High-throughput analysis of antibody colloidal stability using nanoparticle-antibody conjugates
Loading...
Authors
Sule, Shantanu
Issue Date
2013-08
Type
Electronic thesis
Thesis
Thesis
Language
ENG
Keywords
Chemical and biological engineering
Alternative Title
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
School of Engineering
Full Citation
Publisher
Rensselaer Polytechnic Institute, Troy, NY