Browsing by Author "Wolinska, Ewa"

Now showing 1 - 2 of 2

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