Disordered proteins are challenging targets for drug design because they lack well-defined binding pockets. Small molecules can bind them, but when the bound state remains conformationally heterogeneous, these interactions are not readily characterized in terms of conventional binding pockets. Here, we use the concep...
Adelie Louet, Gerhard Hummer, M. Vendruscolo· Journal of the American Chem...· 0 citations
The aggregation of amyloid-β (Aβ) peptides into insoluble deposits is a characteristic hallmark of Alzheimer’s disease (AD) and related neurodegenerative disorders. While AD is the most common cause of dementia, there are currently no disease-modifying treatments which are both affordable and adverse-free. In this stud...
Alexander Röntgen, Jan Lukas Heise, M. Vendruscolo et al.· bioRxiv· 0 citations
Alzheimer's disease affects tens of millions of people worldwide and is associated with the self‐assembly of the Aβ42 peptide into amyloid aggregates. Among the species formed during this process, soluble oligomeric intermediates are the most closely linked to neurotoxicity and are therefore an attractive target for bo...
Magdalena Nowinska, Elijah Suh, C. Mogilevsky et al.· Protein Science· 0 citations
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