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Author Notes:

Email: martha.groover@chbe.gatech.edu; Email: dlynn2@emory.edu

The authors also thank the Robert P. Apkarian Integrated Electron Microscopy Core at Emory University for assistance with TEM measurements.

The authors declare no competing financial interest.

Subjects:

Research Funding:

The authors thank the McDonnell Foundation (21st Century Science Initiative Grant on Studying Complex Systems, 220020271), the NSF (Grants CHE-1507932 and NSF/DMR-BSF 1610377), and the NIH Alzheimer’s Disease Research Center (P50AG025688) for financial support.

Multistep Conformation Selection in Amyloid Assembly.

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Journal Title:

Journal of the American Chemical Society

Volume:

Volume 139, Number 47

Publisher:

, Pages 17007-17010

Type of Work:

Article | Final Publisher PDF

Abstract:

Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection.

Copyright information:

© 2017 American Chemical Society. This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.

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