title: Dihydrofolate reductase inhibitory peptides screened from a structured designed β-loop peptide library displayed on phage.
abstract: Enzyme inhibitory peptides with a loop structure stabilized using an antiparallel β-sheet scaffold (β-loop peptide) were obtained from a designed peptide phage library. Human dihydrofolate reductase (hDHFR) was used as the target enzyme. The obtained β-loop peptides were competitive inhibitors of hDHFR with micromolar inhibition constants and dissociation constants.
authors.affiliation: Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta-cho 4259 B-40, Midori-ku, Yokohama 226-8501, Japan. hmihara@bio.titech.ac.jp.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Tsutsumi
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Nakano
authors.forename: Hisakazu
authors.initials: H
authors.lastname: Mihara
mesh_terms: D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D006801:Humans; D008958:Models, Molecular; D019151:Peptide Library; D017433:Protein Structure, Secondary; D013762:Tetrahydrofolate Dehydrogenase / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D019151:Peptide Library; D013762:Tetrahydrofolate Dehydrogenase