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@article{1773101,
author = {Bartoš, Ladislav and Kabelka, Ivo and Vácha, Robert},
article_location = {New York, USA},
article_number = {11},
doi = {http://dx.doi.org/10.1016/j.bpj.2021.04.005},
keywords = {CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION},
language = {eng},
issn = {0006-3495},
journal = {Biophysical Journal},
title = {Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.},
url = {https://www.sciencedirect.com/science/article/pii/S0006349521003003?via%3Dihub},
volume = {120},
year = {2021}
}
TY - JOUR
ID - 1773101
AU - Bartoš, Ladislav - Kabelka, Ivo - Vácha, Robert
PY - 2021
TI - Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.
JF - Biophysical Journal
VL - 120
IS - 11
SP - 2296-2305
EP - 2296-2305
PB - Cell Press
SN - 00063495
KW - CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION
UR - https://www.sciencedirect.com/science/article/pii/S0006349521003003?via%3Dihub
N2 - Cell membranes are phospholipid bilayers with a large number of embedded transmembrane proteins. Some of these proteins, such as scramblases, have properties that facilitate lipid flip-flop from one membrane leaflet to another. Scramblases and similar transmembrane proteins could also affect the translocation of other amphiphilic molecules, including cell-penetrating or antimicrobial peptides. We studied the effect of transmembrane proteins on the translocation of amphiphilic peptides through the membrane. Using two very different models, we consistently demonstrate that transmembrane proteins with a hydrophilic patch enhance the translocation of amphiphilic peptides by stabilizing the peptide in the membrane. Moreover, there is an optimum amphiphilicity because the peptide could become overstabilized in the transmembrane state, in which the peptide-protein dissociation is hampered, limiting the peptide translocation. The presence of scramblases and other proteins with similar properties could be exploited for more efficient transport into cells. The described principles could also be utilized in the design of a drug-delivery system by the addition of a translocation-enhancing peptide that would integrate into the membrane.
ER -
BARTOŠ, Ladislav, Ivo KABELKA a Robert VÁCHA. Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins. \textit{Biophysical Journal}. New York, USA: Cell Press, 2021, roč.~120, č.~11, s.~2296-2305. ISSN~0006-3495. Dostupné z: https://dx.doi.org/10.1016/j.bpj.2021.04.005.
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