Mutations of Histidine 13 to Arginine and Arginine 5 to Glycine Are Responsible for Different Coordination Sites of Zinc(II) to Human and Murine Peptides

Because mice and rats do not naturally develop Alzheimer's disease, genetically modified animals are required to study this pathology. This striking difference in terms of disease onset could be due to three alterations in the murine sequence (R5G, Y10F and H13R) of the amyloid‐β peptide with r...

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Veröffentlicht in:	Chemistry : a European journal 2018-09, Vol.24 (53), p.14233-14241
Hauptverfasser:	Aliès, Bruno, Borghesani, Valentina, Noël, Sabrina, Sayen, Stephanie, Guillon, Emmanuel, Testemale, Denis, Faller, Peter, Hureau, Christelle
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease amyloid beta-peptides Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - genetics Amyloid beta-Peptides - metabolism analytical chemistry Analytical methods Animals Arginine Arginine - genetics Arginine - metabolism Binding Sites bioinorganic chemistry Chemistry Coordination Complexes - chemistry Coordination Complexes - metabolism Copper - chemistry Copper - metabolism Genetic modification Glycine Glycine - genetics Glycine - metabolism Histidine Histidine - genetics Histidine - metabolism Humans Hydrogen-Ion Concentration Mice mutagenesis Mutagenesis, Site-Directed Mutation Neurodegenerative diseases Nuclear Magnetic Resonance, Biomolecular Peptides pH effects Physiology X-Ray Absorption Spectroscopy Zinc Zinc - chemistry Zinc - metabolism Zinc coordination β-Amyloid
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