AI Article Synopsis
- Research on amyloid fibril formation is crucial because it is linked to neurodegenerative diseases like Alzheimer’s, but there’s limited understanding of intermediate states in this process.
- Using liquid-phase transmission electron microscopy, the study visualizes a specific intermediate structure that forms when Aβ42 peptide aggregates, revealing a ring shape with a diameter in the nanometer range.
- The findings also suggest that the air-liquid interface plays a role in accelerating the formation of these amyloid fibrils.
Article Abstract
Protein/peptide amyloid fibril formation is associated with various neurodegenerative diseases and, hence, has been the subject of extensive studies. From a structure-evolution point of view, we now know a great deal about the initial and final states of this process; however, we know very little about its intermediate states. Herein, we employ liquid-phase transmission electron microscopy to directly visualize the formation of one of the intermediates formed during the aggregation process of an amyloid-forming peptide. As shown in figure, we find that Aβ42, the amyloid formation of which has been linked to the development of Alzheimer's disease, can populate a ring-shaped intermediate structure with a diameter of tens of nanometers; additionally, the air-liquid interface can "catalyze" the formation of amyloid fibrils.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11444734 | PMC |
| http://dx.doi.org/10.1063/5.0222349 | DOI Listing |
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