| CROSS-DISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY |
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Modulation of Amyloid-β Conformation by Charge State of N-Terminal Disordered Region |
| XI Wen-Hui, LI Wen-Fei**, WANG Wei |
| National Laboratory of Solid State Microstructure, and Department of Physics, Nanjing University, Nanjing 210093 |
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Abstract Based on molecular dynamics simulations, we show that variations of the charge states of the histidines, which are the main effects of pH-value change and metal binding, can lead to a drastic change of the intra-peptide interactions of the segment 17–42 and the conformational distribution of the monomeric amyloid-β (Aβ). Since we already knew that the conformational distribution of monomeric Aβ can largely affect Aβ fibrillar aggregation, our results suggest that the pH value change and metal binding can affect the Aβ aggregation by much more complex mechanism than just affecting the inter-peptide interactions. To fully understand the mechanism of metal binding and pH-value induced Aβ aggregation, we also need to consider their effects on the conformational distribution of monomeric Aβ.
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Received: 03 May 2012
Published: 31 July 2012
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| PACS: |
87.15.nr
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(Aggregation)
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87.15.-v
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(Biomolecules: structure and physical properties)
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31.15.xv
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(Molecular dynamics and other numerical methods)
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