Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide
Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1–40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation.
We investigate the quantum anomalous Hall effect in a mixture of ultra-cold neutral bosons and fermions held on a hexagonal optical lattice. In the strong atom-atom interaction limit, composite fermions composed of one fermion with bosons or bosonic holes in the mixture are formed. Such composite fermions have already been generated successfully in experiment [Nat. Phys. {\bf 7}, 642 (2011)]. Here we predict that this kind of composite fermions may provide a realization of the quantum anomalous Hall effect by tuning the atom-atom interaction or the filling of the bosons in the mixture. We also discuss the corresponding experimental signatures of the quantum anomalous Hall effect in the Bose-Fermi mixture on hexagonal optical lattice.