Master Degree / Yüksek Lisans Tezleri

Permanent URI for this collectionhttps://hdl.handle.net/11147/3008

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  • Master Thesis
    The Evaluation of Antiproliferative and Structural Effects of Statins on Non-Small Lung Cancer Cell Line A549
    (Izmir Institute of Technology, 2019) Aksoy, Hatice Nurdan; Ceylan, Çağatay; Çağır, Ali
    Statins are commonly prescribed anti-lipidemic and anti-cholesterol class of drugs. In addition to their major role, they have been found to have anti-cancer effects on in vitro, animal and clinical studies. The aim of this study was to investigate the structural effects of 6 different statins (rosuvastatin, pravastatin, simvastatin, lovastatin, fluvastatin and atorvastatin) on A549 cells by a spectroscopic method. MTT viability tests were carried out to detect the half maximal inhibitory concentrations (IC50) of each statin on A549 cells. The IC50 values were 50 μM for simvastatin, 150 μM for atorvastatin and pravastatin, and 170 μM for fluvastatin, 200 μM for rosuvastatin and lovastatin on A549 cells. The cells were treated with IC5, IC10 and IC50 values of each statins concentration and their whole cell extracts and lipid extracts were compared using FTIR spectroscopy which is one of the most useful techniques to evaluate the structural changes at the macromolecular functional group level. The results indicated that different statins have different prominent effects on A549 cells. All the statins studied caused observable conformational changes on DNA and proteome of A549 cells. Whereas atorvastatin led to lipidation, lovastatin and pravastatin indicated enormous lipid-lowering properties. Based on the cell lipid extracts it was found that hydrocarbon chain length, unsaturation index, phospholipid containing lipids and carbonyl index showed increasing except for rosuvastatin-treated A549 cells. This study indicated that statins caused significant structural and compositional changes on A549 cells based on a spectroscopic evaluation.
  • Master Thesis
    Structural Investigation of Isopropanol and Alkaline Ph-Induced Trypsin Gel and Thin Flim and Its Biotechnological Applications
    (Izmir Institute of Technology, 2011) Karaçiçek, Bilge; Ceylan, Çağatay
    Trypsin is a biologically and industrially important member of serine protease family. Gelation forms a three dimensional network structure through the interaction of protein molecules among themselves and also with the environment. The aim of the study was the investigation of structural and the functional properties of bovine pancreatic trypsin after gelation and aggregation processes. The phase behaviour of trypsin was determined for different protein concentration, NaOH concentration and CaCl2 concentrations. In addition, the effect of sucrose addition to gelation time was observed. Increasing protein concentrations caused a decrease in gelation time. Increasing NaOH concentrations resulted in a decrease in gelation time. In low CaCl2 concentrations gelation was observed but in high CaCl2 concentrations aggregation was observed. The gels were resolubilized in water. Trypsin stability studies showed that there was a nearly 50% specific activity loss after the gelation process. According to FTIR studies β–sheet structure in 1637 cm-1 band disappeared in trypsin gel and trypsin aggregates. Increases in α–helix structure in 1651 cm-1 in trypsin gel with sucrose and aggregate with and without sucrose were observed. Iodoacetamide was shown to delay in gelation indicating the importance of intermolecular disulfides in the gelation process. The QCM studies showed that the film formed after gelation had absorbtion ability to different gases (benzene, carbon monoxide, carbon dioxide, dichloromethane, hydrogen peroxide and propanol) and can be used for gas sensing purposes. GI-XRD studies showed that trypsin thin film did not contain any crystalline structures.