Gramicidin Channels in Phospholipid Bilayers with Unsaturated Acyl Chains

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1997 Sep 1

PMID 9284299

Citations 17

Authors

J Girshman

D V Greathouse

R E Koeppe 2nd

O S Andersen

Affiliations

Soon will be listed here.

Abstract

In organic solvents gramicidin A (gA) occurs as a mixture of slowly interconverting double-stranded dimers. Membrane-spanning gA channels, in contrast, are almost exclusively single-stranded beta(6,3)-helical dimers. Based on spectroscopic evidence, it has previously been concluded that the conformational preference of gA in phospholipid bilayers varies as a function of the degree of unsaturation of the acyl chains. Double-stranded pi pi(5,6)-helical dimers predominate (over single-stranded beta(6,3)-helical dimers) in lipid bilayer membranes with polyunsaturated acyl chains. We therefore examined the characteristics of channels formed by gA in 1-palmitoyl-2-oleoylphosphatidylcholine/n-decane, 1,2-dioleoylphosphatidylcholine/n-decane, and 1,2-dilinoleoylphosphatidylcholine/n-decane bilayers. We did not observe long-lived channels that could be conducting double-stranded pi pi(5,6)-helical dimers in any of these different membrane environments. We conclude that the single-stranded beta(6,3)-helical dimer is the only conducting species in these bilayers. Somewhat surprisingly, the average channel duration and channel-forming potency of gA are increased in dilinoleoylphosphatidylcholine/n-decane bilayers compared to 1-palmitoyl-2-oleoylphosphatidylcholine/n-decane and dioleoylphosphatidylcholine/n-decane bilayers. To test for specific interactions between the aromatic side chains of gA and the acyl chains of the bilayer, we examined the properties of channels formed by gramicidin analogues in which the four tryptophan residues were replaced with naphthylalanine (gN), tyrosine (gT), and phenylalanine (gM). The results show that all of these analogue channels experience the same relative stabilization when going from dioleoylphosphatidylcholine to dilinoleoylphosphatidylcholine bilayers.

Citing Articles

Regulation of Gramicidin Channel Function Solely by Changes in Lipid Intrinsic Curvature.

Maer A, Rusinova R, Providence L, Ingolfsson H, Collingwood S, Lundbaek J Front Physiol. 2022; 13:836789.

PMID: 35350699 PMC: 8957996. DOI: 10.3389/fphys.2022.836789.

Exchange of Gramicidin between Lipid Bilayers: Implications for the Mechanism of Channel Formation.

Lum K, Ingolfsson H, Koeppe 2nd R, Andersen O Biophys J. 2017; 113(8):1757-1767.

PMID: 29045870 PMC: 5647621. DOI: 10.1016/j.bpj.2017.08.049.

Characterizing Residue-Bilayer Interactions Using Gramicidin A as a Scaffold and Tryptophan Substitutions as Probes.

Beaven A, Sodt A, Pastor R, Koeppe 2nd R, Andersen O, Im W J Chem Theory Comput. 2017; 13(10):5054-5064.

PMID: 28870079 PMC: 5634937. DOI: 10.1021/acs.jctc.7b00400.

Gramicidin A Channel Formation Induces Local Lipid Redistribution I: Experiment and Simulation.

Beaven A, Maer A, Sodt A, Rui H, Pastor R, Andersen O Biophys J. 2017; 112(6):1185-1197.

PMID: 28355546 PMC: 5375002. DOI: 10.1016/j.bpj.2017.01.028.

Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved peptide.

Wiedman G, Fuselier T, He J, Searson P, Hristova K, Wimley W J Am Chem Soc. 2014; 136(12):4724-31.

PMID: 24588399 PMC: 3985440. DOI: 10.1021/ja500462s.

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