High-throughput analysis of antibody colloidal stability using nanoparticle-antibody conjugates

Authors
Sule, Shantanu
ORCID
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Other Contributors
Tessier, Peter M.
Garde, Shekhar
Siegel, R. W. (Richard W.)
Underhill, Patrick T.
Dordick, Jonathan S.
Issue Date
2013-08
Keywords
Chemical and biological engineering
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
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Abstract
In Chapter 2, we have evaluated the ionic-strength dependent self-association of three mAbs using self-interaction chromatography for a range of pH values commonly used in antibody formulation (pH 4-6). We find that antibody self-association is minimized at low ionic strength for low pH conditions while high ionic strength minimizes self-association at near-neutral pH. Importantly, this behavior is similar across all three evaluated mAbs and is only weakly influenced by the specific antibody structure. Interestingly, such a pattern of self-interaction is not unique to mAbs (large, multi-domain proteins) but is also observed for some smaller, single-domain globular proteins (e.g., alpha-chymotrypsinogen and ribonuclease A). We have further extended these studies in Chapter 3 using depletant-induced precipitation to infer antibody solubility as a function of pH and ionic strength.
Description
August 2013
School of Engineering
Department
Dept. of Chemical and Biological Engineering
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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