Copper Ion Binding Site in β-Amyloid Peptide
| Autor: | Diana Yugay, Jérôme Gilles, Lisa M. Kawakami, Dominic P. Goronzy, Paul S. Weiss, Yang Yang, Ya-Hong Xie, Zhongbo Yan, Shelley A. Claridge, Tze-Bin Song |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Secondary Aging Circular dichroism Beta sheet Peptide Plasma protein binding Neurodegenerative Alzheimer's Disease 01 natural sciences Protein Structure Secondary 2.1 Biological and endogenous factors Alzheimer's Disease including Alzheimer's Disease Related Dementias General Materials Science Aetiology chemistry.chemical_classification β-amyloid Condensed Matter Physics Amino acid Copper ion binding Neurological scanning tunneling microscopy Alzheimer’s disease Protein Binding Protein Structure Bioengineering 010402 general chemistry 03 medical and health sciences Alzheimer Disease Acquired Cognitive Impairment Humans Histidine Nanoscience & Nanotechnology Binding site Amyloid beta-Peptides Binding Sites binding site Mechanical Engineering Neurosciences Alzheimer's Disease including Alzheimer's Disease Related Dementias (AD/ADRD) General Chemistry histidine brace Peptide Fragments Brain Disorders 0104 chemical sciences Crystallography 030104 developmental biology β-sheet chemistry Biophysics Dementia Copper |
| Zdroj: | Nano letters, vol 16, iss 10 |
| ISSN: | 1530-6992 1530-6984 |
| DOI: | 10.1021/acs.nanolett.6b02590 |
| Popis: | β-Amyloid aggregates in the brain play critical roles in Alzheimer's disease, a chronic neurodegenerative condition. Amyloid-associated metal ions, particularly zinc and copper ions, have been implicated in disease pathogenesis. Despite the importance of such ions, the binding sites on the β-amyloid peptide remain poorly understood. In this study, we use scanning tunneling microscopy, circular dichroism, and surface-enhanced Raman spectroscopy to probe the interactions between Cu2+ ions and a key β-amyloid peptide fragment, consisting of the first 16 amino acids, and define the copper-peptide binding site. We observe that in the presence of Cu2+, this peptide fragment forms β-sheets, not seen without the metal ion. By imaging with scanning tunneling microscopy, we are able to identify the binding site, which involves two histidine residues, His13 and His14. We conclude that the binding of copper to these residues creates an interstrand histidine brace, which enables the formation of β-sheets. |
| Databáze: | OpenAIRE |
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