title: Stability engineering of the human antibody repertoire.
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.
authors.affiliation: Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia. Electronic address: r.rouet@garvan.org.au.
authors.forename: Romain
authors.initials: R
authors.lastname: Rouet
authors.affiliation: MedImmune, Milstein Building, Granta Park, Cambridge CB21 6GH, United Kingdom.
authors.forename: David
authors.initials: D
authors.lastname: Lowe
authors.affiliation: Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia; The University of New South Wales, Faculty of Medicine, St Vincent's Clinical School, Darlinghurst, Sydney, NSW 2010, Australia.
authors.forename: Daniel
authors.initials: D
authors.lastname: Christ
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000235:genetics*; D006801:Humans; D015202:Protein Engineering / Q000379:methods*; D055503:Protein Multimerization; D055550:Protein Stability; D017434:Protein Structure, Tertiary
chemical_list: D000911:Antibodies, Monoclonal
keywords: Antibody therapeutics; Protein aggregation; Protein engineering; Stability