title: Affinity maturation and functional dissection of a humanised anti-RAGE monoclonal antibody by ribosome display.
abstract: The pursuit of more potent, safe, and cost-effective drugs has placed a greater emphasis on antibody optimisation within the drug discovery process. Technologies to rapidly improve antibody drug performance, such as phage display, ribosome display, and yeast display, are playing a key role in this effort. Among these ribosome display is a particularly powerful technology and has recently been applied to the affinity optimisation of a humanised anti-receptor for advanced glycation end products (anti-RAGE) antibody (Finlay et al., J Mol Biol 388:541-558, 2009). By using a combination of error-prone PCR with ribosome display each amino acid position within this humanised antibody was scanned for both its functional importance and its capacity to increase affinity resulting in both affinity-matured antibody variants and a functional map of the antibody paratope.
authors.affiliation: Biotherapeutics Division, National Institute for Biological Standards and Controls, South Mimms, Potters Bar, UK. Simon.hufton@nibsc.hpa.org.uk
authors.forename: Simon E
authors.initials: SE
authors.lastname: Hufton
mesh_terms: D000911:Antibodies, Monoclonal / Q000235:genetics* / Q000276:immunology*; D000915:Antibody Affinity; D019020:Directed Molecular Evolution; D017127:Glycation End Products, Advanced / Q000276:immunology*; D006801:Humans; D016133:Polymerase Chain Reaction; D012270:Ribosomes / Q000235:genetics*
chemical_list: D000911:Antibodies, Monoclonal; D017127:Glycation End Products, Advanced