Bridging the gap: From protein misfolding to protein misfolding diseases

Abstract 

Protein misfolding and aggregation are pathognomic for a number of the most common age-related degenerative diseases. Great progress has been made in studying protein aggregation in the test tube and also in replicating protein aggregation in vertebrate animal models of these diseases. However, we argue here that the development and effective integration of emerging techniques such as the methods of nanoscience and the use of invertebrate models are now providing powerful new opportunities to advance our current understanding of the fundamental origins of these disorders.

Abbreviations: SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, AD, Alzheimer’s Disease, Aβ, Amyloid Beta, APP, Amyloid Precursor Protein, AFM, Atomic Force Microscopy, TCCD, Two Colour Coincidence Detection, QCM, Quartz Crystal Microbalance, SEC, Size Exclusion Chromatography, FRAP, Fluorescence Recovery After Photobleaching, sHsp, small Heat shock protein

Keywords: Amyloid, Neurodegeneration, Nanoscience, D. melanogaster, C. elegans