Abstract
The ion channel-like nanotube structure of the oligomers of amyloid β-peptide (Aβ) was first investigated by molecular modeling. The results reveal that the hydrogen bond net is one of the key factors to stabilize the structure. The hydrophobicity distribution mode of the side chains is in favor of the structure inserting into the bilayers and forming a hydrophilic pore. The lumen space is under the control of the negative potential, weaker but spreading continuously, to which the cation selectivity attributes; meanwhile, the alternate distribution of the stronger positive and negative potentials makes the electrostatic distribution of the structure framework balance, which is also one of the key factors stabilizing the structure. The results lay the theoretical foundation for illuminating the structure stability and the ion permeability, and give a clue to elucidating the molecular mechanism of Alzheimer’s disease (AD) and designing novel drugs to prevent or reverse AD at the root.
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Supported by the National Natural Science Foundation of China (Grant Nos. 30470408 and 20637010) and the Youth Foundation of Science and Technology of Shanxi Province (Grant No. 2006021009)
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Jiao, Y., Yang, P. Molecular modeling of the ion channel-like nanotube structure of amyloid β-peptide. CHINESE SCI BULL 52, 1576–1580 (2007). https://doi.org/10.1007/s11434-007-0220-2
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DOI: https://doi.org/10.1007/s11434-007-0220-2