Amyloid Fibril Structures
Amyloids are highly ordered protein aggregates implicated in various neurodegenerative diseases, including Alzheimer’s (AD) and Parkinson’s (AD) diseases, as well as metabolic disorders like Type 2 Diabetes.
The Schröder group studies the molecular basis of amyloid-related diseases, including Alzheimer's, Parkinsons's, and diabetes. Using cryo-electron microscopy (cryo-EM), we determine the structures of amyloid proteins to gain insights into their aggregation and pathological roles. Furthermore, the group develops computational methods for modeling and refinement of protein structures from low-resolution data and explores applications in protein and peptide design.
Amyloid fibril structures, Cryo-EM, protein design and structure prediction, computational method development
Benedikt Frieg*, Mookyoung Han*, Karin Giller, Christian Dienemann, Dietmar Riedel, Stefan Becker, Loren B. Andreas, Christian Griesinger, and Gunnar F. Schröder Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
Nat Commun 15(1):1297 (2024)
Benedikt Frieg, Leif Antonschmidt, Christian Dienemann, James A. Geraets, Eszter E. Najbauer, Dirk Matthes, Bert L. de Groot, Loren B. Andreas, Stefan Becker, Christian Griesinger, and Gunnar F. Schröder. The 3D structure of lipidic fibrils of α-synuclein.
Nat Commun 13: 6810 (2022)
C. Röder, T. Kupreichyk, L. Gremer, L.U. Schäfer, K.R. Pothula, R.B.G. Ravelli, D. Willbold, W. Hoyer and G.F. Schröder. Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with Aβ fibrils
Nat Struct Mol Biol (2020) 27:660–667
C. Röder, N. Vettore, L. N. Mangels, L. Gremer, R.B.G. Ravelli, D. Willbold, W. Hoyer, A.K. Buell, G.F. Schröder Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
Nat. Commun. 10, Article number: 3754 (2019)
L. Gremer, D. Schölzel, C. Schenk, E. Reinartz, Jörg Labahn, R.B.G. Ravelli, M. Tusche, C. Lopez- Iglesias, W. Hoyer, H. Heise, D. Willbold, G.F. Schröder. Fibril structure of amyloid-ß(1-42) by cryo-electron microscopy
Science 358:116–119 (2017)