Y10W β(1–40) fluorescence reflects epitope exposure in conformers of Alzheimer’s β-peptide

摘要: Abstract The Alzheimer’s β-peptide in neutral aqueous solution is characterized variously as a random coil or heterogeneous mixture of conformers. Under conditions lowered pH characteristic intracellular compartments such endosomes lysosomes, different conformation favored, which reflected the biophysical and biological properties peptide. reactivity epitope monoclonal antibody 6F/3D, encompassing residues 9–14, drastically reduced. fluorescence human sequence β(1–40) with tyrosine at position 10 substituted tryptophan (Y10W β(1–40)) quenched nearly 50% when peptide shifted to 4.6. exposure 6F/3D parallels Y10W changes induced by variety perturbations. linkage sensitivity immunological detection potential for monitoring rapid offers convergence biology biophysics study β-amyloid conformation.