Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases.

摘要: The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the origin an increasing number human diseases. misfolding often associated with assembly into extracellular fibrillar aggregates, commonly termed amyloid fibrils. Despite many efforts expended characterise formation in vitro, it increasingly evident that biological environment which aggregation occurs naturally influences mechanism rate process, as well structure stability resulting This problem not trivial because inherent complexity biology difficulty design proper experiments able address molecular level phenomenon vivo. We will show successful approaches have been used recently illustrate some results contributed elucidate important structural aspects