Browsing by Author "Oguz, Ercan"

Now showing 1 - 4 of 4

Investigation of Interleukins and Oxidative Stress Parameters in Cows Naturally Infected With Bovine Viral Diarrhea Virus
(Univ Agriculture, Fac veterinary Science, 2024) Oguz, Fatma Ertas; Babaoglu, Ali Riza; Turkan, Fikret; Oguz, Ercan; Demirel, Ahmet Fatih; Pacal, Nurettin
Bovine Viral Diarrhea Virus (BVDV) can evade the immune system by modulating cytokines production, therefore enabling the virus to establish persistent infections or exacerbate the severity of disease in infected cattle. The objective of this research was to investigate interleukins and oxidative stress parameters in cows naturally infected with BVDV. The study comprised of two groups: a naturally infected group of 15 cattle with clinical signs of BVDV infection or a history of abortion and confirmed positive for pestivirus by RT-PCR, and a control group of 15 cattle with no abortion anamnesis or clinical symptoms, confirmed negative by RT-PCR. Anti-inflammatory cytokines (IL-4, IL-20, IL-10) and pro-inflammatory ones (IL-1, IL-1(3, IL-6) values were measured in all samples using ELISA method. Additionally, the oxidative stress marker malonaldehyde (MDA) was measured in all samples using the HPLC method. MDA levels were significantly higher in the infected samples compared with the controls. While cytokine levels were elevated in the infected group, however, the differences were not statistically significant. This study found a positive relationship among anti-inflammatory and pro-inflammatory cytokines, as well as a negative relationship among IL-1(3 and IL-1. It was concluded that oxidative stress occurs in BVDV-infected cattle, and the interleukins measured appear to remain in equilibrium by inhibiting each other. Notably, IL-20 was measured for the first time in BVDVinfected cattle, making it an important finding. Altogether, it may be concluded on the basis of these results that cytokines are important in the evaluation of the disease process.
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
Synthesis of 4-Diazocyclohexane Sulfonamide Drug Scaffolds: Investigating Enzyme Inhibition, Antioxidant, and Admet Properties
(Elsevier, 2025) Cetin, Adnan; Oguz, Ercan; Kazancioglu, Elif Akin; Guven, Betul; Kazancioglu, Mustafa Zahrittin; Turkan, Fikret
The inhibitory effects of several sulfonamide derivatives with a 4-diazocyclohexane backbone on alpha-glucosidase and alpha-amylase enzymes were explored. IC50 values for five sulfonamide derivatives were determined, ranging from 2.10 +/- 0.115 to 3.22 +/- 0.227 mu M for alpha-glucosidase and from 1.90 +/- 0.379 to 3.19 +/- 0.604 mu M for alpha-amylase. The results indicated that the inhibitory activity of these derivatives was comparable to the standard inhibitor acarbose. Additionally, the antioxidant potential of the sulfonamide derivatives was assessed using in vitro assays, including cupric ion (Cu2+) reduction, ferric ion (Fe3+) reduction (FRAP assay), DPPH radical scavenging, and ABTS+ radical scavenging methods. While no significant radical scavenging activity was observed in the ABTS assay, minimal antioxidant activity was detected in other methods compared to standard antioxidants. These findings suggest the potential of sulfonamide derivatives as dual enzyme inhibitors with limited antioxidant properties. Additionally, molecular docking and molecular dynamics (MD) simulations demonstrated the stability of 4-diazocyclohexane-based sulfonamide compounds-selected proteins complexes and provided detailed insights into 4a-e compounds-protein interactions at the molecular level. These findings formed the foundation for biologic activity these compounds with optimized binding properties and anticipated inhibitory activities. Moreover, an analysis of physicochemical descriptors and absorption, distribution, metabolism, excretion, and toxicity (ADMET) profiles was conducted to obtain deeper insights into ADMET properties in alpha-glucosidase and alpha-amylase candidate inhibitors.