title: Optimisation of BACE1 inhibition of tripartite structures by modification of membrane anchors, spacers and pharmacophores - development of potential agents for the treatment of Alzheimer's disease.
abstract: Systematic variation of membrane anchor, spacer and pharmacophore building blocks leads to an optimisation of the inhibitory effect of tripartite structures towards BACE1-induced cleavage of the amyloid precursor protein (APP).
authors.affiliation: Department Chemie, Technische Universität Dresden, Germany.
authors.forename: Philipp
authors.initials: P
authors.lastname: Linning
authors.forename: Ute
authors.initials: U
authors.lastname: Haussmann
authors.forename: Isaak
authors.initials: I
authors.lastname: Beyer
authors.forename: Sebastian
authors.initials: S
authors.lastname: Weidlich
authors.forename: Heinke
authors.initials: H
authors.lastname: Schieb
authors.forename: Jens
authors.initials: J
authors.lastname: Wiltfang
authors.forename: Hans-Wolfgang
authors.initials: HW
authors.lastname: Klafki
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Knölker
mesh_terms: D000544:Alzheimer Disease / Q000188:drug therapy*; D053829:Amyloid Precursor Protein Secretases / Q000037:antagonists & inhibitors*; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors*; D004305:Dose-Response Relationship, Drug; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000627:therapeutic use; D006801:Humans; D020128:Inhibitory Concentration 50; D015394:Molecular Structure
chemical_list: D004791:Enzyme Inhibitors; D053829:Amyloid Precursor Protein Secretases; D016282:Aspartic Acid Endopeptidases; C509280:BACE1 protein, human