Characterization of a Disordered Protein during Micellation: Interactions of 伪-Synuclein with Sodium Dodecyl Sulfate

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• 作者：Jianhui Tian ; Anurag Sethi ; Divina Anunciado ; Dung M. Vu ; S. Gnanakaran
• 刊名：The Journal of Physical Chemistry B
• 出版年：2012
• 出版时间：April 19, 2012
• 年：2012
• 卷：116
• 期：15
• 页码：4417-4424
• 全文大小：479K
• 年卷期：v.116,no.15(April 19, 2012)
• ISSN：1520-5207

文摘

To better understand the interaction of 伪-synuclein (伪Syn) with lipid membranes, we carried out self-assembly molecular dynamics simulations of 伪Syn with monomeric and micellar sodium dodecyl sulfate (SDS), a widely used membrane mimic. We find that both electrostatic and hydrophobic forces contribute to the interactions of 伪Syn with SDS. In the presence of 伪Syn, our simulations suggest that SDS aggregates along the protein chain and forms small-size micelles at very early times. Aggregation is followed by formation of a collapsed protein鈥揝DS micelle complex, which is consistent with experimental results. Finally, interaction of 伪Syn with preformed micelles induces alterations in the shape of the micelle, and the N-terminal helix (residues 3 through 37) tends to associate with micelles. Overall, our simulations provide an atomistic description of the early time scale 伪Syn鈥揝DS interaction during the self-assembly of SDS into micelles.