Structural characterization of Cu2+, Ni2+ and Zn2+ binding sites of model peptides associated with neurodegenerative diseases

C Migliorini, E Porciatti, M Luczkowski… - Coordination Chemistry …, 2012 - Elsevier
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 …

Brain proteins that mind metals: a neurodegenerative perspective

DR Brown - Dalton Transactions, 2009 - pubs.rsc.org
There are numerous neurodegenerative diseases but Alzheimer's disease and Parkinson's
disease are the most common. In contrast, prion diseases are very rare but have sparked …

Spectroscopic and electronic structure studies of copper (II) binding to His111 in the human prion protein fragment 106− 115: evaluating the role of protons and …

L Rivillas-Acevedo, R Grande-Aztatzi, I Lomeli… - Inorganic …, 2011 - ACS Publications
The prion protein (PrPC) is implicated in the spongiform encephalopathies in mammals, and
it is known to bind Cu (II) at the N-terminal region. The region around His111 has been …

Fragment length influences affinity for Cu2+ and Ni2+ binding to His96 or His111 of the prion protein and spectroscopic evidence for a multiple histidine binding …

M Klewpatinond, JH Viles - Biochemical Journal, 2007 - portlandpress.com
The prion protein (PrP) is a Cu2+-binding cell-surface glycoprotein. Using various PrP
fragments and spectroscopic techniques, we show that two Cu2+ ions bind to a region …

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

AHM Emwas, ZA Al‐Talla, X Guo… - Magnetic …, 2013 - Wiley Online Library
Copper is an essential nutrient for the normal development of the brain and nervous system,
although the hallmark of several neurological diseases is a change in copper concentrations …

Structural and dynamic characterization of copper (II) binding of the human prion protein outside the octarepeat region

F Berti, E Gaggelli, R Guerrini, A Janicka… - … A European Journal, 2007 - Wiley Online Library
Human prion protein (hPrP) fragments encompassing the 91–120 region, namely hPrP92–
100 (SP1), hPrP106–113 (SP2), hPrP91–120 (LP1), and hPrP91–114 (LP2), were …

Copper coordination to the prion protein: Insights from theoretical studies

L Quintanar, L Rivillas-Acevedo… - Coordination Chemistry …, 2013 - Elsevier
The cellular prion protein (PrPC) has emerged as an important copper binding protein. The
interaction of copper with PrPC may play important roles in both the physiological function of …

Spectroscopic and Theoretical Study of CuI Binding to His111 in the Human Prion Protein Fragment 106–115

T Arcos-López, M Qayyum, L Rivillas-Acevedo… - Inorganic …, 2016 - ACS Publications
The ability of the cellular prion protein (PrPC) to bind copper in vivo points to a physiological
role for PrPC in copper transport. Six copper binding sites have been identified in the …

Palladium complexes affect the aggregation of human prion protein PrP106-126

Y Wang, L Feng, B Zhang, X Wang, C Huang… - Inorganic …, 2011 - ACS Publications
Many neurodegenerative disorders are induced by protein conformational change. Prion
diseases are characterized by protein conformational conversion from a normal cellular form …

Thermodynamic and spectroscopic investigation on the role of Met residues in CuII binding to the non-octarepeat site of the human prion protein

M Remelli, D Valensin, L Toso, E Gralka… - Metallomics, 2012 - academic.oup.com
Among the common features shared by neurodegenerative diseases there is the central role
played by specific proteins or peptides which accumulate in neurons as insoluble plaques or …