Displaying publications 21 - 40 of 64 in total

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  1. GC-MS-based metabolite profiling of Cosmos caudatus leaves possessing alpha-glucosidase inhibitory activity
    Javadi N, Abas F, Abd Hamid A, Simoh S, Shaari K, Ismail IS, et al.
    J Food Sci, 2014 Jun;79(6):C1130-6.
    PMID: 24888400 DOI: 10.1111/1750-3841.12491
    Cosmos caudatus, which is known as "Ulam Raja," is an herbal plant used in Malaysia to enhance vitality. This study focused on the evaluation of the α-glucosidase inhibitory activity of different ethanolic extracts of C. caudatus. Six series of samples extracted with water, 20%, 40%, 60%, 80%, and 100% ethanol (EtOH) were employed. Gas chromatography-mass spectrometry (GC-MS) and orthogonal partial least-squares (OPLS) analysis was used to correlate bioactivity of different extracts to different metabolite profiles of C. caudatus. The obtained OPLS scores indicated a distinct and remarkable separation into 6 clusters, which were indicative of the 6 different ethanol concentrations. GC-MS can be integrated with multivariate data analysis to identify compounds that inhibit α-glucosidase activity. In addition, catechin, α-linolenic acid, α-D-glucopyranoside, and vitamin E compounds were identified and indicate the potential α-glucosidase inhibitory activity of this herb.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  2. Growth inhibition of human liver carcinoma HepG2 cells and α-glucosidase inhibitory activity of Murdannia bracteata (C.B. Clarke) Kuntze ex J.K. Morton extracts
    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: alpha-Glucosidases/metabolism
  3. Hydrazinyl arylthiazole based pyridine scaffolds: Synthesis, structural characterization, in vitro α-glucosidase inhibitory activity, and in silico studies
    Ali F, Khan KM, Salar U, Taha M, Ismail NH, Wadood A, et al.
    Eur J Med Chem, 2017 Sep 29;138:255-272.
    PMID: 28672278 DOI: 10.1016/j.ejmech.2017.06.041
    Acarbose, miglitol, and voglibose are the inhibitors of α-glucosidase enzyme and being clinically used for the management of type-II diabetes mellitus. However, many adverse effects are also associated with them. So, the development of new therapeutic agents is an utmost interest in medicinal chemistry research. Current study is based on the identification of new α-glucosidase inhibitors. For that purpose, hydrazinyl arylthiazole based pyridine derivatives 1-39 were synthesized via two step reaction and fully characterized by spectroscopic techniques EI-MS, HREI-MS, (1)H-, and (13)C NMR. However, stereochemistry of the iminic bond was confirmed by NOESY. All compounds were subjected to in vitro α-glucosidase inhibitory activity and found many folds active (IC50 = 1.40 ± 0.01-236.10 ± 2.20 μM) as compared to the standard acarbose having IC50 value of 856.45 ± 5.60 μM. A limited structure-activity relationship was carried out in order to make a presumption about the substituent's effect on inhibitory activity which predicted that substituents of more negative inductive effect played important role in the activity as compared to the substituents of less negative inductive effect. However, in order to have a good understanding of ligand enzyme interactions, molecular docking study was also conducted. In silico study was confirmed that substituents like halogens (Cl) and nitro (NO2) which have negative inductive effect were found to make important interactions with active site residues.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  4. Identification and characterization of novel α-amylase and α-glucosidase inhibitory peptides from camel whey proteins
    Baba WN, Mudgil P, Kamal H, Kilari BP, Gan CY, Maqsood S
    J Dairy Sci, 2021 Feb;104(2):1364-1377.
    PMID: 33309363 DOI: 10.3168/jds.2020-19271
    This study explores the inhibitory properties of camel whey protein hydrolysates (CWPH) toward α-amylase (AAM) and α-glucosidase (AG). A general full factorial design (3 × 3) was applied to study the effect of temperature (30, 37, and 45°C), time (120, 240, and 360 min), and enzyme (pepsin) concentration (E%; 0.5, 1, and 2%). The results showed that maximum degree of hydrolysis was obtained when hydrolysis was carried out at higher temperature (45°C; P < 0.05), compared with lower temperatures of 30 and 37°C. Electrophoretic pattern displays degradation of all protein bands upon hydrolysis by pepsin at various hydrolysis conditions applied. All the 27 CWPH generated showed significant AAM and AG inhibitory potential as indicated by their lower IC50 values (mg/mL) compared with intact whey proteins. In total 196 peptides were identified from selected hydrolysates and 15 potential peptides (PepSite score > 0.8; http://pepsite2.russelllab.org/) were explored via in silico approach. Novel peptides PAGNFLMNGLMHR, PAVACCLPPLPCHM, MLPLMLPFTMGY, and PAGNFLPPVAAAPVM were identified as potential inhibitors for both AAM and AG due to their high number of binding sites and highest binding probability toward the target enzymes. CCGM and MFE, as well as FCCLGPVPP were identified as AG and AAM inhibitory peptides, respectively. This is the first study that reports novel AG and AAM inhibitory peptides from camel whey proteins. The future direction for this research involves synthesis of these potential AG and AAM inhibitory peptides in a pure form and investigate their antidiabetic properties in the in vitro, as well as in vivo models. Thus, CWPH can be considered for potential applications in glycaemic regulation.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  5. In vitro and in silico evaluations of diarylpentanoid series as α-glucosidase inhibitor
    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: alpha-Glucosidases/metabolism*
  6. Fulltext In vitro antioxidant and, α-glucosidase inhibitory activities and comprehensive metabolite profiling of methanol extract and its fractions from Clinacanthus nutans
    Alam MA, Zaidul IS, Ghafoor K, Sahena F, Hakim MA, Rafii MY, et al.
    BMC Complement Altern Med, 2017 Mar 31;17(1):181.
    PMID: 28359331 DOI: 10.1186/s12906-017-1684-5
    BACKGROUND: This study was aimed to evaluate antioxidant and α-glucosidase inhibitory activity, with a subsequent analysis of total phenolic and total flavonoid content of methanol extract and its derived fractions from Clinacanthus nutans accompanied by comprehensive phytochemical profiling.

    METHODS: Liquid-liquid partition chromatography was used to separate methanolic extract to get hexane, ethyl acetate, butanol and residual aqueous fractions. The total antioxidant activity was determined by 2,2-diphenyl-1-picrylhydrazy (DPPH) radical scavenging and ferric reducing antioxidant power assay (FRAP). The antidiabetic activity of methanol extract and its consequent fractions were examined by α-glucosidase inhibitory bioassay. The chemical profiling was carried out by gas chromatography coupled with quadrupole time-of-flight mass spectrometry (GC Q-TOF MS).

    RESULTS: The total yield for methanol extraction was (12.63 ± 0.98) % (w/w) and highest fractionated value found for residual aqueous (52.25 ± 1.01) % (w/w) as compared to the other fractions. Significant DPPH free radical scavenging activity was found for methanolic extract (63.07 ± 0.11) % and (79.98 ± 0.31) % for ethyl acetate fraction among all the fractions evaluated. Methanol extract was the most prominent in case of FRAP (141.89 ± 0.87 μg AAE/g) whereas most effective reducing power observed in ethyl acetate fraction (133.6 ± 0.2987 μg AAE/g). The results also indicated a substantial α-glucosidase inhibitory activity for butanol fraction (72.16 ± 1.0) % and ethyl acetate fraction (70.76 ± 0.49) %. The statistical analysis revealed that total phenolic and total flavonoid content of the samples had the significant (p 

    Matched MeSH terms: alpha-Glucosidases/metabolism
  7. Inhibition of α-glucosidase activity by selected edible seaweeds and fucoxanthin
    Zaharudin N, Staerk D, Dragsted LO
    Food Chem, 2019 Jan 01;270:481-486.
    PMID: 30174076 DOI: 10.1016/j.foodchem.2018.07.142
    A 5 mg/mL solution of water, methanol and acetone extracts of seaweeds were used for α-glucosidase inhibition assay hyphenated with high performance liquid chromatography-mass spectrometry (HPLC-HRMS). The results showed acetone extracts of Undaria pinnatifida has the strongest inhibitory effect against α-glucosidase activity with IC50 0.08 ± 0.002 mg/mL. The active compound found in Undaria pinnatifida was identified as fucoxanthin. Analytical standard sample of fucoxanthin significantly inhibited α-glucosidase with IC50 value 0.047 ± 0.001 mg/mL. An inhibition kinetics study indicates that fucoxanthin is showing mixed-type inhibition. These results suggest that Undaria pinnatifida has a potential to inhibit α-glucosidase and may be used as a bioactive food ingredient for glycaemic control.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  8. Fulltext Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
    Zabidi NA, Ishak NA, Hamid M, Ashari SE, Mohammad Latif MA
    J Enzyme Inhib Med Chem, 2021 Dec;36(1):109-121.
    PMID: 33249946 DOI: 10.1080/14756366.2020.1844680
    The inhibition of α-glucosidase and DPP enzymes capable of effectively reducing blood glucose level in the management of type 2 diabetes. The purpose of the present study is to evaluate the inhibitory potential of α-glucosidase and DPP (IV) activity including with the 2-NBDG uptake assay and insulin secretion activities through in vitro studies. The selected of active compounds obtained from the screening of compounds by LC-MS were docked with the targeted enzyme that involved in the mechanism of T2DM. From the results, root extracts displayed a better promising outcome in α-glucosidase (IC50 2.72 ± 0.32) as compared with the fruit extracts (IC50 3.87 ± 0.32). Besides, root extracts also displayed a better activity in the inhibition of DPP (IV), enhance insulin secretion and glucose uptake activity. Molecular docking results revealing that phlorizin binds strongly with α-glucosidase, DPP (IV) and Insulin receptor (IR) enzymes with achieving the lowest binding energy value. The present work suggests several of the compounds have the potential that contribute towards inhibiting α-glucosidase and DPP (IV) and thus effective in lowering post-prandial hyperglycaemia.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  9. Fulltext Investigation of α-Glucosidase Inhibitory Metabolites from Tetracera scandens Leaves by GC-MS Metabolite Profiling and Docking Studies
    Nokhala A, Siddiqui MJ, Ahmed QU, Ahamad Bustamam MS, Zakaria AZA
    Biomolecules, 2020 02 12;10(2).
    PMID: 32059529 DOI: 10.3390/biom10020287
    Stone leaf (Tetracera scandens) is a Southeast Asian medicinal plant that has been traditionally used for the management of diabetes mellitus. The underlying mechanisms of the antidiabetic activity have not been fully explored yet. Hence, this study aimed to evaluate the α-glucosidase inhibitory potential of the hydromethanolic extracts of T. scandens leaves and to characterize the metabolites responsible for such activity through gas chromatography-mass spectrometry (GC-MS) metabolomics. Crude hydromethanolic extracts of different strengths were prepared and in vitro assayed for α-glucosidase inhibition. GC-MS analysis was further carried out and the mass spectral data were correlated to the corresponding α-glucosidase inhibitory IC50 values via an orthogonal partial least squares (OPLS) model. The 100%, 80%, 60% and 40% methanol extracts displayed potent α-glucosidase inhibitory potentials. Moreover, the established model identified 16 metabolites to be responsible for the α-glucosidase inhibitory activity of T. scandens. The putative α-glucosidase inhibitory metabolites showed moderate to high affinities (binding energies of -5.9 to -9.8 kcal/mol) upon docking into the active site of Saccharomyces cerevisiae isomaltase. To sum up, an OPLS model was developed as a rapid method to characterize the α-glucosidase inhibitory metabolites existing in the hydromethanolic extracts of T. scandens leaves based on GC-MS metabolite profiling.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  10. Isatin based Schiff bases as inhibitors of α-glucosidase: Synthesis, characterization, in vitro evaluation and molecular docking studies
    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: alpha-Glucosidases/metabolism*
  11. Fulltext Linking Diabetes to Alzheimer's Disease: Potential Roles of Glucose Metabolism and Alpha-Glucosidase
    Wee AS, Nhu TD, Khaw KY, Tang KS, Yeong KY
    Curr Neuropharmacol, 2023;21(10):2036-2048.
    PMID: 36372924 DOI: 10.2174/1570159X21999221111102343
    Alzheimer's disease (AD) and type 2 diabetes mellitus (DM) are more prevalent with ageing and cause a substantial global socio-economic burden. The biology of these two conditions is well elaborated, but whether AD and type 2 DM arise from coincidental roots in ageing or are linked by pathophysiological mechanisms remains unclear. Research findings involving animal models have identified mechanisms shared by both AD and type 2 DM. Deposition of β-amyloid peptides and formation of intracellular neurofibrillary tangles are pathological hallmarks of AD. Type 2 DM, on the other hand, is a metabolic disorder characterised by hyperglycaemia and insulin resistance. Several studies show that improving type 2 DM can delay or prevent the development of AD, and hence, prevention and control of type 2 DM may reduce the risk of AD later in life. Alpha-glucosidase is an enzyme that is commonly associated with hyperglycaemia in type 2 DM. However, it is uncertain if this enzyme may play a role in the progression of AD. This review explores the experimental evidence that depicts the relationship between dysregulation of glucose metabolism and AD. We also delineate the links between alpha-glucosidase and AD and the potential role of alpha-glucosidase inhibitors in treating AD.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  12. Molecular Insight and Mode of Inhibition of α-Glucosidase and α-Amylase by Pahangensin A from Alpinia pahangensis Ridl
    Loo KY, Leong KH, Sivasothy Y, Ibrahim H, Awang K
    Chem Biodivers, 2019 Jun;16(6):e1900032.
    PMID: 30957403 DOI: 10.1002/cbdv.201900032
    The inhibition of carbohydrate-hydrolyzing enzymes in human digestive organs is crucial in controlling blood sugar levels, which is important in treating type 2 diabetes. In the current study, pahangensin A (1), a bis-labdanic diterpene characterized previously in the rhizomes of Alpinia pahangensis Ridl., was identified as an active dual inhibitor for α-amylase (IC50 =114.80 μm) and α-glucosidase (IC50 =153.87 μm). This is the first report on the dual α-amylase and α-glucosidase inhibitory activities of a bis-labdanic diterpene. The Lineweaver-Burk plots of compound 1 indicate that it is a mixed-type inhibitor with regard to both enzymes. Based on molecular docking studies, compound 1 docked in a non-active site of both enzymes. The dual inhibitory activity of compound 1 makes it a suitable natural alternative in the treatment of type 2 diabetes.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  13. New insights into the phytochemical composition, enzyme inhibition and antioxidant properties of desert cotton (Aerva javanica (Bum.f) Shult. -Amaranthaceae)
    Saleem H, Zengin G, Khan KU, Ahmad I, Waqas M, Mahomoodally FM, et al.
    Nat Prod Res, 2021 Feb;35(4):664-668.
    PMID: 30919661 DOI: 10.1080/14786419.2019.1587427
    This study sets out to probe into total bioactive contents, UHPLC-MS secondary metabolites profiling, antioxidant (DPPH, ABTS, FRAP, CUPRAC, phosphomolybdenum and metal chelating) and enzyme inhibitory (acetylcholinesterase- AChE, butyrylcholinesterase- BChE, α-amylase, α glucosidase, and tyrosinase) activities of methanol extract of Aerva javanica, also known as desert cotton or Kapok bush. Aerva javanica contains considerable phenolic (44.79 ± 3.12 mg GAE/g) and flavonoid (28.86 ± 0.12 mg QE/g) contents which tends to correlate with its significant antioxidant potential for ABTS, FRAP and CUPRAC assays with values of 101.41 ± 1.18, 124.10 ± 1.71 and 190.22 ± 5.70 mg TE/g, respectively. The UHPLC-MS analysis identified the presence of 45 phytochemicals belonging to six major groups: phenolic, flavonoids, lignin, terpenes, glycoside and alkaloid. Moreover, the plant extract also showed potent inhibitory action against AChE (3.73 ± 0.22 mg GALAE/g), BChE (3.31 ± 0.19 mg GALAE/g) and tyrosinase (126.05 ± 1.77 mg KAE/g). The observed results suggest A. javanica could be further explored as a natural source of bioactive compounds.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  14. New pyrrolopyridine-based thiazolotriazoles as diabetics inhibitors: enzymatic kinetics and in silico study
    Taha M, Rahim F, Hayat S, Chigurupati S, Khan KM, Imran S, et al.
    Future Med Chem, 2023 Mar;15(5):405-419.
    PMID: 37013918 DOI: 10.4155/fmc-2022-0306
    Aim: To synthesize pyrrolopyridine-based thiazolotriazoles as a novel class of α-amylase and α-glucosidase inhibitors and to determine their enzymatic kinetics. Methodology: Pyrrolopyridine-based thiazolotriazole analogs (1-24) were synthesized and characterized through proton nuclear magnetic resonance, carbon-13 nuclear magnetic resonance and high-resolution electron ionization mass spectrometry. Results: All synthesized analogs displayed good inhibitory potential of α-amylase and α-glucosidase ranging 17.65-70.7 μM and 18.15-71.97 μM, respectively, compared with the reference drug, acarbose (11.98 μM and 12.79 μM). Analog 3 was the most potent among the synthesized analogs, having α-amylase and α-glucosidase inhibitory activity at 17.65 and 18.15 μM, respectively. The structure-activity relationship and binding modes of interactions between selected analogs were confirmed via docking and enzymatic kinetics studies. The compounds (1-24) were tested for cytotoxicity against the 3T3 mouse fibroblast cell line and were observed to be nontoxic.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  15. Fulltext New quinoxalinone inhibitors targeting secreted phospholipase A2 and α-glucosidase
    Alasmary FAS, Alnahdi FS, Ben Bacha A, El-Araby AM, Moubayed N, Alafeefy AM, et al.
    J Enzyme Inhib Med Chem, 2017 Dec;32(1):1143-1151.
    PMID: 28856929 DOI: 10.1080/14756366.2017.1363743
    Elevated blood glucose and increased activities of secreted phospholipase A2 (sPLA2) are strongly linked to coronary heart disease. In this report, our goal was to develop small heterocyclic compound that inhibit sPLA2. The title compounds were also tested against α-glucosidase and α-amylase. This array of enzymes was selected due to their implication in blood glucose regulation and diabetic cardiovascular complications. Therefore, two distinct series of quinoxalinone derivatives were synthesised; 3-[N'-(substituted-benzylidene)-hydrazino]-1H-quinoxalin-2-ones 3a-f and 1-(substituted-phenyl)-5H-[1,2,4]triazolo[4,3-a]quinoxalin-4-ones 4a-f. Four compounds showed promising enzyme inhibitory effect, compounds 3f and 4b-d potently inhibited the catalytic activities of all of the studied proinflammatory sPLA2. Compound 3e inhibited α-glucosidase (IC50 = 9.99 ± 0.18 µM); which is comparable to quercetin (IC50 = 9.93 ± 0.66 µM), a known inhibitor of this enzyme. Unfortunately, all compounds showed weak activity against α-amylase (IC50 > 200 µM). Structure-based molecular modelling tools were utilised to rationalise the SAR compared to co-crystal structures with sPLA2-GX as well as α-glucosidase. This report introduces novel compounds with dual activities on biochemically unrelated enzymes mutually involved in diabetes and its complications.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  16. Oxindole based oxadiazole hybrid analogs: Novel α-glucosidase inhibitors
    Taha M, Imran S, Rahim F, Wadood A, Khan KM
    Bioorg Chem, 2018 02;76:273-280.
    PMID: 29223804 DOI: 10.1016/j.bioorg.2017.12.001
    Inhibition of α-glucosidase is an effective strategy for controlling post-prandial hyperglycemia in diabetic patients. Beside these α-glucosidase inhibitors has been also used as anti-obesity and anti-viral drugs. Keeping in view the greater importance of α-glucosidase inhibitors here in this study we are presenting oxindole based oxadiazoles hybrid analogs (1-20) synthesis, characterized by different spectroscopic techniques including 1H NMR and EI-MS and their α-glucosidase inhibitory activity. All compounds were found potent inhibitors for the enzyme with IC50 values ranging between 1.25 ± 0.05 and 268.36 ± 4.22 µM when compared with the standard drug acarbose having IC50 value 895.09 ± 2.04 µM. Our study identifies novel series of potent α-glucosidase inhibitors and further investigation on this may led to the lead compounds. A structure activity relationship has been established for all compounds. The interactions of the active compounds and enzyme active site were established with the help of molecular docking studies.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  17. Phenolic profiling and evaluation of in vitro antioxidant, α-glucosidase and α-amylase inhibitory activities of Lepisanthes fruticosa (Roxb) Leenh fruit extracts
    Salahuddin MAH, Ismail A, Kassim NK, Hamid M, Ali MSM
    Food Chem, 2020 Nov 30;331:127240.
    PMID: 32585546 DOI: 10.1016/j.foodchem.2020.127240
    The present study focused on the phytochemical profiling along with evaluation of in vitro antioxidant, α-glucosidase and α-amylase inhibitory activities of various crudes and fractions obtained from Lepisanthes fruticosa (Roxb) Leenh fruit. Ethanolic seed crude extract exhibited the strongest radical scavenging, β-carotene bleaching activity, α-glucosidase inhibition and the highest total phenolic content (TPC). Column chromatography afforded various fractions with fraction M4 being the most potent due to the strongest radical scavenging, β-carotene bleaching, α-glucosidase inhibition and greatest amount of TPC. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis of ethanolic seed crude extract and fraction M4 showed the presence of various phytochemicals with antioxidant and antidiabetic properties, which include mostly flavonoids and tannins. The results may suggest that the ethanolic crude seed extract and its fraction could be an excellent source of bioactive phytochemicals with antioxidant and antidiabetic potential.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  18. Fulltext Phyllanthus Niruri Standardized Extract Alleviates the Progression of Non-Alcoholic Fatty Liver Disease and Decreases Atherosclerotic Risk in Sprague-Dawley Rats
    Al Zarzour RH, Ahmad M, Asmawi MZ, Kaur G, Saeed MAA, Al-Mansoub MA, et al.
    Nutrients, 2017 Jul 18;9(7).
    PMID: 28718838 DOI: 10.3390/nu9070766
    Non-alcoholic fatty liver disease (NAFLD) is one of the major global health issues, strongly correlated with insulin resistance, obesity and oxidative stress. The current study aimed to evaluate anti-NAFLD effects of three different extracts of Phyllanthus niruri (P. niruri). NAFLD was induced in male Sprague-Dawley rats using a special high-fat diet (HFD). A 50% methanolic extract (50% ME) exhibited the highest inhibitory effect against NAFLD progression. It significantly reduced hepatomegaly (16%) and visceral fat weight (22%), decreased NAFLD score, prevented fibrosis, and reduced serum total cholesterol (TC) (48%), low-density lipoprotein (LDL) (65%), free fatty acids (FFAs) (25%), alanine aminotransferase (ALT) (45%), alkaline phosphatase (ALP) (38%), insulin concentration (67%), homeostatic model assessment of insulin resistance (HOMA-IR) (73%), serum atherogenic ratios TC/high-density lipoprotein (HDL) (29%), LDL/HDL (66%) and (TC-HDL)/HDL (64%), hepatic content of cholesterol (43%), triglyceride (29%) and malondialdehyde (MDA) (40%) compared to a non-treated HFD group. In vitro, 50% ME of P. niruri inhibited α-glucosidase, pancreatic lipase enzymes and cholesterol micellization. It also had higher total phenolic and total flavonoid contents compared to other extracts. Ellagic acid and phyllanthin were identified as major compounds. These results suggest that P. niruri could be further developed as a novel natural hepatoprotective agent against NAFLD and atherosclerosis.
    Matched MeSH terms: alpha-Glucosidases/metabolism
  19. Potent Antidiabetic Activity and Metabolite Profiling of Melicope Lunu-ankenda Leaves
    Al-Zuaidy MH, Hamid AA, Ismail A, Mohamed S, Abdul Razis AF, Mumtaz MW, et al.
    J Food Sci, 2016 May;81(5):C1080-90.
    PMID: 27074520 DOI: 10.1111/1750-3841.13293
    Diabetes mellitus is normally characterized by chronic hyperglycemia associated with disturbances in the fat, carbohydrate, and protein metabolism. There is an increasing trend of using natural products instead of synthetic agents as alternative therapy for disorders due to their fewer side effects. In this study, antidiabetic and antioxidant activities of different Melicope lunu-ankenda (ML) ethanolic extracts were evaluated using inhibition of α-glucosidase and 2,2-diphenyl-l-picrylhydrazyl (DPPH) radicals scavenging activity, respectively; whereas, proton nuclear magnetic resonance ((1) H NMR) and ultra-high performance liquid chromatography-tandem mass spectrometric (UHPLC-MS/MS) techniques were used for metabolite profiling of ML leaf extracts at different concentrations of ethanol and water. Sixty percent of ethanolic ML extract showed highest inhibitory effect against α-glucosidase enzyme (IC50 of 37 μg/mL) and DPPH scavenging activity (IC50 of 48 μg/mL). Antidiabetic effect of ML extracts was also evaluated in vivo and it was found that the high doses (400 mg/Kg BW) of ML extract exhibited high suppression in fasting blood glucose level by 62.75%. The metabolites responsible for variation among ML samples with variable ethanolic levels have been evaluated successfully using (1) H-NMR-based metabolomics. The principal component analysis (PCA) and partial least squares(PLS) analysis scores depicted clear and distinct separations into 4 clusters representing the 4 ethanolic concentrations by PC1 and PC2, with an eigenvalue of 69.9%. Various (1) H-NMR chemical shifts related to the metabolites responsible for sample difference were also ascribed. The main bioactive compounds identified attributing toward the separation included: isorhamnetin, skimmianine, scopoletin, and melicarpinone. Hence, ML may be used as promising medicinal plant for the development of new functional foods, new generation antidiabetic drugs, as a single entity phytomedicine or in combinational therapy.
    Matched MeSH terms: alpha-Glucosidases/metabolism*
  20. Relationship Between Metabolites Composition and Biological Activities of Phyllanthus niruri Extracts Prepared by Different Drying Methods and Solvents Extraction
    Mediani A, Abas F, Khatib A, Tan CP, Ismail IS, Shaari K, et al.
    Plant Foods Hum Nutr, 2015 Jun;70(2):184-92.
    PMID: 25800644 DOI: 10.1007/s11130-015-0478-5
    The study investigated the changes in the metabolite, antioxidant and α-glucosidase inhibitory activities of Phyllanthus niruri after three drying treatments: air, freeze and oven dryings. Water extracts and extracts obtained using different solvent ratios of ethanol and methanol (50, 70, 80 and 100%) were compared. The relationships among the antioxidant, α-glucosidase inhibitory activity and metabolite levels of the extracts were evaluated using partial least-square analysis (PLS). The solvent selectivity was assessed based on the phytochemical constituents present in the extract and their concentrations quantitatively analyzed using high performance liquid chromatography. The freeze-dried P. niruri samples that were extracted with the mixture of ethanol or methanol with low ratio of water showed higher biological activity values compared with the other extracts. The PLS results for the ethanolic with different ratio and water extracts demonstrated that phenolic acids (chlorogenic acid and ellagic acid) and flavonoids were highly linked to strong α-glucosidase inhibitory and antioxidant activities.
    Matched MeSH terms: alpha-Glucosidases/metabolism
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