Ontology highlight
ABSTRACT:
SUBMITTER: Kroth H
PROVIDER: S-EPMC3464581 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Kroth Heiko H Ansaloni Annalisa A Varisco Yvan Y Jan Asad A Sreenivasachary Nampally N Rezaei-Ghaleh Nasrollah N Giriens Valérie V Lohmann Sophie S López-Deber María Pilar MP Adolfsson Oskar O Pihlgren Maria M Paganetti Paolo P Froestl Wolfgang W Nagel-Steger Luitgard L Willbold Dieter D Schrader Thomas T Zweckstetter Markus M Pfeifer Andrea A Lashuel Hilal A HA Muhs Andreas A
The Journal of biological chemistry 20120813 41
Increasing evidence implicates Aβ peptides self-assembly and fibril formation as crucial events in the pathogenesis of Alzheimer disease. Thus, inhibiting Aβ aggregation, among others, has emerged as a potential therapeutic intervention for this disorder. Herein, we employed 3-aminopyrazole as a key fragment in our design of non-dye compounds capable of interacting with Aβ42 via a donor-acceptor-donor hydrogen bond pattern complementary to that of the β-sheet conformation of Aβ42. The initial de ...[more]