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.
. [J]. 中国物理快报, 2012, 29(8): 88702-088702.
XI Wen-Hui, LI Wen-Fei, and WANG Wei. Modulation of Amyloid-β Conformation by Charge State of N-Terminal Disordered Region. Chin. Phys. Lett., 2012, 29(8): 88702-088702.
2012, Vol. 29 
