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@article{1335966,
author = {Kabelka, Ivo and Vácha, Robert},
article_location = {Melville (USA)},
article_number = {24},
doi = {http://dx.doi.org/10.1063/1.4933229},
keywords = {PORE FORMATION; ANTIMICROBIAL PEPTIDES; PHOSPHOLIPID MEMBRANE; COMPUTER SIMULATION; COARSE GRAINED; MONTE CARLO},
language = {eng},
issn = {0021-9606},
journal = {JOURNAL OF CHEMICAL PHYSICS},
title = {Optimal conditions for opening of membrane pore by amphiphilic peptides},
url = {http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229},
volume = {143},
year = {2015}
}
TY - JOUR
ID - 1335966
AU - Kabelka, Ivo - Vácha, Robert
PY - 2015
TI - Optimal conditions for opening of membrane pore by amphiphilic peptides
JF - JOURNAL OF CHEMICAL PHYSICS
VL - 143
IS - 24
SP - nestránkováno
EP - nestránkováno
PB - AMER INST PHYSICS
SN - 00219606
KW - PORE FORMATION
KW - ANTIMICROBIAL PEPTIDES
KW - PHOSPHOLIPID MEMBRANE
KW - COMPUTER SIMULATION
KW - COARSE GRAINED
KW - MONTE CARLO
UR - http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229
L2 - http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229
N2 - Amphiphilic peptides can interact with biological membranes and severely affect their barrier and signaling functions. These peptides, including antimicrobial peptides, can self-assemble into transmembrane pores that cause cell death. Despite their medical importance, the conditions required for pore formation remain elusive. Monte Carlo simulations with coarse-grained models enabled us to calculate the free energies of pore opening under various conditions. In agreement with oriented circular dichroism experiments, a high peptide-to-lipid ratio was found to be necessary for spontaneous pore assembly. The peptide length has a non-monotonic impact on pore formation, and the optimal length matches with the membrane thickness. Furthermore, the hydrophobicity of the peptide ends and the mutual positions of peptides on the membrane play a role.
ER -
KABELKA, Ivo a Robert VÁCHA. Optimal conditions for opening of membrane pore by amphiphilic peptides. \textit{JOURNAL OF CHEMICAL PHYSICS}. Melville (USA): AMER INST PHYSICS, 2015, roč.~143, č.~24, s.~nestránkováno, 6 s. ISSN~0021-9606. Dostupné z: https://dx.doi.org/10.1063/1.4933229.
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