Master Degree / Yüksek Lisans Tezleri

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

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Author: search.filters.author.Akdoğan, YaşarPublisher: search.filters.publisher.01. Izmir Institute of Technology

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  • Master Thesis
    Preparation and Characterization of Drug Loaded Cationic Albumin Nanoparticles
    (01. Izmir Institute of Technology, 2021) Akdoğan, Yaşar; Emrullahoğlu, Mustafa; Sözer, Sümeyra Çiğdem; Akdoğan, Yaşar; Emrullahoğlu, Mustafa; 03.09. Department of Materials Science and Engineering; 04.04. Department of Photonics; 01. Izmir Institute of Technology; 03. Faculty of Engineering; 04. Faculty of Science
    Serum albumin protein behaves as a carrier and transporter for both hydrophilic and hydrophobic drugs. Therefore, albumin could be used in the drug carrier systems. Since albumin nanoparticles have a negative charge under physiological conditions, their anionic drug loading and delivering capacities are restricted. This study aims to obtain higher anionic drug loading capacity by producing cationic bovine serum albumin nanoparticles (cBSA NPs). Firstly, the carboxyl groups of amino acids present on the surface of albumin were conjugated with ethylenediamine to change the charge of albumin from negative to positive. Then, cBSA NPs were obtained using the desolvation process. Anionic salicylic acid (SA) was used for drug loading studies of the obtained cBSA NPs. SA loading and releasing experiments were studied with UV-Vis and electron paramagnetic resonance (EPR) spectroscopy. In the UV-Vis, the drug loading capacity of cBSA NPs was found to increase ~2 fold, and drug release was slower compared to BSA NPs. For EPR studies, SA was labeled with stable radicals. Spin labels allow the simultaneous monitoring of bound and free drugs in the same sample. The drug was loaded into nanoparticles using two methods. Based on EPR results, it was found that drug was loaded to cBSA NPs with 50% and 93%, and to BSA NPs with 4% and 15% ratios, by desolvation and incubation, respectively. Thus, UV-vis and EPR measurements showed that cBSA NPs have higher SA loading potential and slower release ability compared to anionic albumin nanoparticles.
  • Master Thesis
    Preparation and Characterization of Serum Albumin Nanoparticles Obtained From Modified Bovine Serum Albumin
    (01. Izmir Institute of Technology, 2021) Akdoğan, Yaşar; Demir, Mustafa Muammer; Akdoğan, Yaşar; Demir, Mustafa Muammer; 03.09. Department of Materials Science and Engineering; 03. Faculty of Engineering; 01. Izmir Institute of Technology
    The serum albumin has been used as a drug nanocarrier for a long time due to its rich drug transportation ability. Here, modified bovine serum albumin (BSA) proteins were obtained by conjugation with ethylenediamine and dopamine molecules, separately. Using these modified proteins, new BSA nanoparticles were obtained by a desolvation method. Native BSA has a net negative charge at the physiological condition. However, ethylenediamine conjugation yields a positive charge on it, and thus produces cationic BSA (cBSA) protein. On the other hand, dopamine functionalization (D-BSA) makes BSA eager to coordinate with transition metals. After preparation of modified proteins (cBSA and D-BSA), their nanoparticles were prepared with desolvation method but using different crosslinking mechanisms. For cBSA NPs preparation, a traditional crosslinking agent of glutaraldehyde was used. However, for D-BSA NPs preparation, Fe(III) ions were added to the system to achieve the stable nanoparticle formation. In order to obtain cBSA NPs, several organic solvents were used as desolvating agents. cBSA NPs with an average size around 200 nm were obtained in a high formation yield (54.8%) only through addition of acetonitrile to the cBSA aqueous solution. Similarly, different desolvating agents were studied to obtain D-BSA NPs. The promising results were obtained upon addition of 1:5 (v/v) of water/acetone mixture. After addition of the desolvating agent, Fe(III) ions were added to the solution to interconnect D-BSA with each other. This connection is pH sensitive therefore albumin nanoparticles were stable at basic pH values but not at acidic pH values. By this way, pH sensitive D-BSA NPs around 300 nm particle sizes were obtained.