TY - CHAP
T1 - Molecular Insights into the Effect of Metals on Amyloid Aggregation
AU - Miller, Yifat
N1 - Publisher Copyright:
© 2022, Springer Science+Business Media, LLC, part of Springer Nature.
PY - 2022/1/1
Y1 - 2022/1/1
N2 - 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.
AB - 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.
KW - Amylin
KW - Amyloid β
KW - Amyloidogenic diseases
KW - Metals
KW - Molecular dynamics simulations
KW - α-Synuclein
UR - http://www.scopus.com/inward/record.url?scp=85124612201&partnerID=8YFLogxK
U2 - 10.1007/978-1-0716-1546-1_7
DO - 10.1007/978-1-0716-1546-1_7
M3 - Chapter
C2 - 35167073
AN - SCOPUS:85124612201
T3 - Methods in Molecular Biology
SP - 121
EP - 137
BT - Methods in Molecular Biology
PB - Humana Press Inc.
ER -