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  • 标题:Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation
  • 本地全文:下载
  • 作者:Loredana Mereuta ; Mahua Roy ; Alina Asandei
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2014
  • 卷号:4
  • DOI:10.1038/srep03885
  • 出版社:Springer Nature
  • 摘要:The microscopic details of how peptides translocate one at a time through nanopores are crucial determinants for transport through membrane pores and important in developing nano-technologies. To date, the translocation process has been too fast relative to the resolution of the single molecule techniques that sought to detect its milestones. Using pH-tuned single-molecule electrophysiology and molecular dynamics simulations, we demonstrate how peptide passage through the α-hemolysin protein can be sufficiently slowed down to observe intermediate single-peptide sub-states associated to distinct structural milestones along the pore, and how to control residence time, direction and the sequence of spatio-temporal state-to-state dynamics of a single peptide. Molecular dynamics simulations of peptide translocation reveal the time- dependent ordering of intermediate structures of the translocating peptide inside the pore at atomic resolution. Calculations of the expected current ratios of the different pore-blocking microstates and their time sequencing are in accord with the recorded current traces.
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