• Login
    View Item 
    •   Shocker Open Access Repository Home
    • Fairmount College of Liberal Arts and Sciences
    • Chemistry and Biochemistry
    • CHEM Faculty Scholarship
    • CHEM Faculty Publications
    • View Item
    •   Shocker Open Access Repository Home
    • Fairmount College of Liberal Arts and Sciences
    • Chemistry and Biochemistry
    • CHEM Faculty Scholarship
    • CHEM Faculty Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Comparison of the structural stability and dynamic properties of recombinant anthrax protective antigen and its 2-fluorohistidine-labeled analogue

    Date
    2012-11
    Author
    Hu, Lei
    Joshi, Sangeeta B.
    Andra, Kiran K.
    Thakkar, Santosh V.
    Volkin, David B.
    Bann, James G.
    Middaugh, C.R.
    Metadata
    Show full item record
    Citation
    Hu, Lei; Joshi, Sangeeta B.; Andra, Kiran K.; Thakkar, Santosh V.; Volkin, David B.; Bann, James G.; Middaugh, C.R. 2012. Comparison of the structural stability and dynamic properties of recombinant anthrax protective antigen and its 2-fluorohistidine-labeled analogue. Journal of Pharmaceutical Sciences, v.101 no.11 pp.4118-4128
    Abstract
    Protective antigen (PA) is the primary protein antigenic component of both the currently used anthrax vaccine and related recombinant vaccines under development. An analogue of recombinant PA (2-FHis rPA) has been recently shown to block the key steps of pore formation in the process of inducing cytotoxicity in cells, and thus can potentially be used as an antitoxin or a vaccine. This rPA analogue was produced by fermentation to incorporate the unnatural amino acid 2-fluorohistidine (2-FHis). In this study, the effects of 2-FHis labeling on rPA antigen's conformational stability and dynamic properties were investigated by various biophysical techniques. Temperature/pH stability profiles of rPA and 2-FHis rPA were analyzed by the empirical phase diagram (EPD) approach, and physical stability differences between them were identified. Results showed that rPA and 2-FHis rPA had similar stability at pH 78. With decreasing solution pH, however, 2-FHis rPA was found to be more stable. Dynamic sensitive measurements of the two proteins at pH 5 found that 2-FHis rPA was more dynamic and/or differentially hydrated under acidic pH conditions. The biophysical characterization and stability data provide information useful for the potential development of 2-FHis rPA as a more stable rPA vaccine candidate.
    Description
    Click on the DOI link to access the article (may not be free).
    URI
    http://dx.doi.org/10.1002/jps.23294
    http://hdl.handle.net/10057/5900
    Collections
    • CHEM Faculty Publications

    Browse

    All of Shocker Open Access RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsBy TypeThis CollectionBy Issue DateAuthorsTitlesSubjectsBy Type

    My Account

    LoginRegister

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    DSpace software copyright © 2002-2022  DuraSpace
    DSpace Express is a service operated by 
    Atmire NV