title: A novel β-loop scaffold of phage-displayed peptides for highly specific affinities.
abstract: Loop peptides stabilized by two β-strands were used as a scaffold for a phage displayed peptide library. Affinity-based screening for insulin provided peptides, which showed affinity constants of 10(5) M(-1) order for insulin over 100 times greater than their affinity for the structurally similar insulin-like growth factor 1. The results suggested that the scaffold offers a powerful tool for generating and screening peptides as ligands for drugs and biologics.
authors.affiliation: Department of Bioengineering, Tokyo Institute of Technology, 4259-B40 Nagatsuta-cho, Midori-ku, Yokohama, Japan.
authors.forename: Toshiki
authors.initials: T
authors.lastname: Sawada
authors.forename: Kojiro
authors.initials: K
authors.lastname: Ishiguro
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Takahashi
authors.forename: Hisakazu
authors.initials: H
authors.lastname: Mihara
mesh_terms: D006801:Humans; D007328:Insulin / Q000737:chemistry; D007334:Insulin-Like Growth Factor I / Q000737:chemistry; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D007328:Insulin; D019151:Peptide Library; D010455:Peptides; D007334:Insulin-Like Growth Factor I