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Molecular dynamics simulation-based understanding of the structure and property of amyloid proteins at multiple length scales

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Abstract

Amyloid proteins, which are known as unstructured protein, are able to self-aggregate to form amyloid fibrils, which are related to pathogenesis of various diseases ranging from neurodegenerative diseases to type 2 diabetes. To gain insight into the underlying mechanism of protein aggregation-driven pathogenesis and to develop the molecular-level therapeutics, it is of great importance to understand the structure, aggregation behavior, and properties of amyloid proteins. In this article, we discuss the current state-of-arts in understanding the structure and properties of amyloid proteins and the future directions in studying the amyloidogenic proteins. Specifically, we show recent efforts that have been made to study the structure and properties of amyloidogenic at multiple length scales ranging from amyloid monomers to amyloid fibrils based on molecular dynamics simulations. The molecular dynamics-based computation has allowed for understanding not only how the structure and aggregation propensity of amyloid monomers but also how the mechanical properties of amyloid fibrils are determined. This suggests that molecular dynamics-based computation will play a pivotal role in unveiling the molecular-level underlying mechanism of protein aggregation-driven pathogenesis.

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  1. Biomechanics Laboratory, College of Sport Science, Sungkyunkwan University, Suwon, 16419, Republic of Korea

    Kilho Eom

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Eom, K. Molecular dynamics simulation-based understanding of the structure and property of amyloid proteins at multiple length scales. JMST Adv. 5, 27–36 (2023). https://doi.org/10.1007/s42791-023-00050-0

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