Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue

Ujjayini Ghosh; Wai-Ming Yau; Robert Tycko

doi:10.1039/C8CC01967C

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Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue†

Ujjayini Ghosh,^a Wai-Ming Yau^a and Robert Tycko

*^a

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* Corresponding authors

^a Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 409, Bethesda, Maryland 20892-0520, USA
E-mail: robertty@mail.nih.gov

Abstract

Fibrils formed by 40- and 42-residue amyloid-β (Aβ40 and Aβ42) peptides exhibit molecular-level structural polymorphisms. A recent screen of fibrils derived from brain tissue of Alzheimer's disease patients revealed a single predominant Aβ40 polymorph. We present solid state nuclear magnetic resonance (ssNMR) data that define its coexisting structurally ordered and disordered segments.

This article is part of the themed collection: Amyloid Aggregation

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Article information

DOI: https://doi.org/10.1039/C8CC01967C
Article type: Communication
Submitted: 12 Mar 2018
Accepted: 24 Apr 2018
First published: 24 Apr 2018

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Chem. Commun., 2018,54, 5070-5073

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Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue

U. Ghosh, W. Yau and R. Tycko, Chem. Commun., 2018, 54, 5070 DOI: 10.1039/C8CC01967C

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Chemical Communications

Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue†

Abstract

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Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue

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