The aggregation of proteins into amyloid fibril deposits is a pathological feature of various diseases, including nearly every major neurodegenerative disease such as Alzheimer and Parkinson. We are interested in the mechanism of amyloid formation, and investigate how it can be modulated.
ERC Consolidator project
Control of amyloid formation via β-hairpin molecular recognition features
- Dec 2020: New paper High sequence identity required for amyloid fibril (cross-)elongation, Biophys Chem
- Nov 2020: Celina Schulz has joined the group as PhD student
- October 2020: New paper Metastable oligomers bind to amyloid fibril surfaces and inhibit secondary nucleation of fibrils, Angew Chem
- October 2020: New paper Inhibitor and substrate cooperate to inhibit amyloid fibril elongation, Chem Sci
- July 2020: New paper Clustering of prion protein and α-synuclein oligomers, Commun Biol
- June 2020: New preprint: Aβ oligomers preferentially form under endo-lysosomal conditions, bioRxiv
- June 2020: New paper Fibril structure of islet amyloid polypeptide, Nat Struct Mol Biol; New indication of a link between Alzheimer’s and diabetes; Alzforum: Does common structure explain cross-seeding of fibrils?
- Aug 2019: New paper Beta-wrapin inhibits proliferation of α-synuclein fibrils, eLife; Research into Parkinson’s disease: binding-protein prevents fibril proliferation