Monitoring the prevention of amyloid fibril formation by α‐crystallin

@article{Rekas2007MonitoringTP,
  title={Monitoring the prevention of amyloid fibril formation by $\alpha$‐crystallin},
  author={Agata Rekas and Lucy Jankova and David C Thorn and Roberto Cappai and John A. Carver},
  journal={The FEBS Journal},
  year={2007},
  volume={274}
}
The molecular chaperone, α‐crystallin, has the ability to prevent the fibrillar aggregation of proteins implicated in human diseases, for example, amyloid β peptide and α‐synuclein. In this study, we examine, in detail, two aspects of α‐crystallin's fibril‐suppressing ability: (a) its temperature dependence, and (b) the nature of the aggregating species with which it interacts. First, the efficiency of α‐crystallin to suppress fibril formation in κ‐casein and α‐synuclein increases with… 
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