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

doi:10.1021/jp071364h

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Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations

Journal article

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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 and Liviu Movileanu

The journal of physical chemistry. B, Vol.111(13), pp.3332-3335

04/01/2007

DOI: 10.1021/jp071364h

PMID: 17388500

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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.

Details

Title: Subtitle: Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations
Creators: Carl P. Goodrich - Syracuse University
Serdal Kirmizialtin - The University of Texas at Austin
Beatrice M. Huyghues-Despointes - Mitchell Institute
Aiping Zhu - Syracuse University
J. Martin Scholtz - Mitchell Institute
Dmitrii E. Makarov - The University of Texas at Austin
Liviu Movileanu - Syracuse University
Resource Type: Journal article
Publication Details: The journal of physical chemistry. B, Vol.111(13), pp.3332-3335
DOI: 10.1021/jp071364h
PMID: 17388500
NLM abbreviation: J Phys Chem B
ISSN: 1520-6106
eISSN: 1520-5207
Publisher: American Chemical Society
Language: English
Date published: 04/01/2007
Academic Unit: Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
Record Identifier: 9984293081202771

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