中国物理B ›› 2018, Vol. 27 ›› Issue (3): 38703-038703.doi: 10.1088/1674-1056/27/3/038703

• INTERDISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY • 上一篇    下一篇

Molecular dynamics simulations of membrane deformation induced by amphiphilic helices of Epsin, Sar1p, and Arf1

Zhen-Lu Li(李振鲁)   

  1. 1 Department of Physiology and Biophysics, Case Western Reserve University, Cleveland 44106, USA;
    2 Department of Physics, Nanjing University, Nanjing 210093, China
  • 收稿日期:2017-10-24 修回日期:2017-12-12 出版日期:2018-03-05 发布日期:2018-03-05
  • 通讯作者: Zhen-Lu Li E-mail:zxl480@case.edu
  • 基金资助:

    Project supported by the National Natural Science Foundation of China (Grant Nos. 91427302 and 11474155).

Molecular dynamics simulations of membrane deformation induced by amphiphilic helices of Epsin, Sar1p, and Arf1

Zhen-Lu Li(李振鲁)1,2   

  1. 1 Department of Physiology and Biophysics, Case Western Reserve University, Cleveland 44106, USA;
    2 Department of Physics, Nanjing University, Nanjing 210093, China
  • Received:2017-10-24 Revised:2017-12-12 Online:2018-03-05 Published:2018-03-05
  • Contact: Zhen-Lu Li E-mail:zxl480@case.edu
  • Supported by:

    Project supported by the National Natural Science Foundation of China (Grant Nos. 91427302 and 11474155).

摘要:

The N-terminal amphiphilic helices of proteins Epsin,Sar1p,and Arf1 play a critical role in initiating membrane deformation.The interactions of these amphiphilic helices with the lipid membranes are investigated in this study by combining the all-atom and coarse-grained simulations.In the all-atom simulations,the amphiphilic helices of Epsin and Sar1p are found to have a shallower insertion depth into the membrane than the amphiphilic helix of Arf1,but remarkably, the amphiphilic helices of Epsin and Sar1p induce higher asymmetry in the lipid packing between the two monolayers of the membrane.The insertion depth of amphiphilic helix into the membrane is determined not only by the overall hydrophobicity but also by the specific distributions of polar and non-polar residues along the helix.To directly compare their ability to deform the membrane,the coarse-grained simulations are performed to investigate the membrane deformation under the insertion of multiple helices.

关键词: cell membrane, amphiphilic helix, membrane deformation, molecular simulation

Abstract:

The N-terminal amphiphilic helices of proteins Epsin,Sar1p,and Arf1 play a critical role in initiating membrane deformation.The interactions of these amphiphilic helices with the lipid membranes are investigated in this study by combining the all-atom and coarse-grained simulations.In the all-atom simulations,the amphiphilic helices of Epsin and Sar1p are found to have a shallower insertion depth into the membrane than the amphiphilic helix of Arf1,but remarkably, the amphiphilic helices of Epsin and Sar1p induce higher asymmetry in the lipid packing between the two monolayers of the membrane.The insertion depth of amphiphilic helix into the membrane is determined not only by the overall hydrophobicity but also by the specific distributions of polar and non-polar residues along the helix.To directly compare their ability to deform the membrane,the coarse-grained simulations are performed to investigate the membrane deformation under the insertion of multiple helices.

Key words: cell membrane, amphiphilic helix, membrane deformation, molecular simulation

中图分类号:  (Protein-membrane interactions)

  • 87.15.kt
87.14.ef (Peptides) 87.14.ep (Membrane proteins) 87.15.ap (Molecular dynamics simulation)