Molecular Insights into the Effect of Metals on Amyloid Aggregation

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Amyloid diseases such as Alzheimer’s disease (AD), Parkinson’s disease (PD), and type 2 diabetes (T2D) are characterized by accumulation of misfolded proteins’ species, e.g., oligomers and fibrils. The formation of these species occurs via self-assemble of the misfolded proteins in a process which is named “aggregation.” It is known that essential divalent metal ions initiate the aggregation of these misfolded proteins, and that specific concentrations of these metal ions may be implicated in the pathology of amyloid diseases. This chapter focuses on the effects of two of the most common divalent metal ions in the brain—Zn2+ and Cu2+, and while Zn2+ ion is known as a metal that is release from the pancreas. Specifically, the spotlight of this chapter illustrates recent computational molecular modelling studies that investigate the effect of the concentrations of metal ions on aggregation of the misfolded proteins amylin, amyloid β, and α-synuclein. The challenges for computational molecular modeling and future perspectives are discussed.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages121-137
Number of pages17
DOIs
StatePublished - 1 Jan 2022

Publication series

NameMethods in Molecular Biology
Volume2340
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Amylin
  • Amyloid β
  • Amyloidogenic diseases
  • Metals
  • Molecular dynamics simulations
  • α-Synuclein

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