Abstract:
:Melittin has been reported to form toroidal pores under certain conditions, but the atomic-resolution structure of these pores is unknown. A 9-μs all-atom molecular-dynamics simulation starting from a closely packed transmembrane melittin tetramer in DMPC shows formation of a toroidal pore after 1 μs. The pore remains stable with a roughly constant radius for the rest of the simulation. Surprisingly, one or two melittin monomers frequently transition between transmembrane and surface states. All four peptides are largely helical. A simulation in a DMPC/DMPG membrane did not lead to a stable pore, consistent with the experimentally observed lower activity of melittin on anionic membranes. The picture that emerges from this work is rather close to the classical toroidal pore, but more dynamic with respect to the configuration of the peptides.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Leveritt JM 3rd,Pino-Angeles A,Lazaridis Tdoi
10.1016/j.bpj.2015.04.006subject
Has Abstractpub_date
2015-05-19 00:00:00pages
2424-2426issue
10eissn
0006-3495issn
1542-0086pii
S0006-3495(15)00384-7journal_volume
108pub_type
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