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
- May 2022: New paper The co-chaperonin prefoldin binds IAPP monomers and fibril surfaces, Nat Commun
- Dec 2021: Award for the best PhD thesis of the Faculty of Mathematics and Natural Sciences to Emil Dandanell Agerschou - Congratulations, Emil!
- November 2021: Tina Jacob has joined the group as PhD student
- October 2021: Katharina Filodda has joined the group as PhD student
- July 2021: New paper Aβ oligomers preferentially form under endo-lysosomal conditions, Nat Commun; New insights into the formation of toxic protein clumps
- July 2021: New paper Beta-wrapin against α-synuclein inhibits fibril-induced aggregation in neurons, Front Neurosci
- Dec 2020: New paper High sequence identity required for amyloid fibril (cross-)elongation, Biophys Chem
- 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 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?