Amyloid-β peptide （1-42） aggregation induced by copper ions under acidic conditions
It is well known that the aggregation of amyloid-β peptide （Aβ） induced by Cu^2＋ is related to incubation time, solu-tion pH, and temperature. In this work, the aggregation of Aβ1-42 in the presence of Cu^2＋ under acidic conditions was studied at different incubation time and temperature （e.g. 25 an...
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| Published in | 生物化学与生物物理学报：英文版 no. 7; pp. 570 - 577 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
2013
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| Subjects | |
| Online Access | Get full text |
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| Summary: | It is well known that the aggregation of amyloid-β peptide （Aβ） induced by Cu^2＋ is related to incubation time, solu-tion pH, and temperature. In this work, the aggregation of Aβ1-42 in the presence of Cu^2＋ under acidic conditions was studied at different incubation time and temperature （e.g. 25 and 37℃）. Incubation temperature, pH, and the presence of Cu^2＋ in Aβ solution were confirmed to alter the morphology of aggregation （fibrils or amorphous aggregates）, and the morphology is pivotal for Aβ neuro-toxicity and AIzheimer disease （AD） development. The results of atomic force microscopy （AFM） indicated that the formation of Aβ fibrous morphology is preferred at lower pH, but Cu^2＋ induced the formation of amorphous aggregates. The aggregation rate of Aβ was increased with the elevation of temperature. These results were further confirmed by fluorescence spectroscopy and circular di-chroism spectroscopy and it was found that the formation of β-sheet structure was inhibited by Cu^2＋ binding to Aβ. The result was consistent with AFM observation and the fibrillation process was restrained. We believe that the local charge state in hydrophilic domain of Aβ may play a dom-inant role in the aggregate morphology due to the strong steric hindrance. This research will be valuable for under-standing of Aβ toxicity in AD. |
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| Bibliography: | It is well known that the aggregation of amyloid-β peptide （Aβ） induced by Cu^2＋ is related to incubation time, solu-tion pH, and temperature. In this work, the aggregation of Aβ1-42 in the presence of Cu^2＋ under acidic conditions was studied at different incubation time and temperature （e.g. 25 and 37℃）. Incubation temperature, pH, and the presence of Cu^2＋ in Aβ solution were confirmed to alter the morphology of aggregation （fibrils or amorphous aggregates）, and the morphology is pivotal for Aβ neuro-toxicity and AIzheimer disease （AD） development. The results of atomic force microscopy （AFM） indicated that the formation of Aβ fibrous morphology is preferred at lower pH, but Cu^2＋ induced the formation of amorphous aggregates. The aggregation rate of Aβ was increased with the elevation of temperature. These results were further confirmed by fluorescence spectroscopy and circular di-chroism spectroscopy and it was found that the formation of β-sheet structure was inhibited by Cu^2＋ binding to Aβ. The result was consistent with AFM observation and the fibrillation process was restrained. We believe that the local charge state in hydrophilic domain of Aβ may play a dom-inant role in the aggregate morphology due to the strong steric hindrance. This research will be valuable for under-standing of Aβ toxicity in AD. amyloid-β peptide; copper ions; atomic forcemicroscopy; acidic pH; morphology Yannan Bin, Xia Li, Yonghui He, Shu Chen, Juan Xiang（1 Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education of China, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China 2Institute of Surface Analysis and Biosensing, College of Chemistry and Chemical Engineering, Central South University, Changsha 410083, China 3Key Laboratory of Resources Chemistry of Nonferrous Metals, Ministry of Education, Central South University, Changsha 410083, China） 31-1940/Q |
| ISSN: | 1672-9145 1745-7270 |