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    Biophysical and Stabilization Studies of the Chlamydia trachomatis Mouse Pneumonitis Major Outer Membrane Protein

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    Issue Date
    2009
    Author
    Cai, Sumin
    He, Feng
    Samra, Hardeep S.
    del la Maza, Luis M.
    Bottazzi, Maria E.
    Joshi, Sangeeta B.
    Middaugh, C. Russell
    Publisher
    American Chemical Society
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
    Rights
    This document is the Accepted Manuscript version of a Published Work that appeared in final form in Molecular Pharmaceutics, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/mp900110q.
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    Abstract
    Native Chlamydia trachomatis mouse pneumonitis major outer membrane protein (nMOMP) induces effective protection against genital infection in a mouse challenge model. The conformation of nMOMP is crucial to confer this protective immunity. To achieve a better understanding of the conformational behavior and stability of nMOMP, a number of spectroscopic techniques are employed to characterize the secondary structure (circular dichroism), tertiary structure (intrinsic fluorescence) and aggregation properties (static light scattering and optical density) as a function of pH (3-8) and temperature (10-87.5°C). The data are summarized in an empirical phase diagram (EPD) which demonstrates that the thermal stability of nMOMP is strongly pH-dependent. Three distinctive regions are seen in the EPD. Below the major thermal transition regions, nMOMP remains in its native conformation over the pH range of 3-8. Above the thermal transitions, nMOMP appears in two different structurally altered states; one at pH 3-5 and the other at pH 6-8. The EPD shows that the highest thermal transition point (~ 65°C) of nMOMP is near pH 6. Several potential excipients such as arginine, sodium citrate, Brij 35, sucrose and guanidine are also selected to evaluate their effects on the stability of nMOMP. These particular compounds increase the aggregation onset temperature of nMOMP by more than 10°C, without affecting its secondary and tertiary structure. These results should help formulate a vaccine using a recombinant MOMP.
    URI
    http://hdl.handle.net/1808/24014
    DOI
    https://doi.org/10.1021/mp900110q
    Collections
    • Pharmaceutical Chemistry Scholarly Works [327]
    Citation
    Cai, S., He, F., Samra, H. S., de la Maza, L. M., Bottazzi, M. E., Joshi, S. B., & Middaugh, C. R. (2009). Biophysical and Stabilization Studies of the Chlamydia trachomatis Mouse Pneumonitis Major Outer Membrane Protein. Molecular Pharmaceutics, 6(5), 1553–1561. http://doi.org/10.1021/mp900110q.

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    KU Libraries
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    KU Libraries
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    Lawrence, KS 66045
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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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