Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth
Alexander K. BuellNanoscience Centre, University of Cambridge, 11 JJ Thomson Avenue, West Cambridge CB3 0FF, UKAnne DhulesiaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK)Duncan A. WhiteDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK)Tuomas P. J. KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK)Christopher M. DobsonChristopher M. Dobson, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK)Mark E. WellandChristopher M. Dobson, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK)
2012en
ABI
Annotatsiya
The free energy barriers that determine the kinetics of the growth of amyloid fibrils have been measured for a series of peptides and proteins using a quartz crystal microbalance. The results indicate that the enthalpic contribution to the free energy barrier is invariably unfavorable and correlates with the size and structure of the soluble parent polypeptide, whereas the entropic contribution is favorable and linked to the hydrophobicity of the peptide sequence.
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