Alzheimer’s disease is the most common cause of dementia in Western societies. While the reasons for the disease are under debate, amyloid structures derived either from Aß peptide or τ protein and are thought to be crucial for disease onset. Our institute studies the structure of Aß peptide and the cellular effects caused by specific assembly states of this peptide.

Selected references:

Wulff M, Baumann M, Thümmler A, Yadav JK, Heinrich L, Knüpfer U, Schlenzig D, Schierhorn A, Rahfeld JU, Horn U, Balbach J, Demuth HU, Fändrich M
Enhanced fibril fragmentation of N-terminally truncated and pyroglutamyl-modified Aβ peptide.
Angewandte Chemie Int. Edt. 2016, 55, 5081-5084

Schmidt M, Rohou A, Lasker K, Yadav JK, Schiene-Fischer C, Fändrich M, Grigorieff N
Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.
Proc. Natl. Acad. Sci. U.S.A. 2015, 112, 11858-11863

Haupt C, Leppert J, Rönicke R, Meinhardt J, Yadav JK, Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M
Structural basis of β-amyloid-dependent synaptic dysfunctions.
Angewandte Chemie Int. Edt. 2012, 51, 1576-1579

Fändrich M, Schmidt M, Grigorieff N
Recent progress in understanding Alzheimer's β-amyloid structures.
Trends in Biochem. Sci. 2011, 36, 338-345

Friedrich RP, Tepper K, Rönicke R, Westermann M, Reymann K, Kaether C, Fändrich M
Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity.
Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 1942-1947