Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations

Carl P. Goodrich, Serdal Kirmizialtin, Beatrice M. Huyghues-Despointes, Aiping Zhu, J. Martin Scholtz, Dmitrii E. Makarov, Liviu Movileanu

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73 Scopus citations

Abstract

We used single-channel electrical recordings and Langevin molecular dynamics simulations to explore the electrophoretic translocation of various β-hairpin peptides across the staphylococcal α-hemolysin (αHL) protein pore at single-molecule resolution. The β-hairpin peptides, which varied in their folding properties, corresponded to the C terminal residues of the B1 domain of protein G. The translocation time was strongly dependent on the electric force and was correlated with the folding features of the β-hairpin peptides. Highly unfolded peptides entered the pore in an extended conformation, resulting in fast single-file translocation events. In contrast, the translocation of the folded β-hairpin peptides occurred more slowly. In this case, the β-hairpin peptides traversed the αHL pore in a misfolded or fully folded conformation. This study demonstrates that the interaction between a polypeptide and a β-barrel protein pore is dependent on the folding features of the polypeptide.

Original languageEnglish (US)
Pages (from-to)3332-3335
Number of pages4
JournalJournal of Physical Chemistry B
Volume111
Issue number13
DOIs
StatePublished - Apr 5 2007

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ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

Cite this

Goodrich, C. P., Kirmizialtin, S., Huyghues-Despointes, B. M., Zhu, A., Scholtz, J. M., Makarov, D. E., & Movileanu, L. (2007). Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. Journal of Physical Chemistry B, 111(13), 3332-3335. https://doi.org/10.1021/jp071364h