Saltar al contenido
MilliporeSigma

Direct observation of nucleation and growth in amyloid self-assembly.

Journal of the American Chemical Society (2010-04-20)
Yan Liang, David G Lynn, Keith M Berland
RESUMEN

Access to native protein structure depends on precise polypeptide folding and assembly pathways. Identifying folding missteps that may lead to the nearly 40 protein misfolding diseases could feature prominently in the development of intervention strategies. Accordingly, we have investigated the earliest steps of assembly by the folding nucleus of the Alzheimer's disease Abeta peptide with real-time imaging and fluorescence correlation spectroscopy. These analyses reveal the immediate formation of large micrometer size clusters maintaining properties of intermolecular molten globules. These dynamic unstructured aggregates serve as the nucleating sites for amyloid growth and, as with native protein folding, appear important for backbone desolvation. The resulting amyloid nucleus however is able to template monomer addition from solution at rates from 2K peptides/s at millimolar peptide concentrations. This direct observation of amyloid assembly unifies several divergent models that currently exist for protein misfolding.

MATERIALES
Referencia del producto
Marca
Descripción del producto

Sigma-Aldrich
Rhodamine 110 chloride, suitable for fluorescence, BioReagent, ≥99.0% (UV)
Número de referencia del producto (SKU)
Tamaño de envase
Disponibilidad
Precio
Cantidad
Sigma-Aldrich
Rhodamine 110 chloride, Dye content ≥75 %
Número de referencia del producto (SKU)
Tamaño de envase
Disponibilidad
Precio
Cantidad