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Aggregation, stability, and formulation of human antibody therapeutics

Abstract

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.

Type Journal
Authors Lowe, D.; Dudgeon, K.; Rouet, R.; Schofield, P.; Jermutus, L.; Christ, D.:
Garvan Authors A/Prof Daniel Christ , Dr Peter Schofield , Romain Rouet
Publisher Name ADV PROTEIN CHEM
Published Date 2011-08-19 00:00:00
Published Volume 84
Published Pages 41-61
URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21846562
Status Published In-print
OpenAccess Link https://publications.gimr.garvan.org.au/download.php?11202_11648/LoweAdvancesProofs.pdf