A change of the prion protein conformation results in a class of neurodegenerative diseases
called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld–Jakob …

The coordination ability of histidine containing peptides towards Cu2+ ion is discussed. The
binding ability of the peptide strongly depends on the position and number of histidine …

The aggregation of α-synuclein (AS) is characteristic of Parkinson's disease and other
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …

The prion protein (PrP) is a Cu 2+ binding cell surface glycoprotein that can misfold into a β-
sheet-rich conformation to cause prion diseases. The majority of copper binding studies …

The aggregation of α-synuclein (AS) is a critical step in the etiology of Parkinson's disease
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …

Alpha-synuclein (AS) aggregation is associated with neurodegeneration in Parkinson's
disease (PD). At the same time, alterations in metal ion homeostasis may play a pivotal role …

Copper, as an essential element in human body, can have adverse impact on environment
and healthy individuals if it is excessive. So it is necessary to establish a rapid and effective …

Numerous studies have demonstrated the high metal binding capacity and selectivity of
peptide molecules. The terminal amino group, deprotonated amide nitrogens, and various …

Metal ions, especially redox active copper, are thought to play critical roles in
neurodegenerative disorders. As a matter of fact, metal binding may result into severe …

The synthetic peptide encompassing residues 106− 126 (PrP106− 126,
KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for its binding …