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    Öğe
    Molecular docking and inhibition profiles of some antibiotics on lactoperoxidase enzyme purified from bovine milk
    (Taylor & Francis Inc, 2022) Kalin, Ramazan; Koksal, Zeynep; Bayrak, Songul; Gerni, Serpil; Ozyurek, Isil Nihan; Usanmaz, Hande; Karaman, Muhammet
    Antibiotics are generally used for human and veterinary applications to preserve and to control microbial diseases. Milk has a biologically significant enzyme known as lactoperoxidase (LPO) that is a member of peroxidase family. In metabolism, LPO has ability to catalyze the transformation of thiocyanate (SCN-) to hypothiocyanite (OSCN-) that is an antibacterial agent and the reaction occurs with hydrogen peroxide. In this work, LPO inhibition effects of some antibiotics including cefazolin, oxytetracycline, flunixin meglumine, cefuroxime, tylosin, vancomycin, chloramphenicol and lincomycin were tested. Among the antibiotics cefazolin was indicated the strongest inhibitory efficacy. The half maximal inhibitory concentration (IC50) and the inhibition constant (K-i) values of cefazolin were found as 8.19 and 34.66 mu M, respectively. It was shown competitive inhibition. 5-Methyl-1,3,4-thiadiazol-2-yl moiety activity plays a key role in the inhibition mechanism of cefazolin. Communicated by Ramaswamy H. Sarma
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    Öğe
    Synthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach
    (Elsevier, 2021) Tokali, Feyzi Sinan; Taslimi, Parham; Usanmaz, Hande; Karaman, Muhammet; Sendil, Kivilcim
    In this study, eight new Schiff base derivatives (2a-h) were synthesized and their inhibition activities against Acetylcholinesterase (AChE), Butyrylcholinesterase (BChE), alpha-Glucosidase and Lactoperoxidase (LPO) were investigated. Structures of the synthesized compounds were characterized using H-1 and C-13 nuclear magnetic resonance (NMR), infrared spectroscopy (IR), and high-resolution mass spectrometry (HRMS) spectroscopic methods. AChE was inhibited by these novel Schiff bases (2a-h) in low nanomolar levels, the K-i of which differed between 592.66 +/- 57.04 and 810.78 +/- 84.06 nM. Against BChE, the novel compounds demonstrated Kis varying from 358.31 +/- 37.88 to 577.24 +/- 59.91 nM. Also, these novel Schiff bases effectively inhibited alpha-glucosidase, with K-i values in the range of 1.56 +/- 0.32 to 14.78 +/- 2.57 nM. For LPO, K-i values were in the range of 3.96 +/- 0.37 to 12.75 +/- 0.06 nM. For alpha-glucosidase, the most effective molecules were 2b and 2 g with K-i values of 1.56 +/- 0.32 and 14.78 +/- 2.57 nM, respectively. Molecular docking results showed that the compounds have binding affinity with -5.559,-9.698, -7.606, and -6.971 kcal/mol against LPO, AChE, BChE, and alpha-glucosidase enzyme, respectively. It has been observed that the furan and thiosemicarbazone moieties play an important role in the inhibition of these enzymes. (C) 2020 Elsevier B.V. All rights reserved.