Jiapeng Wei

This study designs de novo proteins that selectively inhibit alpha-synuclein aggregation by targeting specific intermediates, with one binder preferentially inhibiting oligomer formation and secondary nucleation.

This paper demonstrates that reversible peptide self-assembly can be used to achieve tuneable pharmacokinetics for therapeutic peptides, as shown with pramlintide in a rat model.

This study identifies secondary nucleation of α-Synuclein as the key mechanism driving mitochondrial dysfunction and Lewy body formation in Parkinson's Disease.

This study uses single molecule microscopy to show that tau condensate ageing involves liquid-solid coexistence at the fibril level, with spatial heterogeneity driving the transition.

This paper shows that Alzheimer's amyloid-beta peptide forms biomolecular condensates on lipid bilayers, accelerating amyloid aggregation and revealing a new early step in the disease mechanism.

The paper investigates the formation of amyloid loops in brain tissues and finds that protofibril flexibility, not hydrogen bonding, enables loop formation and disease-related toxicity.