QIAD assay for quantitating a compound’s efficacy in elimination of toxic Aβ oligomers

• DOI: 10.1038/srep13222
• Publication Date: 2015-09-23T09:05:00Z
• Authors: Oleksandr Brener; Tina Dunkelmann; Lothar Gremer; Thomas van Groen; Ewa A. Mirecka; Inga Kadish; Antje Willuweit; Janine Kutzsche; Dagmar Jürgens; Stephan Rudolph; Markus Tusche; Patrick Bongen; Jörg Pietruszka; Filipp Oesterhelt; Karl-Josef Langen; Hans-Ulrich Demuth; Arnold Janssen; Wolfgang Hoyer; Susanne A. Funke; Luitgard Nagel-St...; Dieter Willbold
• Keywords: 0301 basic medicine; info:eu-repo/classification/ddc/000; Amyloid beta-Peptides; 000; Taurine; Mice, Transgenic; Protein Aggregation, Pathological; Article; Catechin; 3. Good health; Ferredoxin-NADP Reductase; Mice, Inbred C57BL; Disease Models, Animal; Mice; 03 medical and health sciences; Alzheimer Disease; Mice, Inbred DBA; Animals; Humans; Carrier Proteins; Oligopeptides; Inositol

AbstractStrong evidence exists for a central role of amyloid β-protein (Aβ) oligomers in the pathogenesis of Alzheimer’s disease. We have developed a fast, reliable and robust in vitro assay, termed QIAD, to quantify the effect of any compound on the Aβ aggregate size distribution. Applying QIAD, we studied the effect of homotaurine, scyllo-inositol, EGCG, the benzofuran derivative KMS88009, ZAβ3W, the D-enantiomeric peptide D3 and its tandem version D3D3 on Aβ aggregation. The predictive power of the assay for in vivo efficacy is demonstrated by comparing the oligomer elimination efficiency of D3 and D3D3 with their treatment effects in animal models of Alzheimer´s disease.