Ion-specific effects on prion nucleation and strain formation.

Ordered, fibrous, self-seeding aggregates of misfolded proteins known as amyloids are associated with important diseases in mammals and control phenotypic traits in fungi. A given protein may adopt multiple amyloid conformations, known as variants or strains, each of which leads to a distinct disease pattern or phenotype. Here, we study the effect of Hofmeister ions on amyloid nucleation and strain generation by the prion domain-containing fragment (Sup35NM) of a yeast protein Sup35p.

Continuous polycrystalline zeolitic imidazolate framework-90 membranes on polymeric hollow fibers.

Headed for a membrane: Continuous, polycrystalline ZIF-90 membranes (picture, left) can be grown at 65 °C from methanolic precursor solutions on nanocrystal-seeded surfaces of poly(amide-imide) macroporous hollow fibers (right). The ZIF-90 membranes exhibit good separation properties for linear over cyclic hydrocarbons, as well as gas permeation selectivities higher than Knudsen values.