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

Diverse Fab libraries containing 2–3 × 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 bacteriop...

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Veröffentlicht in:	Gene 1993-06, Vol.128 (1), p.103-109
Hauptverfasser:	Garrard, Lisa J., Henner, Dennis J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacteriophage M13 - genetics Base Sequence Biological and medical sciences Biotechnology Cloning, Molecular Complementarity determining regions display vectors filamentous bacteriophage Fundamental and applied biological sciences. Psychology gene III Health. Pharmaceutical industry humanized antibody Humans Immunoglobulin Fab Fragments - biosynthesis Immunoglobulin Fab Fragments - genetics Immunoglobulin Heavy Chains - biosynthesis Immunoglobulin Heavy Chains - genetics Industrial applications and implications. Economical aspects Insulin-Like Growth Factor I - immunology Molecular Sequence Data Monoclonal antibodies Oligodeoxyribonucleotides Plasmids Production of active biomolecules Protein-Tyrosine Kinases - genetics Proto-Oncogene Proteins - immunology Receptor, ErbB-2 Recombinant Fusion Proteins - biosynthesis
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Zusammenfassung:	Diverse Fab libraries containing 2–3 × 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 μM.
ISSN:	0378-1119 1879-0038
DOI:	10.1016/0378-1119(93)90160-5