TY - JOUR
T1 - Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations
AU - Goodrich, Carl P.
AU - Kirmizialtin, Serdal
AU - Huyghues-Despointes, Beatrice M.
AU - Zhu, Aiping
AU - Scholtz, J. Martin
AU - Makarov, Dmitrii E.
AU - Movileanu, Liviu
PY - 2007/4/5
Y1 - 2007/4/5
N2 - 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.
AB - 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.
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U2 - 10.1021/jp071364h
DO - 10.1021/jp071364h
M3 - Article
C2 - 17388500
AN - SCOPUS:34247528242
SN - 1520-6106
VL - 111
SP - 3332
EP - 3335
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 13
ER -