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Molecular dynamics studies of interactions between Arg(9)(nona-arginine) and a DOPC/DOPG(4:1) membrane

Title
Molecular dynamics studies of interactions between Arg(9)(nona-arginine) and a DOPC/DOPG(4:1) membrane
Authors
Choe, Seungho
DGIST Authors
Choe, Seungho
Issue Date
2020-10
Citation
AIP Advances, 10(10), 105103
Type
Article
Article Type
Article
Keywords
CELL-PENETRATING PEPTIDESARGININE-RICH PEPTIDESPLASMA-MEMBRANETAT PEPTIDETRANSLOCATIONCURVATUREINTERNALIZATIONSIMULATIONSCHOLESTEROLMECHANISMS
ISSN
2158-3226
Abstract
It has been known that the uptake mechanisms of cell-penetrating peptides (CPPs) depend on the experimental conditions such as the concentration of peptides, lipid composition, and temperature. In this study, we investigate the temperature dependence of the penetration of Arg 9 s into a DOPC/DOPG(4:1) membrane using molecular dynamics (MD) simulations at two different temperatures, T = 310 K and T = 288 K. Although it is difficult to identify the temperature dependence because of having only one single simulation at each temperature and no evidence of translocation of Arg 9 s across the membrane at both temperatures, our simulations suggest that following are strongly correlated with the penetration of Arg 9 s: a number of water molecules coordinated by Arg 9 s and the electrostatic energy between Arg 9 s and the lipid molecules. We also present how Arg 9 s change a bending rigidity of the membrane and how a collective behavior between Arg 9 s enhances the penetration and the membrane bending. Our analyses can be applicable to any CPPs to investigate their interactions with various membranes using MD simulations. © 2020 Author(s).
URI
http://hdl.handle.net/20.500.11750/12609
DOI
10.1063/5.0015665
Publisher
American Institute of Physics Inc.
Related Researcher
  • Author Choe, Seungho Biophysics and Soft Matter (BioSM) Lab
  • Research Interests Theoretical Nuclear & Hadron Physics; Theoretical &Computational Biophysics
Files:
Collection:
Department of Energy Science and EngineeringBiophysics and Soft Matter (BioSM) Lab1. Journal Articles


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