Displaying publications 1 - 20 of 65 in total

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  1. Synthesis, molecular docking, acetylcholinesterase and butyrylcholinesterase inhibitory potential of thiazole analogs as new inhibitors for Alzheimer disease
    Rahim F, Javed MT, Ullah H, Wadood A, Taha M, Ashraf M, et al.
    Bioorg Chem, 2015 Oct;62:106-16.
    PMID: 26318401 DOI: 10.1016/j.bioorg.2015.08.002
    A series of thirty (30) thiazole analogs were prepared, characterized by (1)H NMR, (13)C NMR and EI-MS and evaluated for Acetylcholinesterase and butyrylcholinesterase inhibitory potential. All analogs exhibited varied butyrylcholinesterase inhibitory activity with IC50 value ranging between 1.59±0.01 and 389.25±1.75μM when compared with the standard eserine (IC50, 0.85±0.0001μM). Analogs 15, 7, 12, 9, 14, 1, 30 with IC50 values 1.59±0.01, 1.77±0.01, 6.21±0.01, 7.56±0.01, 8.46±0.01, 14.81±0.32 and 16.54±0.21μM respectively showed excellent inhibitory potential. Seven analogs 15, 20, 19, 24, 28, 30 and 25 exhibited good acetylcholinesterase inhibitory potential with IC50 values 21.3±0.50, 35.3±0.64, 36.6±0.70, 44.81±0.81, 46.36±0.84, 48.2±0.06 and 48.72±0.91μM respectively. All other analogs also exhibited well to moderate enzyme inhibition. The binding mode of these compounds was confirmed through molecular docking.
    Matched MeSH terms: Thiazoles/pharmacology*
  2. Antifilarial activity of CGP 20376 against subperiodic Brugia malayi in the leaf-monkey Presbytis cristata
    Mak JW, Suresh K, Lam PL, Choong MF, Striebel HP
    Trop. Med. Parasitol., 1990 Mar;41(1):10-2.
    PMID: 2339241
    CGP 20376, a 5-methoxyl-6-dithiocarbamic-S- (2-carboxy-ethyl) ester derivative of benzothiazole was evaluated for its antifilarial properties and shown to be extremely effective against subperiodic Brugia malayi in the leaf-monkey, Presbytis cristata at oral doses of 20-100 mg/kg. The compound and/or its metabolites had complete micro- and microfilaricidal activities even when given at a single dose of 20 mg/kg. Lower doses had incomplete filaricidal action.
    Matched MeSH terms: Thiazoles/administration & dosage; Thiazoles/pharmacology; Thiazoles/therapeutic use*
  3. Fulltext Natural Bioactive Thiazole-Based Peptides from Marine Resources: Structural and Pharmacological Aspects
    Dahiya R, Dahiya S, Fuloria NK, Kumar S, Mourya R, Chennupati SV, et al.
    Mar Drugs, 2020 Jun 24;18(6).
    PMID: 32599909 DOI: 10.3390/md18060329
    Peptides are distinctive biomacromolecules that demonstrate potential cytotoxicity and diversified bioactivities against a variety of microorganisms including bacteria, mycobacteria, and fungi via their unique mechanisms of action. Among broad-ranging pharmacologically active peptides, natural marine-originated thiazole-based oligopeptides possess peculiar structural features along with a wide spectrum of exceptional and potent bioproperties. Because of their complex nature and size divergence, thiazole-based peptides (TBPs) bestow a pivotal chemical platform in drug discovery processes to generate competent scaffolds for regulating allosteric binding sites and peptide-peptide interactions. The present study dissertates on the natural reservoirs and exclusive structural components of marine-originated TBPs, with a special focus on their most pertinent pharmacological profiles, which may impart vital resources for the development of novel peptide-based therapeutic agents.
    Matched MeSH terms: Thiazoles/chemistry*
  4. Evaluation of a broad spectrum anthelminthic tetramisole on threadworms
    Ghee CG
    Med J Malaya, 1970 Mar;24(3):218-20.
    PMID: 4246805
    Matched MeSH terms: Thiazoles/therapeutic use*
  5. Fulltext Multipotent Cholinesterase Inhibitors for the Treatment of Alzheimer's Disease: Synthesis, Biological Analysis and Molecular Docking Study of Benzimidazole-Based Thiazole Derivatives
    Hussain R, Ullah H, Rahim F, Sarfraz M, Taha M, Iqbal R, et al.
    Molecules, 2022 Sep 18;27(18).
    PMID: 36144820 DOI: 10.3390/molecules27186087
    Twenty-four analogues of benzimidazole-based thiazoles (1-24) were synthesized and assessed for their in vitro acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory potential. All analogues were found to exhibit good inhibitory potential against cholinesterase enzymes, having IC50 values in the ranges of 0.10 ± 0.05 to 11.10 ± 0.30 µM (for AChE) and 0.20 ± 0.050 µM to 14.20 ± 0.10 µM (for BuChE) as compared to the standard drug Donepezil (IC50 = 2.16 ± 0.12 and 4.5 ± 0.11 µM, respectively). Among the series, analogues 16 and 21 were found to be the most potent inhibitors of AChE and BuChE enzymes. The number (s), types, electron-donating or -withdrawing effects and position of the substituent(s) on the both phenyl rings B & C were the primary determinants of the structure-activity relationship (SAR). In order to understand how the most active derivatives interact with the amino acids in the active site of the enzyme, molecular docking studies were conducted. The results obtained supported the experimental data. Additionally, the structures of all newly synthesized compounds were elucidated by using several spectroscopic methods like 13C-NMR, 1H-NMR and HR EIMS.
    Matched MeSH terms: Thiazoles/pharmacology
  6. Synthesis, in vitro α-glucosidase inhibitory activity and molecular docking studies of new thiazole derivatives
    Khan KM, Qurban S, Salar U, Taha M, Hussain S, Perveen S, et al.
    Bioorg Chem, 2016 10;68:245-58.
    PMID: 27592296 DOI: 10.1016/j.bioorg.2016.08.010
    Current study based on the synthesis of new thiazole derivatives via "one pot" multicomponent reaction, evaluation of their in vitro α-glucosidase inhibitory activities, and in silico studies. All synthetic compounds were fully characterized by (1)H NMR, (13)C NMR and EIMS. CHN analysis was also performed. These newly synthesized compounds showed activities in the range of IC50=9.06±0.10-82.50±1.70μM as compared to standard acarbose (IC50=38.25±0.12μM). It is worth mentioning that most of the compounds such as 1 (IC50=23.60±0.39μM), 2 (IC50=22.70±0.60μM), 3 (IC50=22.40±0.32μM), 4 (IC50=26.5±0.40μM), 6 (IC50=34.60±0.60μM), 7 (IC50=26.20±0.43μM), 8 (IC50=14.06±0.18μM), 9 (IC50=17.60±0.28μM), 10 (IC50=27.16±0.41μM), 11 (IC50=19.16±0.19μM), 12 (IC50=9.06±0.10μM), 13 (IC50=12.80±0.21μM), 14 (IC50=11.94±0.18μM), 15 (IC50=16.90±0.20μM), 16 (IC50=12.60±0.14μM), 17 (IC50=16.30±0.29μM), and 18 (IC50=32.60±0.61μM) exhibited potent inhibitory potential. Molecular docking study was performed in order to understand the molecular interactions between the molecule and enzyme. Newly identified α-glucosidase inhibitors except few were found to be completely non-toxic.
    Matched MeSH terms: Thiazoles/chemical synthesis; Thiazoles/pharmacology*; Thiazoles/chemistry
  7. Synthesis of Competitive and Noncompetitive Inhibitors of Alpha-Glucosidase and Anticancer Agents
    Ghani U, Syed SA, Aljunidel S, Khan AA, Nur-E-Alam M, AlNoshan A, et al.
    Chem Biodivers, 2024 May;21(5):e202301399.
    PMID: 38393939 DOI: 10.1002/cbdv.202301399
    Imidazoles and phenylthiazoles are an important class of heterocycles that demonstrate a wide range of biological activities against various types of cancers, diabetes mellitus and pathogenic microorganisms. The heterocyclic structure having oxothiazolidine moiety is an important scaffold present in various drugs, with potential for enzyme inhibition. In an effort to discover new heterocyclic compounds, we synthesized 26 new 4,5-diphenyl-1H-imidazole, phenylthiazole, and oxothiazolidine heterocyclic analogues that demonstrated potent α-glucosidase inhibition and anticancer activities. Majority of the compounds noncompetitively inhibited α-glucosidase except for two that exhibited competitive inhibition of the enzyme. Docking results suggested that the noncompetitive inhibitors bind to an apparent allosteric site on the enzyme located in the vicinity of the active site. Additionally, the analogues also exhibited significant activity against various types of cancers including non-small lung cancer. Since tubulin protein plays an important role in the pathogenesis of non-small lung cancer, molecular docking with one of the target compounds provided important clues to its binding mode. The current work on imidazoles and phenylthiazole derivatives bears importance for designing of new antidiabetic and anticancer drugs.
    Matched MeSH terms: Thiazoles/chemical synthesis; Thiazoles/pharmacology; Thiazoles/chemistry
  8. Synthesis, in vitro β-glucuronidase inhibitory activity and in silico studies of novel (E)-4-Aryl-2-(2-(pyren-1-ylmethylene)hydrazinyl)thiazoles
    Salar U, Khan KM, Syed S, Taha M, Ali F, Ismail NH, et al.
    Bioorg Chem, 2017 02;70:199-209.
    PMID: 28069264 DOI: 10.1016/j.bioorg.2016.12.011
    Current research is based on the synthesis of novel (E)-4-aryl-2-(2-(pyren-1-ylmethylene)hydrazinyl)thiazole derivatives (3-15) by adopting two steps route. First step was the condensation between the pyrene-1-carbaldehyde (1) with the thiosemicarbazide to afford pyrene-1-thiosemicarbazone intermediate (2). While in second step, cyclization between the intermediate (2) and phenacyl bromide derivatives or 2-bromo ethyl acetate was carried out. Synthetic derivatives were structurally characterized by spectroscopic techniques such as EI-MS, 1H NMR and 13C NMR. Stereochemistry of the iminic double bond was confirmed by NOESY analysis. All pure compounds 2-15 were subjected for in vitro β-glucuronidase inhibitory activity. All molecules were exhibited excellent inhibition in the range of IC50=3.10±0.10-40.10±0.90μM and found to be even more potent than the standard d-saccharic acid 1,4-lactone (IC50=48.38±1.05μM). Molecular docking studies were carried out to verify the structure-activity relationship. A good correlation was perceived between the docking study and biological evaluation of active compounds.
    Matched MeSH terms: Thiazoles/pharmacology*; Thiazoles/chemistry*
  9. Fulltext Comparative performance of two commercial neonicotinoid baits against filth flies under field conditions
    Nurita AT, Abu Hassan A
    Trop Biomed, 2010 Dec;27(3):559-65.
    PMID: 21399598 MyJurnal
    Two performance (efficacy and attractiveness) comparisons of neonicotinoid baits QuickBayt® (imidacloprid) and Agita® (thiamethoxam) against filth flies were conducted under field conditions to determine suitability for use outdoors. The first experiment compared bait performance and the second compared effects of different applications on QuickBayt® performance. Applications compared were: (i) scattered in petri dish (SPD); (ii) wet-down in petri dish (WPD); (iii) scattered on cardboard (SCB) and (iv) painted on cardboards (PCB). Efficacy and attractiveness were assessed based on knockdown percentage (KD%) and number of flies feeding on baits, respectively. The KD% of QuickBayt® (34% ± 3.0%) was not significantly higher than Agita® (29% ± 1.3%) (t-test, P>0.05). Agita® (101 ± 5.7 flies) was significantly more attractive to flies than QuickBayt® (76 ± 4.8 flies) and the sugar solution (49 ± 7.2) (one-way ANOVA, P<0.05). The PCB and SCB applications were significantly more attractive to filth flies than WPD and SPD (One-way ANOVA, P<0.05), however differences in KD% were not significantly different (One-way ANOVA, P>0.05). The two baits provided the same level of efficacy in a wide-open area against filth flies of various species. QuickBayt® was more versatile; efficacy was not significantly affected by different applications. Surface area and moisture affects attractiveness of the bait.
    Matched MeSH terms: Thiazoles/pharmacology*; Thiazoles/chemistry
  10. Improved protein deproteinization method for the determination of meloxicam in human plasma and application in pharmacokinetic study
    Liew KB, Loh GO, Tan YT, Peh KK
    Biomed Chromatogr, 2014 Dec;28(12):1782-8.
    PMID: 24788875 DOI: 10.1002/bmc.3221
    A simple, rapid, specific and reliable high-performance liquid chromatographic assay of meloxicam in human plasma has been developed using a C18 reversed-phase analytical column. Reversed-phase chromatography was conducted using a mobile phase of 0.02 potassium dihydrogen phosphate (adjusted to pH 2.7 with phosphoric acid)-acetonitrile-triethylamine (35:65:0.05, v/v) with UV detection at 354 nm. The drug in human plasma was deproteinized using a combination of methanol and chloroform. This method is simple, rapid and consistent with a high recovery of meloxicam in human plasma ranging from 93.29 to 111.09%. Regression analysis for the calibration plot for plasma standards obtained for the drug concentrations between (25-4000) ng/mL indicated excellent linearity (r ≥ 0.9997). The proposed method was applied to study the bioequivalence between Mobic (original) and Melocam (generic) products. The study was conducted on using two tablets (4 × 7.5 mg) of each of the commercial product and the reference standard in a two-way open randomized crossover design involving 20 volunteers. Area under the concentration-time curve, peak concentration (C(max)) and time to reach C(max) were 72,868.61 ng h/mL, 2133.93 ng/mL and 4.06 h for Mobic, and 78,352.52 ng h/mL, 2525.18 ng/mL and 3.61 h for Melocam. Two C(max) were discovered in the pharmacokinetic profiles which confirm enterohepatic recirculation.
    Matched MeSH terms: Thiazoles/adverse effects; Thiazoles/blood*; Thiazoles/pharmacokinetics*; Thiazoles/chemistry
  11. 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: Thiazoles/pharmacology*; Thiazoles/chemistry
  12. New Hybrid Scaffolds based on Hydrazinyl Thiazole Substituted Coumarin; As Novel Leads of Dual Potential; In Vitro α-Amylase Inhibitory and Antioxidant (DPPH and ABTS Radical Scavenging) Activities
    Salar U, Khan KM, Chigurupati S, Syed S, Vijayabalan S, Wadood A, et al.
    Med Chem, 2019;15(1):87-101.
    PMID: 30179139 DOI: 10.2174/1573406414666180903162243
    BACKGROUND: Despite many side effects associated, there are many drugs which are being clinically used for the treatment of type-II diabetes mellitus (DM). In this scenario, there is still need to develop new therapeutic agents with more efficacy and less side effects. By keeping in mind the diverse spectrum of biological potential associated with coumarin and thiazole, a hybrid class based on these two heterocycles was synthesized.

    METHOD: Hydrazinyl thiazole substituted coumarins 4-20 were synthesized via two step reaction. First step was the acid catalyzed reaction of 3-formyl/acetyl coumarin derivatives with thiosemicarbazide to form thiosemicarbazone intermediates 1-3, followed by the reaction with different phenacyl bromides to afford products 4-20. All the synthetic analogs 4-20 were characterized by different spectroscopic techniques such as EI-MS, HREI-MS, 1H-NMR and 13C-NMR. Stereochemical assignment of the iminic double bond was carried out by the NOESY experiments. Elemental analysis was found in agreement with the calculated values.

    RESULTS: Compounds 4-20 were screened for α-amylase inhibitory activity and showed good activity in the range of IC50 = 1.829 ± 0.102-3.37 ± 0.17 µM as compared to standard acarbose (IC50 = 1.819 ± 0.19 µM). Compounds were also investigated for their DPPH and ABTS radical scavenging activities and displayed good radical scavenging potential. In addition to that molecular modelling study was conducted on all compounds to investigate the interaction details of compounds 4- 20 (ligands) with active site (receptor) of enzyme.

    CONCLUSION: The newly identified hybrid class may serve as potential lead candidates for the management of diabetes mellitus.

    Matched MeSH terms: Thiazoles/chemical synthesis; Thiazoles/chemistry*
  13. Synthesis and structure-activity relationship of elastase inhibiting novel ethylated thiazole-triazole acetamide hybrids: Mechanistic insights through kinetics and computational contemplations
    Butt ARS, Abbasi MA, Aziz-Ur-Rehman, Siddiqui SZ, Hassan M, Raza H, et al.
    Bioorg Chem, 2019 05;86:197-209.
    PMID: 30711702 DOI: 10.1016/j.bioorg.2019.01.040
    Keeping in mind the pharmacological importance of 2-aminothiazole and 1,2,4-triazole heterocyclic moieties, a series of novel ethylated bi-heterocyclic acetamide hybrids, 9a-p, was synthesized in a multi-step protocol. The structures of newly synthesized compounds were characterized by 1H NMR, 13C NMR, IR and EI-MS spectral studies. The inhibitory effects of these bi-heterocyclic acetamides (9a-n) were evaluated against elastase and all these molecules were identified as potent inhibitors relative to the standard used. The Kinetics mechanism was analyzed by Lineweaver-Burk plots which revealed that, 9h, inhibited elastase competitively by forming an enzyme-inhibitor complex. The inhibition constants Ki calculated from Dixon plots for this compound was 0.9 µM. The computational study was articulate with the experimental results and these ligands unveiled good binding energy values (kcal/mol). So, these molecules can be considered as promising medicinal scaffolds for the treatment of skin melanoma, wrinkle formation, uneven pigmentation, and solar elastosis.
    Matched MeSH terms: Thiazoles/pharmacology*; Thiazoles/chemistry
  14. New triazinoindole bearing thiazole/oxazole analogues: Synthesis, α-amylase inhibitory potential and molecular docking study
    Rahim F, Tariq S, Taha M, Ullah H, Zaman K, Uddin I, et al.
    Bioorg Chem, 2019 11;92:103284.
    PMID: 31546207 DOI: 10.1016/j.bioorg.2019.103284
    New triazinoindole bearing thiazole/oxazole analogues (1-21) were synthesized and characterized through spectroscopic techniques such as HREI-MS, 1H and 13C NMR. The configuration of compound 2i and 2k was confirmed through NOESY. All analogues were evaluated against α-amylase inhibitory potential. Among the synthesized analogues, compound 1h, 1i, 1j, 2a and 2f having IC50 values 1.80 ± 0.20, 1.90 ± 0.30, 1.2 ± 0.30, 1.2 ± 0.01 and 1.30 ± 0.20 μM respectively, showed excellent α-amylase inhibitory potential when compared with acarbose as standard (IC50 = 0.91 ± 0.20 µM). All other analogues showed good to moderate inhibitory potential. Structural activity relationship (SAR) has been established and binding interactions were confirmed through docking studies.
    Matched MeSH terms: Thiazoles/pharmacology*; Thiazoles/chemistry
  15. Effect of nitazoxanide on diarrhea: A systematic review and network meta-analysis of randomized controlled trials
    Hashan MR, Elhusseiny KM, Huu-Hoai L, Tieu TM, Low SK, Minh LHN, et al.
    Acta Trop, 2020 Oct;210:105603.
    PMID: 32598920 DOI: 10.1016/j.actatropica.2020.105603
    We aimed to systematically review evidence pertaining to the safety and efficacy of nitazoxanide in treating infectious diarrhea. On September 21, 2017, we identified relevant studies using 12 databases. The estimates of the included studies were pooled as a risk ratio (RR). We conducted a network and pairwise random-effects meta-analysis for both direct and indirect comparisons of different organisms that are known to cause diarrhea. The primary and secondary analysis outcomes were clinical response until cessation of illness, parasitological response and adverse events. We included 18 studies in our analysis. In cryptosporidiosis, the overall estimate favored nitazoxanide in its clinical response in comparison with placebo RR 1.46 [95% CI 1.22-1.74; P-value <0.0001]. Network meta-analysis among patients with Giardia intestinalis showed an increase in the probability of diarrheal cessation and parasitological responses in comparison with placebo, RR 1.69 [95% CI 1.08-2.64, P-score 0.27] and RR 2.91 [95% CI 1.72-4.91, P-score 0.55] respectively. In Clostridium difficile infection, the network meta-analysis revealed a non-significantly superior clinical response effect of nitazoxanide to metronidazole 31 days after treatment RR 1.21 [95% CI 0.87-1.69, P-score 0.26]. In Entamoeba histolytica, the overall estimate significantly favored nitazoxanide in parasitological response with placebo RR 1.80 [95% CI 1.35-2.40, P-value < 0.001]. We highlighted the effectiveness of nitazoxanide in the cessation of diarrhea caused by Cryptosporidium, Giardia intestinalis and Entamoeba histolytica infection. We also found significant superiority of NTZ to metronidazole in improving the clinical response to G. intestinalis, thus it may be a suitable candidate for treating infection-induced diarrhea. To prove the superiority of NTZ during a C. difficile infection may warrant a larger-scale clinical trial since its superiority was deemed insignificant. We recommend nitazoxanide as an appropriate option for treating infectious diarrhea.
    Matched MeSH terms: Thiazoles/adverse effects; Thiazoles/therapeutic use*
  16. Semicarbazones, thiosemicarbazone, thiazole and oxazole analogues as monoamine oxidase inhibitors: Synthesis, characterization, biological evaluation, molecular docking, and kinetic studies
    Qazi SU, Naz A, Hameed A, Osra FA, Jalil S, Iqbal J, et al.
    Bioorg Chem, 2021 10;115:105209.
    PMID: 34364054 DOI: 10.1016/j.bioorg.2021.105209
    A series of semicarbazone, thiosemicarbazone, thiazole, and oxazole derivatives were designed, synthesized, and examined for monoamine oxidase inhibition using two isoforms, i.e., MAO-A and MAO-B. Among all the analogues, 3c and 3j possessed substantial activity against MAO-A with IC50 values of 5.619 ± 1.04 µM and 0.5781 ± 0.1674 µM, respectively. Whereas 3d and 3j were active against monoamine oxidase B with the IC50 values of 9.952 ± 1.831 µM and 3.5 ± 0.7 µM, respectively. Other derivatives active against MAO-B were 3c and 3g with the IC50 values of 17.67 ± 5.6 µM and 37.18 ± 2.485 µM. Moreover, molecular docking studies were achieved for the most potent compound (3j) contrary to human MAO-A and MAO-B. Kinetic studies were also performed for the most potent analogue to evaluate its mode of interaction with MAO-A and MAO-B.
    Matched MeSH terms: Thiazoles/pharmacology*; Thiazoles/chemistry
  17. 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: Thiazoles/chemical synthesis*; Thiazoles/pharmacology*
  18. Synthetic nanoparticle-conjugated bisindoles and hydrazinyl arylthiazole as novel antiamoebic agents against brain-eating amoebae
    Kanwal, Mungroo MR, Anwar A, Ali F, Khan S, Abdullah MA, et al.
    Exp Parasitol, 2020 Nov;218:107979.
    PMID: 32866583 DOI: 10.1016/j.exppara.2020.107979
    Balamuthia mandrillaris and Naegleria fowleri are free-living amoebae that can cause life-threatening infections involving the central nervous system. The high mortality rates of these infections demonstrate an urgent need for novel treatment options against the amoebae. Considering that indole and thiazole compounds possess wide range of antiparasitic properties, novel bisindole and thiazole derivatives were synthesized and evaluated against the amoebae. The antiamoebic properties of four synthetic compounds i.e., two new bisindoles (2-Bromo-4-(di (1H-indol-3-yl)methyl)phenol (denoted as A1) and 2-Bromo-4-(di (1H-indol-3-yl)methyl)-6-methoxyphenol (A2)) and two known thiazole (4-(3-Nitrophenyl)-2-(2-(pyridin-3-ylmethylene)hydrazinyl)thiazole (A3) and 4-(Biphenyl-4-yl)-2-(2-(1-(pyridin-4-yl)ethylidene)hydrazinyl)thiazole (A4)) were evaluated against B. mandrillaris and N. fowleri. The ability of silver nanoparticle (AgNPs) conjugation to enrich antiamoebic activities of the compounds was also investigated. The synthetic heterocyclic compounds demonstrated up to 53% and 69% antiamoebic activities against B. mandrillaris and N. fowleri respectively, while resulting in up to 57% and 68% amoebistatic activities, respectively. Antiamoebic activities of the compounds were enhanced by up to 71% and 51% against B. mandrillaris and N. fowleri respectively, after conjugation with AgNPs. These compounds exhibited potential antiamoebic effects against B. mandrillaris and N. fowleri and conjugation of synthetic heterocyclic compounds with AgNPs enhanced their activity against the amoebae.
    Matched MeSH terms: Thiazoles
  19. Determination of optimal extraction time and temperature by response surface methodology to obtain high-level antioxidant activity in culinary-medicinal oyster mushroom, Pleurotus ostreatus (Jacq.:Fr.) P. Kumm. (higher basidiomycetes)
    Lim SM, Yim HS
    Int J Med Mushrooms, 2012;14(6):593-602.
    PMID: 23510253
    A central composite design of response surface methodology (RSM) was employed to optimize the extraction time (X1: 266.4-393.6 min) and temperature (X2: 42.9-57.1°C) of Pleurotus ostreatus aqueous extract with high antioxidant activities, namely DPPH radical-scavenging activity, ABTS radical cation inhibition, and ferric reducing/antioxidant power, as well as total phenolic content (TPC). Results showed that the data were adequately fitted into four second-order polynomial models developed by RSM. The extraction time and temperature were found to have significant quadratic effects on antioxidant activities and TPC. The optimal extraction time and temperature were 282.3 min and 42.9°C (DPPH), 393.6 min and 42.9°C (ABTS), 340.4 min and 49.8°C (FRAP), and 347.6 min, 49.7°C (TPC), with corresponding yields of 53.32%, 73.20%, 37.14 mM Fe2+ equivalents/100 g, and 826.33 mg gallic acid equivalents/100 g, respectively. These experimental data were close to their predicted values. The establishment of such a model provides a good experimental basis for employing RSM to optimize the extraction time and temperature for high antioxidant activities from P. ostreatus.
    Matched MeSH terms: Thiazoles; Benzothiazoles
  20. Ziprasidone-loaded arabic gum modified montmorillonite-tailor-made pectin based gastroretentive composites
    Bera H, Abbasi YF, Yoke FF, Seng PM, Kakoti BB, Ahmmed SKM, et al.
    Int J Biol Macromol, 2019 May 15;129:552-563.
    PMID: 30707999 DOI: 10.1016/j.ijbiomac.2019.01.171
    Novel diethanolamine-grafted high-methoxyl pectin (DGP)-arabic gum (AG) modified montmorillonite (MMT) composites were developed for intragastric ziprasidone HCl (ZIP) delivery by combining floating and mucoadhesion mechanisms. The ZIP-loaded clay-biopolymer matrices were accomplished by ionotropic gelation protocol utilizing zinc acetate in the presence or absence of covalent crosslinker, glutaraldehyde (GA). Various formulations exhibited excellent drug entrapment efficiency (DEE, %) and sustained drug release profiles, which were influenced by the polymer-blend (DGP:AG) ratios, reinforcing filler (MMT) existence and crosslinking procedure. The optimal composites (F-3) demonstrated DEE of 61% and Q8h of 52% with outstanding buoyancy, mucin adsorption ability and biodegradability. The release profile of F-3 was best fitted in the Korsmeyer-Peppas model with Fickian diffusion driven mechanism. The mucin adsorption to composites F-3 followed Freundlich isotherms. The molar mass between crosslinks of composites (F-3) calculated employing Flory-Rehner equation was increased with temperature. Moreover, the thermal, X-ray and infrared analyses confirmed a compatible environment of drug in the composites, except certain extent of transformation of the crystalline drug to its amorphous form. The SEM studies revealed the spherical morphology of the composites. Thus, the newly developed DGP-AG-MMT composites are appropriate for gastroretentive ZIP delivery over an extended period of time.
    Matched MeSH terms: Thiazoles/chemistry*
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