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    Chemical and Physical Characterization of Therapeutic Proteins in Solution and Amorphous Solids

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    Issue Date
    2008-06-16
    Author
    Sinha, Sandipan
    Publisher
    University of Kansas
    Format
    190 pages
    Type
    Dissertation
    Degree Level
    PH.D.
    Discipline
    Pharmaceutical Chemistry
    Rights
    This item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
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    Abstract
    The chemical and physical stability of proteins in solution and solids was addressed in this dissertation. Protein-excipient interactions in lyophilized solids were studied by hydrogen/deuterium exchange with mass spectrometry (chapter 3) while glycosylation quanitification (chapter 4) and deamidation (chapter 5) was characterized in antibodies in solution. LC/ESI-MS was the method of choice for all studies. Hydrogen/deuterium exchange study showed that the method can be used to obtain region specific information about protein-excipient interactions in solids. It was demonstrated that exchange protection did not occur uniformly along the backbone of the protein and was dependant on excipient type and protein structure. The glycosylation quanitification study demonstrated that the Fc/2 (limited proteolysis followed by reduction) method was relatively quick and accurate and showed comparable values to the standard sugar release assay. Antibody deamidation study demonstrated that secondary structure played a pivotal role in determination of the deamidation products in antibodies.
    URI
    http://hdl.handle.net/1808/4242
    Collections
    • Dissertations [4475]
    • Pharmaceutical Chemistry Dissertations and Theses [141]

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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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