Surveying the Energy Landscapes of Aβ Fibril Polymorphism

The Journal of Physical Chemistry. B
Mingchen ChenPeter G Wolynes

Abstract

Many unrelated proteins and peptides have been found spontaneously to form amyloid fibers above a critical concentration. Even for a single sequence, however, the amyloid fold is not a single well-defined structure. Although the cross-β hydrogen bonding pattern is common to all amyloids, all other aspects of amyloid fiber structures are sensitive to both the sequence of the aggregating peptides and the solvent conditions under which the aggregation occurs. Amyloid fibers are easy to identify and grossly characterize using microscopy, but their insolubility and aperiodicity along the dimensions transverse to the fiber axis have complicated detailed experimental structural characterization. In this paper, we explore the landscape of possibilities for amyloid protofilament structures that are made up of a single stack of peptides associated in a parallel in-register manner. We view this landscape as a two-dimensional version of the usual three-dimensional protein folding problem: the survey of the two-dimensional folds of protein ribbons. Adopting this view leads to a practical method of predicting stable protofilament structures of arbitrary sequences. We apply this scheme to variants of Aβ, the amyloid forming peptide that is ch...Continue Reading

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Citations

Aug 28, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xinyu GuPeter G Wolynes
Feb 8, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xun ChenPeter G Wolynes
Jan 10, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Ruth NussinovHyunbum Jang
Jan 20, 2021·The Journal of Physical Chemistry. B·Gregory-Neal Gomes, Zachary A Levine
Aug 14, 2020·The Journal of Physical Chemistry. B·Nathaniel CharestJoan-Emma Shea
May 18, 2019·ACS Chemical Neuroscience·Yuechuan XuPeter G Vekilov
Aug 24, 2021·Frontiers in Molecular Biosciences·Yuan-Wei MaMin-Yeh Tsai
Sep 15, 2021·Proceedings of the National Academy of Sciences of the United States of America·Yuechuan XuPeter G Vekilov

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