Browsing by Subject "Catechin"

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    Catechin encapsulated antioxidant electrospun nanofibers: A comparative study between cyclodextrin complex nanofibers and poly(vinyl alcohol) nanofibers
    (American Chemical Society, 2023-05-31) Yıldız, Zehra İrem; Topuz, Fuat; Uyar, Tamer
    Catechin is a plant polyphenol with a strong antioxidant effect. However, its use is limited due to its poor water solubility and sensitivity to light and oxygen. Here, catechin could be solubilized by inclusion complexation with cyclodextrin (CD) (CD-IC), and their solutions were electrospun into fibers in the presence and absence of poly(vinyl alcohol) (PVA) to compare the stabilization of catechin for its antioxidant activity. The antioxidant activity of catechin/CD IC nanofibers was also compared to that of the powder form. Scanning electron microscopy (SEM) analysis revealed the production of bead-free nanofibers. The successful incorporation of catechin into nanofibers was confirmed by Fourier-transform infrared spectroscopy (FTIR) analysis of catechin CC bond stretching. Likewise, 1H NMR spectroscopic analysis revealed the characteristic aromatic protons of catechin. The formation of inclusion complexes was confirmed by X-ray diffraction (XRD) and dissolution testing by the disappearance of crystalline peaks and rapid fiber dissolution, respectively. Finally, antioxidant testing demonstrated the higher antioxidant activity of polymer-free CD-IC nanofibers.
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    ItemOpen Access
    Site-specific fluorescence polarization for studying the disaggregation of α-synuclein fibrils by small molecules
    (American Chemical Society, 2017) Haney, C. M.; Cleveland, C. L.; Wissner, R. F.; Owei, L.; Robustelli, J.; Daniels, M. J.; Canyurt, M.; Rodriguez, P.; Ischiropoulos, H.; Baumgart, T.; Petersson, E. J.
    Fibrillar aggregates of the protein α-synuclein (αS) are one of the hallmarks of Parkinson’s disease. Here, we show that measuring the fluorescence polarization (FP) of labels at several sites on αS allows one to monitor changes in the local dynamics of the protein after binding to micelles or vesicles, and during fibril formation. Most significantly, these site-specific FP measurements provide insight into structural remodeling of αS fibrils by small molecules and have the potential for use in moderate-throughput screens to identify small molecules that could be used to treat Parkinson’s disease. © 2016 American Chemical Society.