Aggregation, stability, and formulation of human antibody therapeutics
Many human monoclonal antibodies display poor biophysical properties, such as low stability and a propensity to aggregate. These unfavorable tendencies can be even more pronounced for human antibody fragments, which often require a considerable degree of optimization. In this review, we describe methods for analyzing aggregation and stability of human antibodies and antibody fragments. We also provide an overview of recent approaches to improve these properties through engineering and formulation.
|Authors||Lowe, D.; Dudgeon, K.; Rouet, R.; Schofield, P.; Jermutus, L.; Christ, D.:|
|Publisher Name||ADV PROTEIN CHEM|
|DOI||B978-0-12-386483-3.00004-5 [pii] 10.1016/B978-0-12-386483-3.00004-5|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21846562|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/11202|