| Literature DB >> 24291820 |
Romain Rouet1, David Lowe2, Daniel Christ3.
Abstract
Human monoclonal antibodies often display limited thermodynamic and colloidal stabilities. This behavior hinders their production, and places limitations on the development of novel formulation conditions and therapeutic applications. Antibodies are highly diverse molecules, with much of the sequence variation observed within variable domain families and, in particular, their complementarity determining regions. This has complicated the development of comprehensive strategies for the stability engineering of the human antibody repertoire. Here we provide an overview of the field, and discuss recent advances in the development of robust and aggregation resistant antibody therapeutics. CrownEntities:
Keywords: Antibody therapeutics; Protein aggregation; Protein engineering; Stability
Mesh:
Substances:
Year: 2013 PMID: 24291820 DOI: 10.1016/j.febslet.2013.11.029
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124