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    Synthesis, biological evaluation and molecular docking studies of 8-(hetero)aryl caffeine derivatives
    (Elsevier Science Sa, 2023) Khan, Siraj; Bugday, Nesrin; Yasar, Seyma; Rehman, Asim Ur.; Ul Haq, Ihsan; Yasar, Sedat
    A series of 8-(hetero)aryl caffeine was synthesized by the C -H bond activation reaction using Pd-NHCs complexes as a catalyst. 8-(hetero)aryl caffeine derivatives were screened for their antioxidant, antimicro-bial, and enzyme inhibitory activities and in-silico studies. The 4a, 4b, 4e, 4f, 4 g, 4i, and 4n showed sig-nificant total antioxidant capacity (TAC) of 64.03, 50.87, 70.02, 98.14, 71.81, 45.48, and 44.28 & mu;g AAE/mg, respectively. The 4a, 4b, 4d, 4e, 6 h, 4i, 4j, 4k, and 4l were found active against Staphylococcus aureus at a minimum inhibitory concentration of 25, 12.5, 12.5, 12.5, 12.5, 6.25, 6.25, 6.25, and 6.25 & mu;g/ml, respec-tively. Some derivatives displayed activity against Escherichia coli, Bacillus subtilus, Klebsiella pneumonae, and Pseudomonas aeruginosa.A good activity was exhibited against Alternaria solani among five fungal strains. All the com-pounds (4a-4n) showed excellent protein kinase inhibitory activity except 4e, 4 g, and 4n. Addition-ally, 8-(hetero)aryl caffeine derivatives showed & alpha;-amylase inhibition potential (IC50 = 1.49 & PLUSMN; 0.317 to 7.44 & PLUSMN; 0.156 & mu;g/ml) compared to standard acarbose (IC50 = 4.34 & PLUSMN; 0.333 & mu;g/ml). The 4b, 4d, 4j, 4 m, and 4n compounds displayed good & alpha;-glucosidase inhibitory potential. Molecular modeling was done for protein kinase, & alpha;-amylase, and & alpha;-glucosidase. The results of these activities proved the caffeine deriva-tives to be bioactive.& COPY; 2023 Elsevier B.V. All rights reserved.
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    Synthesis, molecular docking, and biological evaluation of 5-alkyl(aryl)-2-isobutylthiazole derivatives: As ?-amylase, ?-glucosidase, and protein kinase inhibitors
    (Wiley, 2022) Khan, Siraj; Bugday, Nesrin; Rehman, Asim Ur; Ul Haq, Ihsan; Yasar, Sedat; Ozdemir, Ismail
    A series of 18 biologically active C5-arylated-2-isobutylthiazole derivatives that were synthesized by Pd-NHC complexes [Pd(mu-Cl)Cl (NHC)](2), NHC = SIXyl, 2), (LCl2Pd-NHC, L = PPh3, 3), (LCl2Pd-NHC, L = Py, 4), (LCl2Pd-NHC, L = 3-CHO-Py, 5) catalyzed C-H bond activation reactions. The catalytic activity of Pd-NHC complexes was examined on the C-H bond activation reaction of 2-isobutylthiazole. All Pd-NHC complexes were characterized by( 1)H nuclear magnetic resonance specroscopy (NMR), C-13 NMR, fouirer transform infrared spektroscopy (FTIR), quadrupole-time of flying-liquit cromotagraphy/mass spektroscopy (Q-TOF-LC/MS), gas chromatography-mass spectrometry (GCMS), and melting point detection technique. The physicochemical properties, pharmacokinetics, and drug-likeness were calculated by SwissADME. PkCSM database was used to calculate toxicities profile. All the products (6a-6s) were additionally assessed in vitro for their antidiabetic potential using alpha-amylase and alpha-glucosidase inhibitory activities. The protein kinase activity was performed to evaluate their anticancer activities. All the compounds possess drug-like characters as they followed Lipinski's rule of five (RO5). Almost all the compounds showed no to fewer toxicities. In addition, other than the compounds, that is, 6a, 6b, 6c, 6m, 6n, 6p, and 6s, the rest of the compounds showed good alpha-glucosidase inhibitory potential (IC50 7.17 +/- 0.201 to 74.08 +/- 0.244 mu g/ml) when compared with acarbose standard (IC50 16.59 +/- 0.135 mu g/ml). All compounds had moderate to good inhibitory potential against the alpha-amylase enzyme, with IC50 values ranging from 12.00 +/- 0.289 to 76.15 +/- 0.477 mu g/ml. Eleven analogs (6e, 6f, 6g, 6h, 6j, 6k, 6l, 6n, 6o, 6p, and 6r) showed good to moderate activity. Seven analogs (6a, 6b, 6c, 6d, 6i, 6m, and 6s) showed no alpha-amylase inhibitory activity. The protein kinase inhibition potential was determined for the first time, and the compounds 6d, 6e, 6f, 6h, 6k, 6p, and 6r depicted activity with the zone of inhibition in the range of 9 +/- 1.3 to 19 +/- 1.5 mm. The ligands and active site binding interactions of alpha-glucosidase, alpha-amylase, and protein kinase enzymes were also studied using molecular modeling.