Nanostructural Differentiation and Toxicity of Amyloid-β25-35 Aggregates Ensue from Distinct Secondary Conformation

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  • Yongxiu Song, Jiangsu University
  • ,
  • Ping Li, National Center for Nanoscience and Technology (NCNST), Beijing
  • ,
  • Lei Liu, Jiangsu University
  • ,
  • Christian Bortolini
  • ,
  • Mingdong Dong

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, A beta 25-35, a fragment of amyloid beta(1-42) (A beta 42), 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.

Original languageEnglish
Article number765
JournalScientific Reports
Volume8
Number of pages9
ISSN2045-2322
DOIs
Publication statusPublished - 15 Jan 2018

    Research areas

  • ISLET AMYLOID POLYPEPTIDE, ALZHEIMERS-DISEASE, PROTEIN, FIBRILS, PEPTIDES, SPECTROSCOPY

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