Multi-Frequency, Multi-Technique Pulsed EPR Investigation of the Copper Binding Site of Murine Amyloid β Peptide

2014 ◽  
Vol 54 (5) ◽  
pp. 1561-1564 ◽  
Author(s):  
Donghun Kim ◽  
Jeong Kyu Bang ◽  
Sun Hee Kim
Keyword(s):  
Binding Site ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Copper Binding ◽  
Pulsed Epr

Modelling Copper Binding to the Amyloid-β Peptide in Alzheimer

2010 ◽  
Vol 63 (3) ◽  
pp. 345 ◽  
Author(s):  
V. Chandana Epa ◽  
Victor A. Streltsov ◽  
Joseph N. Varghese
Keyword(s):  
Reactive Oxygen Species ◽  
Binding Site ◽  
Reactive Oxygen Species Generation ◽  
Computational Modelling ◽  
Amyloid Β ◽  
Reactive Oxygen ◽  
Oxidative Modification ◽  
Amyloid Β Peptide ◽  
Oxygen Species ◽  
Copper Binding

Oxidative modification due to reactive oxygen species generated by Cu2+ bound to the amyloid-β peptide may be one of the sources of neurodegeneration observed in Alzheimer’s disease. Understanding the structure and function of the copper binding site can assist in the design of effective therapeutics. This paper highlights some of the most significant recent developments in computational modelling studies of the structure of the binding site and reaction mechanisms of reactive oxygen species generation.

Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptides

2000 ◽  
Vol 349 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Marc H. BAUMANN ◽  
Jukka KALLIJÄRVI ◽  
Hilkka LANKINEN ◽  
Claudio SOTO ◽  
Matti HALTIA
Keyword(s):  
Apolipoprotein E ◽  
Binding Site ◽  
Late Onset ◽  
Specific Binding ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Structural Motif ◽  
Amyloid Β Peptide ◽  
High Avidity ◽  
Amyloidogenic Protein

Inheritance of the apolipoprotein E (apoE) ϵ4 allele is a risk factor for late-onset Alzheimer's disease (AD). Biochemically apoE is present in AD plaques and neurofibrillary tangles of the AD brain. There is a high avidity and specific binding of apoE and the amyloid β-peptide (Aβ). In addition to AD apoE is also present in many other cerebral and systemic amyloidoses, Down's syndrome and prion diseases but the pathophysiological basis for its presence is still unknown. In the present study we have compared the interaction of apoE with Aβ, the gelsolin-derived amyloid fragment AGel183-210 and the amyloidogenic prion fragments PrP109-122 and PrP109-141. We show that, similar to Aβ, also AGel and PrP fragments can form a complex with apoE, and that the interaction between apoE and the amyloidogenic protein fragments is mediated through the same binding site on apoE. We also show that apoE increases the thioflavin-T fluorescence of PrP and AGel and that apoE influences the content of β-sheet conformation of these amyloidogenic fragments. Our results indicate that amyloids and amyloidogenic prion fragments share a similar structural motif, which is recognized by apoE, possibly through a single binding site, and that this motif is also responsible for the amyloidogenicity of these fragments.

Affinity of Cu+for the Copper-Binding Domain of the Amyloid-β Peptide of Alzheimer’s Disease

2011 ◽  
Vol 50 (5) ◽  
pp. 1614-1618 ◽  
Author(s):  
Heather A. Feaga ◽  
Richard C. Maduka ◽  
Monique N. Foster ◽  
Veronika A. Szalai
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Binding Domain ◽  
Amyloid Β Peptide ◽  
Copper Binding

Copper Binding Induces Polymorphism in Amyloid-β Peptide: Results of Computational Models

2018 ◽  
Vol 122 (29) ◽  
pp. 7243-7252 ◽  
Author(s):  
Dinh Quoc Huy Pham ◽  
Mai Suan Li ◽  
Giovanni La Penna
Keyword(s):  
Computational Models ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Copper Binding

Computational models explain how copper binding to amyloid-β peptide oligomers enhances oxidative pathways

2019 ◽  
Vol 21 (17) ◽  
pp. 8774-8784 ◽  
Author(s):  
Giovanni La Penna ◽  
Mai Suan Li
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Computational Models ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Copper Binding ◽  
Aβ Peptides ◽  
Intrinsically Disordered ◽  
Disordered Peptides

Amyloid-β (Aβ) peptides are intrinsically disordered peptides and their aggregation is the major hallmark of Alzheimer's disease (AD) development.

Modeling Copper Binding to the Amyloid-β Peptide at Different pH: Toward a Molecular Mechanism for Cu Reduction

2012 ◽  
Vol 116 (39) ◽  
pp. 11899-11910 ◽  
Author(s):  
Sara Furlan ◽  
Christelle Hureau ◽  
Peter Faller ◽  
Giovanni La Penna
Keyword(s):  
Molecular Mechanism ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Copper Binding

Molecular modeling of zinc and copper binding with Alzheimer’s amyloid β-peptide

BioMetals ◽  
2007 ◽  
Vol 21 (2) ◽  
pp. 189-196 ◽  
Author(s):  
Daxiong Han ◽  
Haiyan Wang ◽  
Pin Yang
Keyword(s):  
Molecular Modeling ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Copper Binding

scholarly journals High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide

FEBS Journal ◽  
2006 ◽  
Vol 274 (1) ◽  
pp. 46-59 ◽  
Author(s):  
Jens Danielsson ◽  
Roberta Pierattelli ◽  
Lucia Banci ◽  
Astrid Gräslund
Keyword(s):  
High Resolution ◽  
Binding Site ◽  
Amyloid Β ◽  
Zinc Binding ◽  
Amyloid Β Peptide ◽  
Nmr Studies ◽  
Zinc Binding Site ◽  
High Resolution Nmr
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