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@article{1438436,
author = {Kabelka, Ivo and Vácha, Robert},
article_location = {New York, USA},
article_number = {6},
doi = {http://dx.doi.org/10.1016/j.bpj.2018.08.012},
keywords = {CELL-PENETRATING PEPTIDES; SOLID-STATE NMR; TRANSMEMBRANE HELIX INSERTION; ORIENTED CIRCULAR-DICHROISM; MOLECULAR-DYNAMICS METHOD; ANTIMICROBIAL PEPTIDE; LIPID-BILAYERS; FORCE-FIELD; AMPHIPATHIC PEPTIDES; BUFORIN II},
language = {eng},
issn = {0006-3495},
journal = {Biophysical Journal},
title = {Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane},
volume = {115},
year = {2018}
}
TY - JOUR
ID - 1438436
AU - Kabelka, Ivo - Vácha, Robert
PY - 2018
TI - Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane
JF - Biophysical Journal
VL - 115
IS - 6
SP - 1045-1054
EP - 1045-1054
PB - Cell Press
SN - 00063495
KW - CELL-PENETRATING PEPTIDES
KW - SOLID-STATE NMR
KW - TRANSMEMBRANE HELIX INSERTION
KW - ORIENTED CIRCULAR-DICHROISM
KW - MOLECULAR-DYNAMICS METHOD
KW - ANTIMICROBIAL PEPTIDE
KW - LIPID-BILAYERS
KW - FORCE-FIELD
KW - AMPHIPATHIC PEPTIDES
KW - BUFORIN II
N2 - Cell-penetrating and some antimicrobial peptides can translocate across lipid bilayers without disrupting the membrane structure. However, the molecular properties required for efficient translocation are not fully understood. We employed the Metropolis Monte Carlo method together with coarse-grained models to systematically investigate free-energy landscapes associated with the translocation of secondary amphiphilic peptides. We studied a-helical peptides with different length, amphiphilicity, and distribution of hydrophobic content and found a common translocation path consisting of adsorption, tilting, and insertion. In the adsorbed state, the peptides are parallel to the membrane plane, whereas, in the inserted state, the peptides are perpendicular to the membrane. Our simulations demonstrate that, for all tested peptides, there is an optimal ratio of hydrophilic/hydrophobic content at which the peptides cross the membrane the easiest. Moreover, we show that the hydrophobicity of peptide termini has an important effect on the translocation barrier. These results provide general guidance to optimize peptides for use as carriers of molecular cargos or as therapeutics themselves.
ER -
KABELKA, Ivo and Robert VÁCHA. Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane. \textit{Biophysical Journal}. New York, USA: Cell Press, 2018, vol.~115, No~6, p.~1045-1054. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2018.08.012.
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