Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide

Significance Alzheimer’s disease is a devastating neurodegenerative disease and the most common cause of dementia. It involves the self-assembly of the amyloid β peptide into fibrillar aggregates through an autocatalytic amplification mechanism—secondary nucleation. This study investigates the mechanism of surface-catalyzed secondary nucleation and asks whether it has a templating role in which nucleating species take up the structure of the parent fibril. This is important in understanding the formation of oligomers, which are considered to be the neurotoxic species during the disease. The results provide a high-resolution view of secondary nucleation and show the steps of attachment, growth along the fibrils and finally detachment and appearance of new fibrils.

• Publication year

  2023

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  2023-06-12

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1073/pnas.2220664120PMID 37307445PMCID 10288637
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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