase inhibition activity, 3-methylkaempferol (5) exhibited significant inhibitory activity with an IC50 value 21.0 µM. The present study revealed that Hornstedtia species have potential activities as antioxidant and α-glucosidase inhibitors.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  4. Taha M, Ismail NH, Lalani S, Fatmi MQ, Atia-Tul-Wahab, Siddiqui S, et al.
    Eur J Med Chem, 2015 Mar 6;92:387-400.
    PMID: 25585009 DOI: 10.1016/j.ejmech.2015.01.009
    In an effort to design and synthesize a new class of α-glucosidase inhibitor, we synthesized benzothiazole hybrid having benzohydrazide moiety (5). Compound 5 was reacted with various substituted aryl aldehyde to generate a small library of compounds 6-35. Synthesis of compounds was confirmed by the spectral information. These compounds were screened for their α-glucosidase activity. They showed a varying degree of α-glucosidase inhibition with IC50 values ranging between 5.31 and 53.34 μM. Compounds 6, 7, 9-16, 19, 21-30, 32-35 showed superior activity as compared to standard acarbose (IC50 = 906 ± 6.3 μM). This has identified a new class of α-glucosidase inhibitors. The predicted physico-chemical properties indicated the drug appropriateness for most of these compounds, as they obey Lipinski's rule of five (RO5). A hybrid B3LYP density functional theory (DFT) was employed for energy, minimization of 3D structures for all synthetic compounds using 6-311 + G(d,p) basis sets followed by molecular docking to explore their interactions with human intestinal C- and N-terminal domains of α-glucosidase. All compounds bind to the prospective allosteric site of the C- terminal domain, and consequently, may be considered as mixed inhibitors. It was hypothesized that both the dipole moment and H-bond interactions govern the biological activation of these compounds.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  5. Rahim F, Ullah K, Ullah H, Wadood A, Taha M, Ur Rehman A, et al.
    Bioorg Chem, 2015 Feb;58:81-7.
    PMID: 25528720 DOI: 10.1016/j.bioorg.2014.12.001
    A new series of triazinoindole analogs 1-11 were synthesized, characterized by EI-MS and (1)H NMR, evaluated for α-glucosidase inhibitory potential. All eleven (11) analogs showed different range of α-glucosidase inhibitory potential with IC50 value ranging between 2.46±0.008 and 312.79±0.06 μM when compared with the standard acarbose (IC50, 38.25±0.12 μM). Among the series, compounds 1, 3, 4, 5, 7, 8, and 11 showed excellent inhibitory potential with IC50 values 2.46±0.008, 37.78±0.05, 28.91±0.0, 38.12±0.04, 37.43±0.03, 36.89±0.06 and 37.11±0.05 μM respectively. All other compounds also showed good enzyme inhibition. The binding modes of these analogs were confirmed through molecular docking.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  6. Khan KM, Rahim F, Wadood A, Kosar N, Taha M, Lalani S, et al.
    Eur J Med Chem, 2014 Jun 23;81:245-52.
    PMID: 24844449 DOI: 10.1016/j.ejmech.2014.05.010
    In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values 16.5-385.9 μM, if compared with the standard acarbose (IC50 = 906 ± 6.387 μM). In addition, molecular docking studies were carried out to explore the binding interactions of biscoumarin derivatives with the enzyme. This study has identified a new class of potent α-glucosidase inhibitors.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  7. Taha M, Ismail NH, Imran S, Rokei MQB, Saad SM, Khan KM
    Bioorg Med Chem, 2015 Aug 01;23(15):4155-4162.
    PMID: 26183542 DOI: 10.1016/j.bmc.2015.06.060
    Oxadiazole derivatives (6-28) having hydrazone linkage, were synthesized through condensation reaction between benzohydrazide 5 with various benzaldehydes. The oxadiazoles derivatives (6-28) were evaluated for their α-glucosidase inhibitory activity. The IC50 values for inhibition activity vary in the range between 2.64 ± 0.05 and 460.14 ± 3.25 μM. The IC50 values were being compared to the standard acarbose (IC50=856.45 ± 5.60 μM) and it was found that compounds 6-9, 12, 13, 16, 18, 20, 22-28 were found to be more active than acarbose, while other compounds showed no activity. Structure-activity relationship (SAR) studies suggest that oxadiazole benzohydrazones (6-28) inhibitory potential is dependent on substitution of the N-benzylidene part. Compound 18 (IC50=2.64 ± 0.05 μM), which has trihydroxy substitution at C-2', C-4', and C-5' on N-benzylidene moiety, recorded the highest inhibition activity that is three-hundred times more active than the standard drug, acarbose (IC50=856.45 ± 5.60 μM). Compound 23 (IC50=34.64 ± 0.35 μM) was found to be the most active among compounds having single hydroxyl substitution. Shifting hydroxyl from C-2' to C-4' (6) and C-3' (7) reduces inhibitory activity significantly. Compounds with chlorine substituent (compounds 16, 28, and 27) showed potent activities but lower as compared to hydroxyl analogs. Substituent like nitro or methyl groups at any position suppresses enzyme inhibition activity. This reveals the important presence of hydroxyl and halo groups to have enzyme inhibitory potential.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology
  8. Rahim F, Malik F, Ullah H, Wadood A, Khan F, Javid MT, et al.
    Bioorg Chem, 2015 Jun;60:42-8.
    PMID: 25955493 DOI: 10.1016/j.bioorg.2015.03.005
    Isatin base Schiff bases (1-20) were synthesized, characterized by (1)H NMR and EI/MS and evaluated for α-glucosidase inhibitory potential. Out of these twenty (20) compounds only six analogs showed potent α-glucosidase inhibitory potential with IC50 value ranging in between 2.2±0.25 and 83.5±1.0μM when compared with the standard acarbose (IC50=840±1.73μM). Among the series compound 2 having IC50 value (18.3±0.56μM), 9 (83.5±1.0μM), 11 (3.3±0.25μM), 12 (2.2±0.25μM), 14 (11.8±0.15μM), and 20 (3.0±0.15μM) showed excellent inhibitory potential many fold better than the standard acarbose. The binding interactions of these active analogs were confirmed through molecular docking.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  9. Noreen T, Taha M, Imran S, Chigurupati S, Rahim F, Selvaraj M, et al.
    Bioorg Chem, 2017 06;72:248-255.
    PMID: 28482265 DOI: 10.1016/j.bioorg.2017.04.010
    Twenty five derivatives of indole carbohydrazide (1-25) had been synthesized. These compounds were characterized using 1H NMR and EI-MS, and further evaluated for their α-amylase inhibitory potential. The analogs (1-25) showed varying degree of α-amylase inhibitory potential. ranging between 9.28 and 599.0µM when compared with standard acarbose having IC50 value 8.78±0.16µM. Six analogs, 25 (IC50=9.28±0.153µM), 22 (IC50=9.79±0.43µM), 4 (IC50=11.08±0.357µM), 1 (IC50=12.65±0.169µM), 8 (IC50=21.37±0.07µM) and 14 (IC50=43.21±0.14µM) showed potent α-amylase inhibition as compared to the standard acarbose (IC50=8.78±0.16µM). All other analogs displayed good to moderate inhibitory potential. Structure-activity relationship was established through the interaction of the active compounds with enzyme active site with the help of docking studies.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  10. Al-Salahi R, Ahmad R, Anouar E, Iwana Nor Azman NI, Marzouk M, Abuelizz HA
    Future Med Chem, 2018 08 01;10(16):1889-1905.
    PMID: 29882426 DOI: 10.4155/fmc-2018-0141
    AIM: Using a simple modification on a previously reported synthetic route, 3-benzyl(phenethyl)-2-thioxobenzo[g]quinazolin-4(3H)-ones (1 and 2) were synthesized with high yields. Further transformation of 1 and 2 produced derivatives 3-26, which were structurally characterized based on NMR and MS data, and their in vitro α-glucosidase inhibitory activity was evaluated using Baker's yeast α-glucosidase enzyme.

    RESULTS: Compounds 2, 4, 8, 12 and 20 exhibited the highest activity (IC50 = 69.20, 59.60, 49.40, 50.20 and 83.20 μM, respectively) compared with the standard acarbose (IC50 = 143.54 μM).

    CONCLUSION: A new class of potent α-glucosidase inhibitors was identified, and the molecular docking predicted plausible binding interaction of the targets in the binding pocket of α-glucosidase and rationalized the structure-activity relationship (SARs) of the target compounds.

    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  11. Javid MT, Rahim F, Taha M, Rehman HU, Nawaz M, Wadood A, et al.
    Bioorg Chem, 2018 08;78:201-209.
    PMID: 29597114 DOI: 10.1016/j.bioorg.2018.03.022
    α-Glucosidase is a catabolic enzyme that regulates the body's plasma glucose levels by providing energy sources to maintain healthy functioning. 2-Amino-thiadiazole (1-13) and 2-amino-thiadiazole based Schiff bases (14-22) were synthesized, characterized by 1H NMR and HREI-MS and screened for α-glucosidase inhibitory activity. All twenty-two (22) analogs exhibit varied degree of α-glucosidase inhibitory potential with IC50 values ranging between 2.30 ± 0.1 to 38.30 ± 0.7 μM, when compare with standard drug acarbose having IC50 value of 39.60 ± 0.70 μM. Among the series eight derivatives 1, 2, 6, 7, 14, 17, 19 and 20 showed outstanding α-glucosidase inhibitory potential with IC50 values of 3.30 ± 0.1, 5.80 ± 0.2, 2.30 ± 0.1, 2.70 ± 0.1, 2.30 ± 0.1, 5.50 ± 0.1, 4.70 ± 0.2, and 5.50 ± 0.2 μM respectively, which is many fold better than the standard drug acarbose. The remaining analogs showed good to excellent α-glucosidase inhibition. Structure activity relationship has been established for all compounds. The binding interactions of these compounds were confirmed through molecular docking.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  12. Chatsumpun N, Sritularak B, Likhitwitayawuid K
    Molecules, 2017 Oct 30;22(11).
    PMID: 29084164 DOI: 10.3390/molecules22111862
    Roots of Boesenbergia rotunda (L.) Mansf. are prominent ingredients in the cuisine of several Asian countries, including Thailand, Malaysia, Indonesia, India, and China. An extract prepared from the roots of this plant showed strong inhibitory activity against enzymes α-glucosidase and pancreatic lipase and was subjected to chromatographic separation to identify the active components. Three new biflavonoids of the flavanone-chalcone type (9, 12, and 13) were isolated, along with 12 known compounds. Among the 15 isolates, the three new compounds showed stronger inhibitory activity against α-glucosidase than the drug acarbose but displayed lower pancreatic lipase inhibitory effect than the drug orlistat. The results indicated the potential of B. rotunda roots as a functional food for controlling after-meal blood glucose levels.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology
  13. Pramai P, Abdul Hamid NA, Mediani A, Maulidiani M, Abas F, Jiamyangyuen S
    J Food Drug Anal, 2018 01;26(1):47-57.
    PMID: 29389588 DOI: 10.1016/j.jfda.2016.11.023
    In an attempt to profile the metabolites of three different varieties of germinated rice, specifically black (GBR), red, and white rice, a 1H-nuclear-magnetic-resonance-based metabolomics approach was conducted. Multivariate data analysis was applied to discriminate between the three different varieties using a partial least squares discriminant analysis (PLS-DA) model. The PLS model was used to evaluate the relationship between chemicals and biological activities of germinated rice. The PLS-DA score plot exhibited a noticeable separation between the three rice varieties into three clusters by PC1 and PC2. The PLS model indicated that α-linolenic acid, γ-oryzanol, α-tocopherol, γ-aminobutyric acid, 3-hydroxybutyric acid, fumaric acid, fatty acids, threonine, tryptophan, and vanillic acid were significantly correlated with the higher bioactivities demonstrated by GBR that was extracted in 100% ethanol. Subsequently, the proposed biosynthetic pathway analysis revealed that the increased quantities of secondary metabolites found in GBR may contribute to its nutritional value and health benefits.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  14. Leong SW, Abas F, Lam KW, Yusoff K
    Bioorg. Med. Chem. Lett., 2018 02 01;28(3):302-309.
    PMID: 29292226 DOI: 10.1016/j.bmcl.2017.12.048
    A series of thirty-four diarylpentanoids derivatives were synthesized and evaluated for their α-glucosidase inhibitory activity. Eleven compounds (19, 20, 21, 24, 27, 28, 29, 31, 32, 33 and 34) were found to significantly inhibit α-glucosidase in which compounds 28, 31 and 32 demonstrated the highest activity with IC50 values ranging from 14.1 to 15.1 µM. Structure-activity comparison shows that multiple hydroxy groups are essential for α-glucosidase inhibitory activity. Meanwhile, 3,4-dihydroxyphenyl and furanyl moieties were found to be crucial in improving α-glucosidase inhibition. Molecular docking analyses further confirmed the critical role of both 3,4-dihydroxyphenyl and furanyl moieties as they bound to α-glucosidase active site in different mode. Overall result suggests that diarylpentanoids with both five membered heterocyclic ring and polyhydroxyphenyl moiety could be a new lead design in the search of novel α-glucosidase inhibitor.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  15. Saleh MSM, Bukhari DAM, Siddiqui MJA, Kasmuri AR, Murugesu S, Khatib A
    Nat Prod Res, 2020 May;34(9):1341-1344.
    PMID: 30678487 DOI: 10.1080/14786419.2018.1560295
    Different extraction processes were employed to extract bioactive metabolites from Salacca zalacca flesh by a range of aqueous and organic solvents. The highest extraction yield was obtained by 50% ethanol extract of SE (73.18 ± 4.35%), whereas SFE_1 showed the lowest yield (0.42 ± 0.08%). All extracts were evaluated for in vitro α-glucosidase inhibitory activity, measured by their IC50 values in comparison to that of quercetin, the positive control (IC50 = 2.7 ± 0.7 μg/mL). The lowest α-glucosidase inhibitory activity was indicated by water extract of SE (IC50 = 724.3 ± 42.9 μg/mL) and the highest activity was demonstrated by 60% ethanol extract by UAE (IC50 = 16.2 ± 2.4 μg/mL). All extracts were analysed by GC-MS and identified metabolites like carbohydrates, fatty acids, organic acids, phenolic acids, sterols and alkane-based compounds etcetera that may possess the potential as α-glucosidase inhibitor and may attribute to the α-glucosidase inhibitory activity.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  16. Ooi KL, Loh SI, Tan ML, Muhammad TS, Sulaiman SF
    J Ethnopharmacol, 2015 Mar 13;162:55-60.
    PMID: 25554642 DOI: 10.1016/j.jep.2014.12.030
    The juice of the entire fresh herb and infusion of dried sample of Murdannia bracteata are consumed to treat liver cancer and diabetes in Malaysia. However, no scientific evidence of these bioactivities has been reported.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  17. Taha M, Ismail NH, Imran S, Wadood A, Rahim F, Saad SM, et al.
    Bioorg Chem, 2016 Jun;66:117-23.
    PMID: 27149363 DOI: 10.1016/j.bioorg.2016.04.006
    Twenty derivatives of 5-aryl-2-(6'-nitrobenzofuran-2'-yl)-1,3,4-oxadiazoles (1-20) were synthesized and evaluated for their α-glucosidase inhibitory activities. Compounds containing hydroxyl and halogens (1-6, and 8-18) were found to be five to seventy folds more active with IC50 values in the range of 12.75±0.10-162.05±1.65μM, in comparison with the standard drug, acarbose (IC50=856.45±5.60μM). Current study explores the α-glucosidase inhibition of a hybrid class of compounds of oxadiazole and benzofurans. These findings may invite researchers to work in the area of treatment of hyperglycemia. Docking studies showed that most compounds are interacting with important amino acids Glu 276, Asp 214 and Phe 177 through hydrogen bonds and arene-arene interaction.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  18. Abdullah NH, Salim F, Ahmad R
    Molecules, 2016 Apr 27;21(5).
    PMID: 27128898 DOI: 10.3390/molecules21050525
    Continuing our interest in the Uncaria genus, the phytochemistry and the in-vitro α-glucosidase inhibitory activities of Malaysian Uncaria cordata var. ferruginea were investigated. The phytochemical study of this plant, which employed various chromatographic techniques including recycling preparative HPLC, led to the isolation of ten compounds with diverse structures comprising three phenolic acids, two coumarins, three flavonoids, a terpene and an iridoid glycoside. These constituents were identified as 2-hydroxybenzoic acid or salicylic acid (1), 2,4-dihydroxybenzoic acid (2), 3,4-dihydroxybenzoic acid (3), scopoletin or 7-hydroxy-6-methoxy-coumarin (4), 3,4-dihydroxy-7-methoxycoumarin (5), quercetin (6), kaempferol (7), taxifolin (8), loganin (9) and β-sitosterol (10). Structure elucidation of the compounds was accomplished with the aid of 1D and 2D Nuclear Magnetic Resonance (NMR) spectral data and Ultraviolet-Visible (UV-Vis), Fourier Transform Infrared (FTIR) spectroscopy and mass spectrometry (MS). In the α-glucosidase inhibitory assay, the crude methanolic extract of the stems of the plant and its acetone fraction exhibited strong α-glucosidase inhibition activity of 87.7% and 89.2%, respectively, while its DCM fraction exhibited only moderate inhibition (75.3%) at a concentration of 1 mg/mL. The IC50 values of both fractions were found to be significantly lower than the standard acarbose suggesting the presence of potential α-glucosidase inhibitors. Selected compounds isolated from the active fractions were then subjected to α-glucosidase assay in which 2,4-dihydroxybenzoic acid and quercetin showed strong inhibitory effects against the enzyme with IC50 values of 549 and 556 μg/mL compared to acarbose (IC50 580 μg/mL) while loganin and scopoletin only showed weak α-glucosidase inhibition of 44.9% and 34.5%, respectively. This is the first report of the isolation of 2-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid and loganin from the genus and the first report of the α-glucosidase inhibitory potential of 2,4-dihydroxybenzoic acid.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  19. Anouar el H, Zakaria NS, Alsalme A, Shah SA
    Mini Rev Med Chem, 2015;15(14):1148-58.
    PMID: 26205959
    A natural pentacyclic triterpenoid oleanolic acid 1 and its biotransformed metabolites 2-3 are potential α-glucosidase inhibitors. To elucidate the inhibitory mechanism of compounds 1, 2 and 3 against α-glucosidase, we calculated (i) their electronic and optical properties using DFT and TD-DFT at the B3LYP/6-31G(d) level in gas and IEF-PCM solvent; and (ii) their binding energies to α-glucosidase via docking study. DFT results showed that the α-glucosidase inhibtion is mainly depend on the polarity parameters of the studied compounds. Docking results revealed that the activity increased with binding energies (i.e. the stability of ligand-receptor complex). The specroscopic data of oleanolic acid 1 and its metabolites 2 and 3 are well predicetd for 13C NMR chemical shifts (R2=99%) and 1H NMR chemical shifts (R2=90%); and for (ii) UV/vis spectra. The assignments and interpretation of NMR chemical shifts and bathochromic shift of λMAX absorption bands are discussed.
    Matched MeSH terms: Glycoside Hydrolase Inhibitors/pharmacology*
  20. 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: Glycoside Hydrolase Inhibitors/pharmacology*
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