title: Camptothecin binds to a synthetic peptide identified by a T7 phage display screen.
abstract: An analysis of non-biotinylated camptothecin (CPT) binding to the C-20-biotinylated CPT binding peptide NSSQSARR was carried out using two methods, quartz-crystal microbalance (QCM) and surface plasmon resonance (SPR). The peptide was immobilized peptide on a sensor chip and showed a dissociation constant (KD) of approximately 0.1 microM against CPT in QCM and SPR experiments.
authors.affiliation: Genome and Drug Discovery Research Center, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
authors.forename: Yoichi
authors.initials: Y
authors.lastname: Takakusagi
authors.forename: Susumu
authors.initials: S
authors.lastname: Kobayashi
authors.forename: Fumio
authors.initials: F
authors.lastname: Sugawara
mesh_terms: D000595:Amino Acid Sequence; D000970:Antineoplastic Agents; D017123:Bacteriophage T7; D001665:Binding Sites; D002166:Camptothecin / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship; D020349:Surface Plasmon Resonance
chemical_list: D000970:Antineoplastic Agents; D019151:Peptide Library; D010455:Peptides; D002166:Camptothecin