Inverted micelle formation of cell-penetrating peptide studied by coarse-grained simulation: importance of attractive force between cell-penetrating peptides and lipid head group |
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Authors: | Kawamoto Shuhei Takasu Masako Miyakawa Takeshi Morikawa Ryota Oda Tatsuki Futaki Shiroh Nagao Hidemi |
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Affiliation: | Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa 920-1192, Japan. kawamoto@cphys.s.kanazawa-u.ac.jp |
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Abstract: | Arginine-rich peptide and Antennapedia are cell-penetrating peptides (CPPs) which have the ability to permeate plasma membrane. Deformation of the plasma membrane with CPPs is the key to understand permeation mechanism. We investigate the dynamics of CPP and the lipid bilayer membrane by coarse-grained simulation. We found that the peptide makes inverted micelle in the lipid bilayer membrane, when the attractive potential between the peptide and lipid heads is strong. The inverted micelle is formed to minimize potential energy of the peptide. For vesicle membrane, the peptide moves from the outer vesicle to the inner vesicle through the membrane. The translocation of the peptide suggests inverted micelle model as a possible mechanism of CPPs. |
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