Keywords
Molecular Dynamics Simulation, Alzheimer’S Disease, Amyloid Peptides, Trehalose
Abstract
The molecular dynamics simulation method was used to study the molecular mechanism of trehalose inhibiting the conformational transition of amyloid polypeptide 42 (a¦Â42). The results showed that the concentration of trehalose solution has a very important influence on the conformational transition of a¦Â42. In water and low-concentration trehalose solution ( 0.18mol¡¤l-1), a¦Â42 can transform from the initial ¦Á-helical structure into a ¦Â-sheet secondary structure; but when the trehalose concentration is 0.37mol¡¤l-1, it can effectively inhibit the conformational transformation of a¦Â42. This is Because trehalose uses its preferential exclusion effect to enrich water molecules within 0.2nm around the polypeptide, while itself aggregates near a position 0.4nm away from the polypeptide. In addition, trehalose can also reduce the hydrophobic interaction between polypeptides, Reduce long-distance contacts within the polypeptide molecule and effectively inhibit the hydrophobic collapse and conformational transition of the polypeptide. The results of the above molecular simulation have very important theoretical guidance for the further rational design of efficient inhibitors of Alzheimer’s disease.
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Original research done by Liu Fufeng, Dong Xiaoyan, Sun Yan
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