Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.

Citation data:

Solid state nuclear magnetic resonance, ISSN: 1527-3326, Vol: 88, Page: 1-14

Publication Year:
2017
Usage 25
Clicks 21
Abstract Views 2
Link-outs 2
Captures 28
Readers 28
Mentions 1
News Mentions 1
Social Media 6
Tweets 6
Citations 7
Citation Indexes 7
PMID:
29035839
DOI:
10.1016/j.ssnmr.2017.10.001
Author(s):
van der Wel, Patrick C A
Publisher(s):
Elsevier BV
Tags:
Physics and Astronomy; Chemistry
Most Recent Tweet View All Tweets
Most Recent News Mention
review description
The aggregation of proteins and peptides into a variety of insoluble, and often non-native, aggregated states plays a central role in many devastating diseases. Analogous processes undermine the efficacy of polypeptide-based biological pharmaceuticals, but are also being leveraged in the design of biologically inspired self-assembling materials. This Trends article surveys the essential contributions made by recent solid-state NMR (ssNMR) studies to our understanding of the structural features of polypeptide aggregates, and how such findings are informing our thinking about the molecular mechanisms of misfolding and aggregation. A central focus is on disease-related amyloid fibrils and oligomers involved in neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntington's disease. SSNMR-enabled structural and dynamics-based findings are surveyed, along with a number of resulting emerging themes that appear common to different amyloidogenic proteins, such as their compact alternating short-β-strand/β-arc amyloid core architecture. Concepts, methods, future prospects and challenges are discussed.