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    Öğe
    Antioxidant activity and hemocompatibility study of quercetin loaded plga nanoparticles
    (Shaheed Beheshti Univ, Sch Pharmacy, 2020) Derman, Serap; Uzunoğlu, Deniz; Acar, Tayfun; Arasoğlu, Tulin; Uçak, Samet; Özalp, V. Cengiz; Mansuroğlu, Banu
    Quercetin (QU) is an important flavonoid compound presenting lots of biological activities, but its application has been limited due to its low aqueous solubility and instability. In this study, conducted to improve these properties of the quercetin, quercetin-encapsulated PLGA nanoparticles were prepared, characterized, and evaluated for antioxidant and hemolytic activity. Nanoparticles were produced by single emulsion solvent evaporation method. Four different process parameters initial QU amount, PVA concentration, PVA volume, and initial PLGA amount were investigated to obtain the nanoparticles which have minimum particle size and maximum entrapment efficiency. Synthesized nanoparticles were evaluated for particle size, entrapment efficiency, and reaction yield. Additionally, antioxidant properties and in-vitro hemolytic activity of quercetin loaded nanoparticles with different particle size were also evaluated for the first time in the literature. The antioxidant activity results showed that nanoparticles have different antioxidant activity, depending on the amount of quercetin release from nanoparticles at different particle sizes. The hemolytic activity results show that all nanoparticles exhibited favorable compatibility to red blood cells and no significant hemolytic effect was observed.
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    Öğe
    Evaluation of Bacteriophage ?11 host recognition protein and its host-binding peptides for diagnosing/targeting of Saphylococcus aureus infections
    (2024) Dokuz, Senanur; Taşdurmazlı, Semra; Acar, Tayfun; Duran, Gizem Nur; Özdemir, Çilem; Özbey, Utku; Özbil, Mehmet; Karadayı, Şükriye; Bayrak, Ömer Faruk; Derman, Serap; Chen, John Yu-Shen; Özbek, Tülin
    Evaluating the potential of using both synthetic and biological products as targeting agents for the diagnosis, imaging, and treatment of infections due to particularly antibiotic-resistant pathogens is important for controlling infections. We examined the interaction between Gp45, a receptor-binding protein of the ϕ11 lysogenic phage, and its host S. aureus, a common cause of nosocomial infections. Using molecular dynamics and docking simulations, we identified the peptides that bind to S. aureus wall teichoic acids via Gp45. We compared the binding affinity of Gp45 and the two highest-scoring peptide sequences (P1 and P3) and their scrambled forms using microscopy, spectroscopy, and ELISA. Our results revealed that rGp45 (recombinant Gp45) and chemically synthesized P1 had a higher binding affinity for S. aureus compared with all other peptides, with the exception of E. coli. Furthermore, rGp45 had a capture efficiency of over 86%; P1 had a capture efficiency of over 64%. Overall, our findings suggest that receptor-binding proteins such as rGp45, which provide a critical initiation of the phage life cycle for host adsorption, might play an important role in the diagnosis, imaging, and targeting of bacterial infections. Studying such proteins could accordingly enable the development of effective strategies for controlling infections.