Informace o publikaci

Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes

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BROŽEK Radim KABELKA Ivo VÁCHA Robert

Rok publikování 2020
Druh Článek v odborném periodiku
Časopis / Zdroj The Journal of Physical Chemistry B
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://doi.org/10.1021/acs.jpcb.0c03291
Doi http://dx.doi.org/10.1021/acs.jpcb.0c03291
Klíčová slova Free energy; Lipids; Peptides and proteins; Membranes; Conformation
Popis 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.
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