The causes of pathological conditions\ud such as Alzheimer’s and Parkinson’s\ud diseases are becoming better\ud understood. Proteins that misfold from\ud their native structure to form aggregates\ud of β-sheet fibrils — termed amyloid — are\ud known1,2 to be implicated in these ‘amyloid\ud diseases’. Understanding the early steps\ud of fibril formation is critical, and the\ud conditions, mechanism and kinetics of\ud protein and peptide aggregation are being\ud widely investigated through a variety of\ud in vitro studies.\ud Kinetic aspects of the dispersion of the\ud protein or peptide in solution are thought\ud to influence the fibrillization process by\ud mass-transfer effects. In addition, mixing also\ud leads to shear forces, which can influence\ud fibril growth by perturbing the equilibrium\ud between the isolated and aggregated proteins,\ud causing existing fibrils to fragment and create\ud new nuclei3. Writing in the Journal of the\ud American Chemical Society, David Talaga\ud and co-workers have now highlighted4 an\ud additional factor that can influence the\ud fibrillization of amyloid-forming proteins —\ud the presence of hydrophobic interfaces
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