Chapter title |
Molecular Insights into the Effect of Metals on Amyloid Aggregation.
|
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Book title |
Computer Simulations of Aggregation of Proteins and Peptides
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Published in |
Methods in molecular biology, January 2022
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DOI | 10.1007/978-1-0716-1546-1_7 |
Pubmed ID | |
Book ISBNs |
978-1-07-161545-4, 978-1-07-161546-1
|
Authors |
Miller, Yifat, Yifat Miller |
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. |
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Researcher | 1 | 25% |
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Neuroscience | 1 | 25% |
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