AI Article Synopsis
- Amyloid nanostructures form due to proteins misfolding and aggregating, which contributes to degenerative diseases like Alzheimer's and Parkinson's.
- The study focuses on the Aβ25-35 fragment of amyloid β(1-42) to explore how its secondary structure impacts the toxicity and aggregation of amyloid fibrils.
- Different structural motifs in amyloid aggregates lead to varying degrees of cell membrane disruption and cytotoxicity, aiding in the understanding of how these peptides interact with cells in the context of amyloid diseases.
Article Abstract
Amyloid nanostructures are originated from protein misfolding and aberrant aggregation, which is associated with the pathogenesis of many types of degenerative diseases, such as Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease. The secondary conformation of peptides is of a fundamental importance for aggregation and toxicity of amyloid peptides. In this work, Aβ25-35, a fragment of amyloid β(1-42) (Aβ42), was selected to investigate the correlation between secondary structures and toxicity of amyloid fibrils. Furthermore, each aggregation assemblies show different cell membrane disruption and cytotoxicity. The structural analysis of amyloid aggregates originated from different secondary structure motifs is helpful to understand the mechanism of peptides/cell interactions in the pathogenesis of amyloid diseases.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5768673 | PMC |
| http://dx.doi.org/10.1038/s41598-017-19106-y | DOI Listing |
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