Materials Science and Engineering / Malzeme Bilimi ve Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/4719
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Article Citation - WoS: 18Citation - Scopus: 20A Simple Desolvation Method for Production of Cationic Albumin Nanoparticles With Improved Drug Loading and Cell Uptake(Editions de Sante, 2020) Sözer, Sümeyra Çiğdem; Akdoğan, Yaşar; Başol, Merve; Çakan Akdoğan, Gülçin; Sözer, Sümeyra Çiğdem; 03.09. Department of Materials Science and Engineering; 01. Izmir Institute of Technology; 03. Faculty of EngineeringThe transport protein albumin has been used as a drug nanocarrier for a long time due to its versatility. Albumin is negatively charged at physiological conditions limiting its anionic drug loading capacity. However, loading of anionic drugs in the albumin nanoparticles (NPs), can be facilitated by albumin cationization. Here, we postulate a simple desolvation method for preparation of cationic albumin NPs with improved anionic drug loading. First, bovine serum albumin was cationized with ethylenediamine. Next, salicylic acid (SA) was added to the cationic bovine serum albumin (cBSA) solution prior to the desolvation. Among different desolvating agents tested, acetonitrile allowed the highest nanoparticle formation yield. The SEM analyses showed that the average size of cBSA NPs decreased from ~200 nm to ~100 nm upon SA loading. Moreover, the drug loading capacity of cBSA NPs was found to increase ~2 fold, and drug release was slower compared to BSA NPs. Finally, a significant increase in cellular uptake of cBSA NPs compared to that of native BSA NPs showed the potential for improved drug delivery. © 2020 Elsevier B.V.Article Citation - WoS: 33Citation - Scopus: 36Epr Studies of Intermolecular Interactions and Competitive Binding of Drugs in a Drug-Bsa Binding Model(Royal Society of Chemistry, 2016) Akdoğan, Yaşar; Emrullahoğlu, Mustafa; Akdoğan, Yaşar; Üçüncü, Muhammed; Çakan Akdoğan, Gülçin; Emrullahoğlu, Mustafa; 03.09. Department of Materials Science and Engineering; 04.04. Department of Photonics; 03. Faculty of Engineering; 04. Faculty of Science; 01. Izmir Institute of TechnologyUnderstanding intermolecular interactions between drugs and proteins is very important in drug delivery studies. Here, we studied different binding interactions between salicylic acid and bovine serum albumin (BSA) using electron paramagnetic resonance (EPR) spectroscopy. Salicylic acid was labeled with a stable radical (spin label) in order to monitor its mobilized (free) or immobilized (bound to BSA) states. In addition to spin labeled salicylic acid (SL-salicylic acid), its derivatives including SL-benzoic acid, SL-phenol, SL-benzene, SL-cyclohexane and SL-hexane were synthesized to reveal the effects of various drug binding interactions. EPR results of these SL-molecules showed that hydrophobic interaction is the main driving force. Whereas each of the two functional groups (-COOH and -OH) on the benzene ring has a minute but detectable effect on the drug-protein complex formation. In order to investigate the effect of electrostatic interaction on drug binding, cationic BSA (cBSA) was synthesized, altering the negative net charge of BSA to positive. The salicylic acid loading capacity of cBSA is significantly higher compared to that of BSA, indicating the importance of electrostatic interaction in drug binding. Moreover, the competitive binding properties of salicylic acid, ibuprofen and aspirin to BSA were studied. The combined EPR results of SL-salicylic acid/ibuprofen and SL-ibuprofen/salicylic acid showed that ibuprofen is able to replace up to ∼83% of bound SL-salicylic acid, and salicylic acid can replace only ∼14% of the bound SL-ibuprofen. This indicates that ∼97% of all salicylic acid and ibuprofen binding sites are shared. On the other hand, aspirin replaces only ∼23% of bound SL-salicylic acid, and salicylic acid replaces ∼50% of bound SL-aspirin, indicating that ∼73% of all salicylic acid and aspirin binding sites are shared. These results show that EPR spectroscopy in combination with the spin labeling technique is a very powerful method to investigate drug binding dynamics in detail.