Optimal conditions for opening of membrane pore by amphiphilic peptides

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Publikace nespadá pod Pedagogickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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KABELKA Ivo VÁCHA Robert

Rok publikování 2015
Druh Článek v odborném periodiku
Časopis / Zdroj JOURNAL OF CHEMICAL PHYSICS
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229
Doi http://dx.doi.org/10.1063/1.4933229
Obor Fyzikální chemie a teoretická chemie
Klíčová slova PORE FORMATION; ANTIMICROBIAL PEPTIDES; PHOSPHOLIPID MEMBRANE; COMPUTER SIMULATION; COARSE GRAINED; MONTE CARLO
Popis 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.
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