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 Szule, J. A.
Right arrow Articles by Rand, R. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Szule, J. A.
Right arrow Articles by Rand, R. P.
Biophysical Journal 85:1702-1712 (2003)
© 2003 The Biophysical Society

The Effects of Gramicidin on the Structure of Phospholipid Assemblies

J. A. Szule and R. P. Rand

Biological Sciences, Brock University, St. Catharines, Ontario, Canada, L2S 3A1

Correspondence: Address reprint requests to Peter Rand, Brock University, St. Catharines, Ontario, Canada, L2S 3A1. Tel.: 905-688-5550 x-3390; Fax: 905-688-1855; E-mail: rrand{at}spartan.ac.brocku.ca.

Gramicidin is an antibiotic peptide that can be incorporated into the monolayers of cell membranes. Dimerization through hydrogen bonding between gramicidin monomers in opposing leaflets of the membrane results in the formation of an iontophoretic channel. Surrounding phospholipids influence the gating properties of this channel. Conversely, gramicidin incorporation has been shown to affect the structure of spontaneously formed lipid assemblies. Using small-angle x-ray diffraction and model systems composed of phospholipids and gramicidin, the effects produced by gramicidin on lipid layers were measured. These measurements explore how peptides are able to modulate the spontaneous curvature properties of phospholipid assemblies. The reverse hexagonal, HII, phase formed by dioleoylphosphatidylethanolamine (DOPE) monolayers decreased in lattice dimension with increasing incorporation of gramicidin. This indicated that gramicidin itself was adding negative curvature to the lipid layers. In this system, gramicidin was measured to have an apparent intrinsic radius of curvature, of -7.1 Å. The addition of up to 4 mol% gramicidin in DOPE did not result in the monolayers becoming stiffer, as measured by the monolayer bending moduli. Dioleoylphosphatidylcholine (DOPC) alone forms the lamellar (L{alpha}) phase when hydrated, but undergoes a transition into the reverse hexagonal (HII) phase when mixed with gramicidin. The lattice dimension decreases systematically with increased gramicidin content. Again, this indicated that gramicidin was adding negative curvature to the lipid monolayers but the mixture behaved structurally much less consistently than DOPE/gramicidin. Only at 12 mol% gramicidin in dioleoylphosphatidylcholine could an apparent radius of intrinsic curvature of gramicidin be estimated as -7.4 Å. This mixture formed monolayers that were very resistant to bending, with a measured bending modulus of 115 kT.




This article has been cited by other articles:


Home page
ScienceHome page
J. A. Szule and J. R. Coorssen
Comment on "Transmembrane Segments of Syntaxin Line the Fusion Pore of Ca2+-Triggered Exocytosis"
Science, October 29, 2004; 306(5697): 813b - 813b.
[Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2003 by the Biophysical Society.