Acta Phys. -Chim. Sin. ›› 2014, Vol. 30 ›› Issue (8): 1587-1596.doi: 10.3866/PKU.WHXB201405291

• BIOPHYSICAL CHEMISTRY • Previous Articles    

Molecular Dynamics Simulations on the Binding of Fullerene to Amyloid-β Oligomers

ZHOU Xiao-Ying, XI Wen-Hui, WEI Guang-Hong   

  1. Department of Physics, Fudan University, Key Laboratory for Computational Physical Sciences Ministry of Education, State Key Laboratory of Surface Physics, Shanghai 200433, P. R. China
  • Received:2014-04-11 Revised:2014-05-28 Published:2014-07-18
  • Contact: WEI Guang-Hong
  • Supported by:

    The project was supported by the National Natural Science Foundation of China (11274075).


We investigated the binding process of fullerene to fibril-like Aβ42 oligomers by performing multiple molecular dynamics simulations. It was observed that the C60 molecule searched a series of positions on the surfaces of the Aβ42 oligomers before finding a stable binding state. Multi-binding sites have been identified and these can be classified into six types according to the type of residue in contact with the fullerene. The sites near the central hydrophobic core (CHC) (17LVFFA21) and the turn region (27NKGAI31) were identified as the most suitable sites with the lowest associated binding energies. These bound states were primarily stabilized by van der Waals interactions, while the solvation effect acted as a destabilizing factor.

Key words: Multi-site binding, Binding energy, Secondary structure disruption, Hydrophobic cave, Groove-rolling mechanism