Structural Studies of Copper(I) Complexes of Amyloid-β Peptide Fragments: Formation of Two-Coordinate Bis(histidine) Complexes
| Autor: | Kenneth D. Karlin, Ninian J. Blackburn, Gnana S. Siluvai, Richard A. Himes, Ga Young Park |
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| Rok vydání: | 2008 |
| Předmět: |
chemistry.chemical_classification
Reactive oxygen species Amyloid beta-Peptides Amyloid Extended X-ray absorption fine structure Protein Conformation Chemistry Stereochemistry Ligand chemistry.chemical_element General Chemistry Copper Article Peptide Fragments Catalysis Absorptiometry Photon Protein structure Organic chemistry Histidine Beta (finance) |
| Zdroj: | Angewandte Chemie International Edition. 47:9084-9087 |
| ISSN: | 1521-3773 1433-7851 |
| DOI: | 10.1002/anie.200803908 |
| Popis: | The beta bind: Copper(I) binds to amyloid {beta}-peptide fragments (see structure) as a stable bis(histidine), two-coordinate, near-linear complex, even in the presence of potential additional ligands. As has been proposed or assumed in other studies, the copper(I)-peptide complexes react with dioxygen to form the reactive oxygen species H{sub 2}O{sub 2}, without the need for a third histidine ligand to promote the chemistry. |
| Databáze: | OpenAIRE |
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