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Selection of an anti-IGF-1 Fab from a Fab phage library created by mutagenesis of multiple CDR loops

1993; Elsevier BV; Volume: 128; Issue: 1 Linguagem: Inglês

10.1016/0378-1119(93)90160-5

1879-0038

Lisa J. Garrard, Dennis J. Henner,

Protein purification and stability

Diverse Fab libraries containing 2-3 x 10(8) members were generated by randomizing amino acid residues within four of the six complementarity determining regions of a humanized version of an anti-HER-2 Ab (hu4D5). These libraries were subsequently displayed on the surface of the filamentous bacteriophage M13 and selected for binding to three proteins: CD4, insulin-like growth factor 1 (IGF-1), and tissue plasminogen activator. An Fab-bacteriophage was isolated that showed specific binding to IGF-1. The affinity of this Fab was determined to be 3.5 microM.