help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mihailescu, D.
Right arrow Articles by Smith, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mihailescu, D.
Right arrow Articles by Smith, J. C.

Biophys J, October 2000, p. 1718-1730, Vol. 79, No. 4

Atomic Detail Peptide-Membrane Interactions: Molecular Dynamics Simulation of Gramicidin S in a DMPC Bilayer

Dan Mihailescu*dagger and Jeremy C. Smithdagger

 *Faculty of Biology, University of Bucharest, 76201 Bucharest, Romania; and  dagger Lehrstuhl für Biocomputing, IWR, Universität Heidelberg, D-69120 Heidelberg, Germany

Molecular dynamics simulations have been performed of the sequence-symmetric cyclic decapeptide antibiotic gramicidin S (GS), in interaction with a hydrated dimyristoylphosphatidylcholine (DMPC) bilayer, and the results compared with a "control" simulation of the system in the absence of GS. Following experimental evidence, the GS was initially set in a single antiparallel beta -sheet conformation with two Type II' beta -turns in an amphiphilic interaction with the membrane. This conformation and position remained in the 6.5 ns simulation. Main-chain dihedrals are on average ~26° from those determined by NMR experiment on GS in dimethylsulfoxide (DMSO) solution. Sequence-symmetric main-chain and side-chain dihedral angle pairs converge to within ~5° and ~10°, respectively. The area per lipid, lipid tail order parameters, and quadrupole spin-lattice relaxation times of the control simulation are mostly in good agreement with corresponding experiments. The GS has little effect on the membrane dipole potential or water permeability. However, it is found to have a disordering effect (in agreement with experiment) and a fluidifying effect on lipids directly interacting with it, and an ordering effect on those not directly interacting.

Biophys J, October 2000, p. 1718-1730, Vol. 79, No. 4
© 2000 by the Biophysical Society   0006-3495/00/10/1718/13  $2.00


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
J. A. Vila, D. R. Ripoll, and H. A. Scheraga
Atomically detailed folding simulation of the B domain of staphylococcal protein A from random structures
PNAS, December 9, 2003; 100(25): 14812 - 14816.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
D. E. Elmore and D. A. Dougherty
Investigating Lipid Composition Effects on the Mechanosensitive Channel of Large Conductance (MscL) Using Molecular Dynamics Simulations
Biophys. J., September 1, 2003; 85(3): 1512 - 1524.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the Biophysical Society.