Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 21, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/ijms21124287
Keywords
molecular imaging; amyloid beta-peptides; islet amyloid polypeptide; high-speed atomic force microscopy
Funding
- Kanazawa University CHOZEN project
- NIH [AG048934]
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Individual Alzheimer's disease (AD) patients have been shown to have structurally distinct amyloid-beta (A beta) aggregates, including fibrils, in their brain. These findings suggest the possibility of a relationship between AD progression and A beta fibril structures. Thus, the characterization of the structural dynamics of A beta could aid the development of novel therapeutic strategies and diagnosis. Protein structure and dynamics have typically been studied separately. Most of the commonly used biophysical approaches are limited in providing substantial details regarding the combination of both structure and dynamics. On the other hand, high-speed atomic force microscopy (HS-AFM), which simultaneously visualizes an individual protein structure and its dynamics in liquid in real time, can uniquely link the structure and the kinetic details, and it can also unveil novel insights. Although amyloidogenic proteins generate heterogeneously aggregated species, including transient unstable states during the aggregation process, HS-AFM elucidated the structural dynamics of individual aggregates in real time in liquid without purification and isolation. Here, we review and discuss the HS-AFM imaging of amyloid aggregation and strategies to optimize the experiments showing findings from A beta and amylin, which is associated with type II diabetes, shares some common biological features with A beta, and is reported to be involved in AD.
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