A massively parallel analysis of the effects of mutations on amyloid beta nucleation provide the first comprehensive atlas of how mutations alter the formation of amyloid fibrils.

The high affinity α-synuclein-monomer binder AS69 converts into a strong sub-stoichiometric inhibitor of nucleation processes upon formation of the AS69-α-synuclein complex, achieving reduced aggregation in vitro and in vivo.

Ligands that bind dimers of light chain variable domains inhibit the formation of amyloid fibrils.

Atomic structures of hIAPP fibrillar segments, determined using the cryo electron microscopy method MicroED, reveal that strong, stable intermolecular interactions are important features of cytotoxic amyloid proteins.

CLR01 is a small molecule that could be an effective topical microbicide to eliminate HIV (and other enveloped viruses), and to antagonize host-encoded amyloid fibrils that promote HIV infection.

Size threshold and suprastructure formation are key parameters that control the infective potential of amyloid fibrils as prion particles.

Aβ inhibitors effectively block its aggregation, while also reducing seeding of tau aggregation from Aβ, tau, and AD derived fibrils, suggesting the two share a structurally related disease relevant interface.

Ex vivo characterization of the interaction of human sperm with semen factors reveals that semen amyloids, previously discovered due to their ability to enhance HIV infection, serve a physiological function by promoting disposal of the defective sperm.

The alpha-synuclein fibril structure reported here buries residues 50-57 at the interface between its two protofilaments, suggesting that familial Parkinson's disease associated mutations in these residues lead to a structure not compatible with the one presented here.

Novel designed alpha-sheet peptides inhibit amyloidosis in two different systems and preferentially bind the toxic oligomer.