This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Antibodies with engineered changes in receptor binding sites find therapeutic application as treatments of cancer and autoimmune diseases. Often, these small structural changes lead to dramatic differences in solution viscosity, especially at the high concentrations required for therapeutic use. The viscosity of antibodies can vary from 2 centi Poise (cP) to 90 cP, with a substantial impact on biotechnology manufacturing processes and drug administration. Reversible self-association of the antibodies has been observed by ultracentrifugation and light scattering studies in dilute solutions, but shed no direct insight into their behavior at high concentrations. A study antibody solution viscosity as a function of primary structure changes and solution ions (chaotropic and kosmotropic) is proposed. The use of SAXS to measure antibody aggregate sizes, shapes, and association at high concentration is expected to give new understanding of the mechanisms and forces that effect protein behavior high concentrations.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-28
Application #
7598325
Study Section
Special Emphasis Panel (ZRG1-BPC-E (40))
Project Start
2007-03-01
Project End
2008-02-29
Budget Start
2007-03-01
Budget End
2008-02-29
Support Year
28
Fiscal Year
2007
Total Cost
$993
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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