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dc.contributor.authorCai, Sumin
dc.contributor.authorHe, Feng
dc.contributor.authorSamra, Hardeep S.
dc.contributor.authordel la Maza, Luis M.
dc.contributor.authorBottazzi, Maria E.
dc.contributor.authorJoshi, Sangeeta B.
dc.contributor.authorMiddaugh, C. Russell
dc.date.accessioned2017-05-08T17:53:07Z
dc.date.available2017-05-08T17:53:07Z
dc.date.issued2009
dc.identifier.citationCai, 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.en_US
dc.identifier.urihttp://hdl.handle.net/1808/24014
dc.description.abstractNative 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.en_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsThis 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.en_US
dc.subjectChlamydiaen_US
dc.subjectMOMPen_US
dc.subjectBiophysical Characterizationen_US
dc.subjectStabilizationen_US
dc.titleBiophysical and Stabilization Studies of the Chlamydia trachomatis Mouse Pneumonitis Major Outer Membrane Proteinen_US
dc.typeArticleen_US
kusw.kuauthorCai, Sumin
kusw.kuauthorHe, Feng
kusw.kuauthorSamra, Hardeep S.
kusw.kuauthorJoshi, Sangeeta B.
kusw.kuauthorMiddaugh, C. Russell
kusw.kudepartmentPharmaceutical Chemistryen_US
dc.identifier.doi10.1021/mp900110qen_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC2757499en_US
dc.rights.accessrightsopenAccess


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