Organizations of melittin peptides after spontaneous penetration into cell membranes
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review
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Original language | English |
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Pages (from-to) | 4368-4381 |
Journal / Publication | Biophysical Journal |
Volume | 121 |
Issue number | 22 |
Online published | 4 Oct 2022 |
Publication status | Published - 15 Nov 2022 |
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Link to Scopus | https://www.scopus.com/record/display.uri?eid=2-s2.0-85140052661&origin=recordpage |
Permanent Link | https://scholars.cityu.edu.hk/en/publications/publication(3d7c987c-ad8a-49d8-be24-686ed623d2ee).html |
Abstract
The antimicrobial peptide, melittin, is a potential next-generation antibiotic because melittin can spontaneously form pores in bacterial cell membranes and cause cytoplasm leakage. However, the organizations of melittin peptides in cell membranes remain elusive, which impedes the understanding of the poration mechanism. In this work, we use coarse-grained and all-atom molecular dynamics (MD) simulations to investigate the organizations of melittin peptides during and after spontaneous penetration into DPPC/POPG lipid bilayers. We find that the peptides in lipid bilayers adopt either a transmembrane conformation or a U-shaped conformation, which are referred to as T- and U-peptides, respectively. Several U-peptides and/or T-peptides aggregate to form stable pores. We analyze a T-pore consisting of four T-peptides and a U-pore consisting of three U-peptides and one T-peptide. In both pores, peptides are organized in a manner such that polar residues face inward and hydrophobic residues face outward, which stabilizes the pores and produces water channels. Compared with the U-pore, the T-pore has lower energy, larger pore diameter, and higher permeability. However, the T-pore occurs less frequently than the U-pore in our simulations, probably because the formation of the T-pore is kinetically slower than the U-pore. The stability and permeability of both pores are confirmed by 300 ns all-atom MD simulations. The peptide organizations obtained in this work should deepen the understanding of the stability, poration mechanism, and permeability of melittin, and facilitate the optimization of melittin to enhance the antibacterial ability.
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Organizations of melittin peptides after spontaneous penetration into cell membranes. / Sun, Liang; Wang, Simin; Tian, Fujia et al.
In: Biophysical Journal, Vol. 121, No. 22, 15.11.2022, p. 4368-4381.
In: Biophysical Journal, Vol. 121, No. 22, 15.11.2022, p. 4368-4381.
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review
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