Lj. Garrard et Dj. Henner, SELECTION OF AN ANTI-IGF-1 FAB FROM A FAB PHAGE LIBRARY CREATED BY MUTAGENESIS OF MULTIPLE CDR LOOPS, Gene, 128(1), 1993, pp. 103-109
Diverse Fab libraries containing 2-3 x 10(8) members were generated by
randomizing amino acid residues within four of the six complementarit
y determining regions of a humanized version of an anti-HER-2 Ab (hu4D
5). These libraries were subsequently displayed on the surface of the
filamentous bacteriophage M13 and selected for binding to three protei
ns: CD4, insulin-like growth factor 1 (IGF-1), and tissue plasminogen
activator. An Fab-bacteriophage was isolated that showed specific bind
ing to IGF-1. The affinity of this Fab was determined to be 3.5 muM.