Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surface
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- 作者：Sara Y. Chenga ; sara.y.cheng@utexas.edu" class="auth_mail" title="E-mail the corresponding author ; George Choub ; Creighton Buieb ; Mark W. Vaughnb ; Campbell Comptonc ; Kwan H. Chengd ; e ; kcheng1@trinity.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Molecular dynamics simulations ; Asymmetric lipid membrane ; Protein structures on surfaces ; Protein&ndash ; lipid interactions ; Protein aggregation ; Beta-amyloid
- 刊名：Chemistry and Physics of Lipids
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：196
- 期：Complete
- 页码：33-51
- 全文大小：4639 K
文摘
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Studied protein structure on asymmetric bilayer with neutral and anionic lipids and symmetric bilayer with neutral lipids.
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Observed larger folding, domain aggregation, and tilt angle of the absorbed protein on the asymmetric bilayer surfaces.
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Detected more focused bilayer thinning in the asymmetric bilayer due to weaker lipid–protein interactions.
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Lipid order packing rather than transmembrane electric field regulates the protein structure on bilayer surface.