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On the Structural Diversity and Individuality of Polymorphic Amyloid Protein Assemblies

Lutter, Liisa, Aubrey, Liam D., Xue, Wei-Feng (2021) On the Structural Diversity and Individuality of Polymorphic Amyloid Protein Assemblies. Journal of Molecular Biology, 433 (20). p. 167124. ISSN 0022-2836. (doi:10.1016/j.jmb.2021.167124) (KAR id:93218)


The prediction of highly ordered three-dimensional structures of amyloid protein fibrils from the amino acid sequences of their monomeric self-assembly precursors constitutes a challenging and unresolved aspect of the classical protein folding problem. Because of the polymorphic nature of amyloid assembly whereby polypeptide chains of identical amino acid sequences under identical conditions are capable of self-assembly into a spectrum of different fibril structures, the prediction of amyloid structures from an amino acid sequence requires a detailed and holistic understanding of its assembly free energy landscape. The full extent of the structure space accessible to the cross-β molecular architecture of amyloid must also be resolved. Here, we review the current understanding of the diversity and the individuality of amyloid structures, and how the polymorphic landscape of amyloid links to biology and disease phenotypes. We present a comprehensive review of structural models of amyloid fibrils derived by cryo-EM, ssNMR and AFM to date, and discuss the challenges ahead for resolving the structural basis and the biological consequences of polymorphic amyloid assemblies.

Item Type: Article
DOI/Identification number: 10.1016/j.jmb.2021.167124
Uncontrolled keywords: amyloid fibril structure polymorphism folding/misfolding protein aggregation
Subjects: Q Science
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 16 Feb 2022 15:06 UTC
Last Modified: 02 Jul 2022 23:00 UTC
Resource URI: (The current URI for this page, for reference purposes)

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