Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.

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Authors

BARTOŠ Ladislav KABELKA Ivo VÁCHA Robert

Year of publication 2021
Type Article in Periodical
Magazine / Source Biophysical Journal
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://www.sciencedirect.com/science/article/pii/S0006349521003003?via%3Dihub
Doi http://dx.doi.org/10.1016/j.bpj.2021.04.005
Keywords CELL-PENETRATING PEPTIDESMOLECULAR-DYNAMICSFORCE-FIELDEXTENSION
Description 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.
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