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  1. Article ; Online: TEMPO-conjugated tobacco mosaic virus as a magnetic resonance imaging contrast agent for detection of superoxide production in the inflamed liver.

    Lumata, Jenica L / Hagge, Laurel M / Gaspar, Miguel A / Trashi, Ikeda / Ehrman, Ryanne N / Koirala, Shailendra / Chiev, Alyssa C / Wijesundara, Yalini H / Darwin, Cary B / Pena, Salvador / Wen, Xiaodong / Wansapura, Janaka / Nielsen, Steven O / Kovacs, Zoltan / Lumata, Lloyd L / Gassensmith, Jeremiah J

    Journal of materials chemistry. B

    2024  Volume 12, Issue 13, Page(s) 3273–3281

    Abstract: Superoxide, an anionic dioxygen molecule, plays a crucial role in redox regulation within the body but is implicated in various pathological conditions when produced excessively. Efforts to develop superoxide detection strategies have led to the ... ...

    Abstract Superoxide, an anionic dioxygen molecule, plays a crucial role in redox regulation within the body but is implicated in various pathological conditions when produced excessively. Efforts to develop superoxide detection strategies have led to the exploration of organic-based contrast agents for magnetic resonance imaging (MRI). This study compares the effectiveness of two such agents, nTMV-TEMPO and kTMV-TEMPO, for detecting superoxide in a mouse liver model with lipopolysaccharide (LPS)-induced inflammation. The study demonstrates that kTMV-TEMPO, with a strategically positioned lysine residue for TEMPO attachment, outperforms nTMV-TEMPO as an MRI contrast agent. The enhanced sensitivity of kTMV-TEMPO is attributed to its more exposed TEMPO attachment site, facilitating stronger interactions with water protons and superoxide radicals. EPR kinetics experiments confirm kTMV-TEMPO's faster oxidation and reduction rates, making it a promising sensor for superoxide in inflamed liver tissue.
    MeSH term(s) Mice ; Animals ; Superoxides ; Contrast Media/chemistry ; Tobacco Mosaic Virus ; Lipopolysaccharides ; Magnetic Resonance Imaging/methods ; Liver
    Chemical Substances Superoxides (11062-77-4) ; Contrast Media ; Lipopolysaccharides
    Language English
    Publishing date 2024-03-27
    Publishing country England
    Document type Journal Article
    ZDB-ID 2702241-9
    ISSN 2050-7518 ; 2050-750X
    ISSN (online) 2050-7518
    ISSN 2050-750X
    DOI 10.1039/d3tb02765a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Self-assembly of a fluorescent virus-like particle for imaging in tissues with high autofluorescence.

    Trashi, Ikeda / Durbacz, Mateusz Z / Trashi, Orikeda / Wijesundara, Yalini H / Ehrman, Ryanne N / Chiev, Alyssa C / Darwin, Cary B / Herbert, Fabian C / Gadhvi, Jashkaran / De Nisco, Nicole J / Nielsen, Steven O / Gassensmith, Jeremiah J

    Journal of materials chemistry. B

    2023  Volume 11, Issue 20, Page(s) 4445–4452

    Abstract: Virus-like particles (VLPs) are engineered nanoparticles that mimic the properties of viruses-like high tolerance to heat and proteases-but lack a viral genome, making them non-infectious. They are easily modified chemically and genetically, making them ... ...

    Abstract Virus-like particles (VLPs) are engineered nanoparticles that mimic the properties of viruses-like high tolerance to heat and proteases-but lack a viral genome, making them non-infectious. They are easily modified chemically and genetically, making them useful in drug delivery, enhancing vaccine efficacy, gene delivery, and cancer immunotherapy. One such VLP is Qβ, which has an affinity towards an RNA hairpin structure found in its viral RNA that drives the self-assembly of the capsid. It is possible to usurp the native way infectious Qβ self-assembles to encapsidate its RNA to place enzymes inside the VLP's lumen as a protease-resistant cage. Further, using RNA templates that mimic the natural self-assembly of the native capsid, fluorescent proteins (FPs) have been placed inside VLPs in a "one pot" expression system. Autofluorescence in tissues can lead to misinterpretation of results and unreliable science, so we created a single-pot expression system that uses the fluorescent protein smURFP, which avoids autofluorescence and has spectral properties compatible with standard commercial filter sets on confocal microscopes. In this work, we were able to simplify the existing "one-pot" expression system while creating high-yielding fluorescent VLP nanoparticles that could easily be imaged inside lung epithelial tissue.
    MeSH term(s) Capsid Proteins/metabolism ; Capsid/metabolism ; RNA, Viral
    Chemical Substances Capsid Proteins ; RNA, Viral
    Language English
    Publishing date 2023-05-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2702241-9
    ISSN 2050-7518 ; 2050-750X
    ISSN (online) 2050-7518
    ISSN 2050-750X
    DOI 10.1039/d3tb00469d
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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