Browsing by Author "Rozbicki, Przemyslaw"

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Design, Synthesis, and Characterization of Novel Substituted 1,2,4-Triazines: Cytotoxic Activity on HepG2 and HT-29 Cell Lines, Enzyme Inhibition, and Molecular Docking Studies
(Wiley, 2025) Cetin, Adnan; Oguz, Ercan; Wolinska, Ewa; Rozbicki, Przemyslaw; Branowska, Danuta; Turkan, Fikret
1,2,4-Triazines exhibit various pharmacological properties due to their strong biological activities, such as anticancer, anti-inflammatory, antimicrobial, antiviral, and antioxidant, and also occupy an important place in the pharmaceutical field. The tested compounds were synthesized and characterized. 1,2,4-Triazines were evaluated for their inhibitory and cytotoxicity effects on acetylcholinesterase (AChE), glutathione S-transferase (GST), human liver cancer cell line (HepG2), and human colorectal adenocarcinoma cell line (HT-29). 1,2,4-Triazines (3a-c, 5, 6, 10) were found to inhibit these enzymes with IC50 values ranging from 1.41 to 4.28 mu M for AChE and from 1.58 to 4.13 mu M for GST. 1,2,4-Triazine compounds were tested in range of 12.5-100 mu M concentrations against HepG2 and HT-29 cell lines. Among the 1,2,4-triazines tested, 10 was the most effective substance on HepG2 cells, especially at high doses, while 3b was effective on HT-29. Furthermore, molecular docking results indicated that the 1,2,4-triazines showed strong binding and stability at the active site of enzymes and selected proteins. 1,2,4-Triazines may serve as promising precursors for the design of potent enzyme inhibitors and anticancer agents.
Pharmacological Assessment of Disulfide-Triazine Hybrids: Synthesis, Enzyme Inhibition, and Molecular Docking Study
(Springer Birkhauser, 2024) Turkan, Fikret; Cetin, Adnan; Rozbicki, Przemyslaw; Oguz, Ercan; Wolinska, Ewa; Branowska, Danuta
Acetylcholinesterase (AChE) is indispensable for neurotransmission, while glutathione S-transferase (GST) plays a crucial role in cellular detoxification and protection. These enzymes are pivotal subjects in scientific investigations aimed at understanding neurological functions and maintaining cellular equilibrium. In pursuit of this objective, a set of disulfide-triazine hybrids (1, 2, and 3a-h) was effectively synthesized and methodically examined for their capacity to inhibit both AChE and GST (the Ki values for AChE range from 0.893 +/- 0.117 mu M to 7.961 +/- 0.421 mu M, while the IC50 values fall within the range of 1.919-6.243 mu M. For GST, the Ki values span from 2.093 +/- 0.276 mu M to 8.840 +/- 1.934 mu M, with IC50 values ranging from 2.152 to 4.747 mu M). After synthesizing the compounds and studying their biological effects, molecular docking analyses were conducted to understand how these compounds interact with target enzymes. This helped identify how the compounds bind and which amino acid residues are crucial for inhibition. The positive results highlight the potential of disulfide-triazine hybrids as strong inhibitors of AChE and GST, suggesting they could be further developed and optimized as therapeutic agents.
Synthesis and Examination of 1,2,4-Triazine Hybrids as Potential Inhibitory Drugs: Inhibition Effects on Ache and Gst Enzymes in Silico and in Vitro Conditions
(Wiley-v C H verlag Gmbh, 2024) Rozbicki, Przemyslaw; Oguz, Ercan; Wolinska, Ewa; Turkan, Fikret; Cetin, Adnan; Branowska, Danuta
The crucial functions of acetylcholinesterase (AChE) in neurotransmission and glutathione S-transferase (GST) in detoxification and cellular protection underscore their pivotal roles as key enzymes, essential for maintaining the integrity of neurological and cellular homeostasis. For this purpose, a series of 1,2,4-triazine-sulfonamide hybrids (3a-r) was successfully synthesized, and subsequently evaluated for their inhibitory effects on AChE and GST. The investigation was complemented by molecular docking studies and ADMET (Absorption, Distribution, Metabolism, Excretion, and Toxicity) predictions. The synthesized hybrids demonstrated significant promise in inhibiting both AChE and GST activities. Molecular docking analyses provided insights into the interactions between the compounds and the target enzymes, shedding light on potential binding modes and key amino acid residues involved. Furthermore, the study benefited from ADMET predictions, offering valuable information on the compounds' pharmacokinetic properties and potential toxicity. The promising results obtained from this comprehensive approach highlight the potential of these 1,2,4-triazine-sulfonamide hybrids as effective inhibitors of AChE and GST, paving the way for further development and optimization in the pursuit of novel therapeutic agents. A series of 1,2,4-triazine-sulfonamide hybrids (3a-r) was synthesized and evaluated for their inhibitory effects on acetylcholinesterase (AChE) and glutathione S-transferase (GST). The hybrids demonstrated promising inhibition of both AChE and GST activities. Molecular docking analyses provided insights into the interactions between the compounds and the target enzymes. image