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Suitably substituted cinnamamides (3a-n) were successfully synthesized and tested for α-glucosidase inhibitory activity. Nine of the synthesized cinnamamides (3a-f, k-m) displayed moderate inhibitory activity, which was better than acarbose (IC50 = 185.00 ± 9.4 µM), with IC50 values ranging from 44.43 ± 5.7 to 91.14 ± 11.4 µM. Their α-glucosidase inhibitory activity greatly depended on their structure with electron-withdrawing groups on the cinnamoyl aromatic ring causing increased inhibition activity. According to the in vitro assay results, compound 3b with p-dimethylamino on the cinnamoyl ring has the best α-glucosidase inhibitory activity. The new synthesized cinnamamides (3b-i) showed acceptable physicochemical and pharmacokinetics characteristics with little toxicity indicating their potential use as lead drug candidates. Molecular docking studies of compound 3b (binding energy −8.33 kcal/mol) revealed that it interacted with His626 and two catalytic residues of α-glucosidase, namely Asp469 and Asp568. Overall, these cinnamamides show potential as lead structures for further optimization as α-glucosidase inhibitors. [ABSTRACT FROM AUTHOR]

4-Methoxyphenethyl (E)-3-(o-tolyl)acrylate (1) was obtained in a good yield by the reaction of 2-methylcinnamic acid, 4-methoxyphenethyl alcohol, 2-methyl-6-nitrobenzoic anhydride, 4-dimethylaminopyridine, and triethylamine at room temperature for 40 min. The structure of 4-methoxyphenethyl (E)-3-(o-tolyl)acrylate (1) was established by FTIR, NMR, and the high resolution of mass spectroscopies. 4-Methoxyphenethyl (E)-3-(o-tolyl)acrylate (1) showed higher α-glucosidase inhibition activity than standard drug acarbose. The molecular docking study exhibited that the title compound 1 had a good affinity for α-glucosidase (PDB ID: 3W37) and formed some interactions with the α-glucosidase active site residue. [ABSTRACT FROM AUTHOR]

The involvement of Fenton reaction on biodegradation of methyl orange (MO) by brown-rot fungus Fomitopsis pinicola was investigated based on Fe2+-dependent reaction. The degradation of MO (final concentration 75 mg/l) was performed in mineral salt media with and without Fe2+ with incubation period at 0, 7, 14, 21, and 28 days. Degradation analysis was performed using UV-Vis Spectrophotometer and LC-TOF/MS. F. pinicola decolorized MO in a medium containing Fe2+ and a medium that lacked the mineral, at percentages of 89.47% and 80.08%, respectively. The optimum decolorization occurred after 28 days of incubation with the fungus on the presence of Fe2+, indicated that the presence of Fe2+ enhanced MO degradation with assumed to correlate with Fenton reaction. Two metabolites were detected through the LC-TOF/MS analysis, namely 4-(2-(4-(dimethyliminio)-2-hydroxycyclohexa-2,5-dien-1-ylidene) hydrazinyl) phenolate (m/z 258, RT: 1.28 min, compound 1) and 4-(2-(4-(dimethyliminio) cyclohexa-2,5-dien-1-ylidene) hydrazinyl) benzenesulfonate (m/z 391, RT: 2.70 min, compound 2). Compound 1 was a transformation product of hydroxylation and methylation, compound 2 was a product of dehydroxylation and desulfonation. This study indicated that the transformation of the metabolite structures was involved hydroxyl radical (•OH) and enzymatic mechanisms, which involved Fe2+-dependent reaction. [ABSTRACT FROM AUTHOR]

Reports on a study which focused on the cloning and characterization of an Escherichia coli's gene in relation to the encoding of a transketolase-like enzyme. Synthesis of D-1-deoxyxylulose 5-phosphate; Methodology used to conduct the study; Results of the study.