Comparative Molecular Dynamics Study of Aβ Adsorption on the Self-Assembled Monolayers

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• 作者：Qiuming Wang ; Chao Zhao ; Jun Zhao ; Jingdai Wang ; Jui-Chen Yang ; Xiang Yu ; Jie Zheng
• 刊名：Langmuir
• 出版年：2010
• 出版时间：March 2, 2010
• 年：2010
• 卷：26
• 期：5
• 页码：3308-3316
• 全文大小：1135K
• 年卷期：v.26,no.5(March 2, 2010)
• ISSN：1520-5827

文摘

The adsorption and aggregation of the amyloid-β (Aβ) peptides on the cell membrane plays a causal role in the pathogenesis of Alzheimer’s disease. Here, we report all-atom molecular dynamics (MD) simulations to study the interactions of Aβ oligomer with self-assembled monolayers (SAMs) terminated with hydrophobic CH₃ and hydrophilic OH functional groups, with particular interests in how surface chemistry and Aβ orientation affect the adsorption behavior of Aβ. Simulation results show that the CH₃-SAM has a stronger binding affinity to Aβ than the OH-SAM does, although both surfaces can induce Aβ adsorption. Regardless of the characteristics of the surface, the hydrophobic C-terminal region is more likely to be adsorbed on the SAMs, indicating a preferential orientation and interface for Aβ adsorption. Structural and energetic comparison among six Aβ-SAM systems further reveals that Aβ orientation, SAM surface hydrophobicity, and interfacial waters all determine Aβ adsorption behavior on the surface, highlighting the importance of hydrophobic interactions at the interface. This work may provide parallel insights into the interactions of Aβ with lipid bilayers.