@article{oai:nagoya.repo.nii.ac.jp:00028613,
 author = {Miyazaki, Yusuke and Okazaki, Susumu and Shinoda, Wataru},
 issue = {7},
 journal = {Biochimica et Biophysica Acta (BBA) - Biomembranes},
 month = {Jul},
 note = {Understanding the molecular mechanism underlying pore formation in lipid membranes by antimicrobial peptides is of great importance in biological sciences as well as in drug design applications. Melittin has been widely studied as a pore forming peptide, though the molecular mechanism for pore formation is still illusive. We examined the free energy barrier for the creation of a pore in lipid membranes with and without multiple melittin peptides. It was found that six melittin peptides significantly stabilized a pore, though a small barrier (a few kBT) for the formation still existed. With five melittin peptides or fewer, the pore formation barrier was much higher, though the established pore was in a local energy minimum. Although seven melittins effectively reduced the free energy barrier, a single melittin peptide left the pore after a long time MD simulation probably because of the overcrowded environment around the bilayer pore. Thus, it is highly selective for the number of melittin peptides to stabilize the membrane pore, as was also suggested by the line tension evaluations. The free energy cost required to insert a single melittin into the membrane is too high to explain the one-by-one insertion mechanism for pore formation, which also supports the collective melittin mechanism for pore formation., ファイル公開：2020-07-01},
 pages = {1409--1419},
 title = {Free energy analysis of membrane pore formation process in the presence of multiple melittin peptides},
 volume = {1861},
 year = {2019}
}