Multi‐Frequency,Multi‐Technique Pulsed EPR Investigation of the Copper Binding Site of Murine Amyloid β Peptide |
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| Authors: | Donghun Kim Dr. Jeong Kyu Bang Dr. Sun Hee Kim |
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| Affiliation: | 1. Western Seoul Center, Korea Basic Science Institute, Seoul 120‐140 (Korea);2. Division of Magnetic Resonance Korea Basic Science Institute, Ochang, Chungbuk 363‐883 (Korea) |
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| Abstract: | Copper‐amyloid peptides are proposed to be the cause of Alzheimer’s disease, presumably by oxidative stress. However, mice do not produce amyloid plaques and thus do not suffer from Alzheimer’s disease. Although much effort has been focused on the structural characterization of the copper‐ human amyloid peptides, little is known regarding the copper‐binding mode in murine amyloid peptides. Thus, we investigated the structure of copper‐murine amyloid peptides through multi‐frequency, multi‐technique pulsed EPR spectroscopy in conjunction with specific isotope labeling. Based on our pulsed EPR results, we found that Ala2, Glu3, His6, and His14 are directly coordinated with the copper ion in murine amyloid β peptides at pH 8.5. This is the first detailed structural characterization of the copper‐binding mode in murine amyloid β peptides. This work may advance the knowledge required for developing inhibitors of Alzheimer’s disease. |
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| Keywords: | Alzheimer’ s disease ENDOR EPR spectroscopy HYSCORE murine amyloid peptides |
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