Investigation of the effects of thiazole compounds on thioredoxin reductase 1 (TrxR1), glutathione S-transferase (GST), and glutathione reductase (GR) targeted human brain glioblastoma cancer (U-87 MG).

Cancer is a fatal disease that kills thousands of people worldwide. Despite the information produced by research on cancer treatment, applications in cancer treatment are limited. Therefore, scientists' efforts to develop more effective treatment approaches continue.

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies.

Lactoperoxidase enzyme (LPO) is secreted from salivary, mammary, and other mucosal glands including the bronchi, lungs, and nose, which had functions as a natural and the first line of defense towards viruses and bacteria. In this study, methyl benzoates were examined in LPO enzyme activity. Methyl benzoates are used as precursors in the synthesis of aminobenzohydrazides used as LPO inhibitors.

Structure-Activity Relationship of Methyl 4-Aminobenzoate Derivatives as Being Drug Candidate Targeting Glutathione Related Enzymes: in Vitro and in Silico Approaches.

A thiol compound, glutathione, is essential for healthy cell defence against xenobiotics and oxidative stress. Glutathione reductase (GR) and glutathione S-transferase (GST) are two glutathione-related enzymes that function in the antioxidant and the detoxification systems. In this study, potential inhibitory effects of methyl 4-aminobenzoate derivatives on GR and GST were examined in vitro.

Inhibition Profiles and Molecular Docking Analysis of Benzohydrazide Derivatives on Red Blood Cell Carbonic Anhydrases Isozymes.

Background: Carbonic anhydrases (CAs, EC 4.2.1.

Synthesis and Anticancer Potential of New Hydroxamic Acid Derivatives as Chemotherapeutic Agents.

Histone deacetylase (HDAC) inhibitors have been shown to induce differentiation, cell cycle arrest, and apoptosis due to their low toxicity, inhibiting migration, invasion, and angiogenesis in many cancer cells. Studies show that hydroxamic acids are generally used as anticancers. For this reason, it is aimed to synthesize new derivatives of hydroxamic acids, to examine the anticancer properties of these candidate inhibitors, and to investigate the inhibition effects on some enzymes that cause multidrug resistance in cancer cells.

Biological evaluation and in silico study of benzohydrazide derivatives as paraoxonase 1 inhibitors.

Serum paraoxonase 1 (PON1) is found in all mammalian species and is a calcium-dependent hydrolytic enzyme. PON1 hydrolyze several substrates, including carbonates, esters, and organophosphates. In the current study, we aimed to investigate the effect of the presynthesized benzohydrazide derivatives (1-9) on PON1 activity.

2-Amino thiazole derivatives as inhibitors of some metabolic enzymes: An in vitro and in silico study.

The thiazole derivatives are desirable compounds in the evaluation of their biological activities such as antiprotozoal antibacterial, antifungal, antituberculosis. Considering the medical application potential of 2-amino thiazole compounds, we aimed to determine the effects of 2-amino thiazole derivatives on the activities of carbonic anhydrase I-II isoenzymes, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Among the chemicals we used in our study, 2-amino-4-(4-chlorophenyl)thiazole compound exhibited the best inhibition against hCA I with K of 0.

Methyl benzoate derivatives: in vitro Paraoxonase 1 inhibition and in silico studies.

Paraoxonase 1 (PON1) can metabolize some compounds such as aromatic carboxylic acid and unsaturated aliphatic esters, arylesters, cyclic carbonate, plucuronide drugs, some carbamate insecticide classes, nerve gases, and lactone compounds. Methyl benzoate has recently been shown to display potent toxicity against several insect species. In the current study, we aimed to investigate the effect of the methyl benzoate compounds (1-17) on PON1 activity.