title: Structure-activity relationship study on polyglutamine binding peptide QBP1.
abstract: Aggregation and deposition of expanded polyglutamine proteins in the brain cause neurodegenerative diseases including Huntington disease. This pathogenic process is suppressed and delayed in the presence of polyglutamine binding peptide 1 (QBP1), which we previously identified as an undecapeptide binding to pathogenic polyglutamine proteins from phage display peptide libraries. In this paper, a structure-activity relationship study on QBP1 was conducted to determine the pharmacophores for inhibition of polyglutamine aggregation. Furthermore, a truncation study identified an octapeptide as the minimum structure for suppressing aggregation of polyglutamine proteins, which is equipotent to the parent undecapeptide QBP1.
authors.affiliation: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Tomita
authors.forename: H Akiko
authors.initials: HA
authors.lastname: Popiel
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Nagai
authors.forename: Tatsushi
authors.initials: T
authors.lastname: Toda
authors.forename: Yuji
authors.initials: Y
authors.lastname: Yoshimitsu
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Ohno
authors.forename: Shinya
authors.initials: S
authors.lastname: Oishi
authors.forename: Nobutaka
authors.initials: N
authors.lastname: Fujii
mesh_terms: D000595:Amino Acid Sequence; D020128:Inhibitory Concentration 50; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology; D019151:Peptide Library; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D019151:Peptide Library; C407346:polyglutamine-binding protein 1