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@article{1680660, author = {Brožek, Radim and Kabelka, Ivo and Vácha, Robert}, article_location = {Washington, D.C.}, article_number = {28}, doi = {http://dx.doi.org/10.1021/acs.jpcb.0c03291}, keywords = {Free energy; Lipids; Peptides and proteins; Membranes; Conformation}, language = {eng}, issn = {1520-6106}, journal = {The Journal of Physical Chemistry B}, title = {Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes}, url = {https://doi.org/10.1021/acs.jpcb.0c03291}, volume = {124}, year = {2020} }
TY - JOUR ID - 1680660 AU - Brožek, Radim - Kabelka, Ivo - Vácha, Robert PY - 2020 TI - Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes JF - The Journal of Physical Chemistry B VL - 124 IS - 28 SP - 5940-5947 EP - 5940-5947 PB - American Chemical Society SN - 15206106 KW - Free energy KW - Lipids KW - Peptides and proteins KW - Membranes KW - Conformation UR - https://doi.org/10.1021/acs.jpcb.0c03291 L2 - https://doi.org/10.1021/acs.jpcb.0c03291 N2 - Biological membranes present a major obstacle for the delivery of therapeutic agents into cells. Some peptides have been shown to translocate across the membrane spontaneously, and they could be thus used as drug-carriers. However, the advantageous peptide properties for the translocation remain unclear. Of particular interest is the effect of a proline-induced kink in alpha-helical peptides, because the kink was previously reported to both increase and decrease the antimicrobial activity. The antimicrobial activity of peptides could be related to their translocation across the membrane as is the case of the buforin 2 peptide investigated here. Using computer simulations with two independent models, we consistently showed that the presence of the kink has (1) no effect on the translocation barrier, (2) reduces the peptide affinity to the membrane, and (3) disfavors the transmembrane state. Moreover, we were able to determine that these effects are mainly caused by the peptide increased polarity, not the increased flexibility of the kink. The provided molecular understanding can be utilized for the design of cell-penetrating and drug-carrying peptides. ER -
BROŽEK, Radim, Ivo KABELKA a Robert VÁCHA. Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes. \textit{The Journal of Physical Chemistry B}. Washington, D.C.: American Chemical Society, 2020, roč.~124, č.~28, s.~5940-5947. ISSN~1520-6106. Dostupné z: https://dx.doi.org/10.1021/acs.jpcb.0c03291.
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