All Amytracker molecules are designed to interact with the same binding site on the amyloid oligomer. Competition assays have shown that Amytracker competes for the congo red binding site but show much higher affinity. In essence the binding cavity and binding mode of Amytracker is is dictated by a groove lined with repetitive positive charged side-chains. The detection of prefibrillar species appears dependent on 8 repetitive β sheets, composed of a minimum of eight in-register parallel-β-strands.
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- Bäck, M. et al. (2016) Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant Aβ Amyloid Fibrils and Alzheimer's Disease Brain-Derived Aβ. Chemistry - A European Journal; 22, 18335-18338
- Herrmann, U.S. et al. (2015) Structure-based drug design identifies polythiophenes as antiprion compounds. Sci. Transl. Med., 7(299), 299ra123
- Schütz, A. K. et al. (2011) The Amyloid–Congo Red Interface at Atomic Resolution. Angew Chem Int Ed, 50(26), 5956-5960