The Effects of Hydrophobic Mismatch between Phosphatidylcholine Bilayers and Transmembrane Alpha-Helical Peptides Depend on the Nature of Interfacially Exposed Aromatic and Charged Residues
The Effects of Hydrophobic Mismatch between Phosphatidylcholine Bilayers and Transmembrane Alpha-Helical Peptides Depend on the Nature of Interfacially Exposed Aromatic and Charged Residues
In this study, we investigated the extent to which different aromatic and positively charged side chains, which often flank transmembrane segments of proteins, can influence lipid-peptide interactions. Model systems consisting of phosphatidylcholine and hydrophobic -helical peptides with different flanking residues were investigated. The peptides were incorporated in relatively thick and in relatively thin lipid bilayers to create a peptide-bilayer hydrophobic mismatch, and the compensating effects on lipid structure were analyzed. When relatively long with respect to the thickness of the bilayer, the peptides that are flanked by the aromatic side chains, Trp, Tyr, and Phe, all induce a significant ordering of the lipid acyl chains, while the peptides flanked by the charged residues Lys, Arg, and His do not. However, when the peptides are relatively short with respect to the thickness of the bilayer, their effect on lipid organization does not depend primarily on their aromatic or charged character. Peptides flanked by Trp, Tyr, Lys, or (at low pH) His residues are effective in inducing mismatch-relieving cubic and inverted hexagonal phases, while analogues flanked by Phe, Arg, or (at neutral pH) His residues cannot induce an inverted hexagonal phase. The different responses to mismatch might reflect the different interfacial affinities of the residues that were investigated.
8396-8404
de Planque, M R R
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Boots, J W P
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Rijkers, D T S
c797cab5-6d4d-457e-88c8-34b162006696
Liskamp, R M J
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Greathouse, D V
a1be1f6a-2843-4999-88d7-8de1ece68708
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf
April 2002
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Boots, J W P
3c58917d-31cd-4365-9a43-2dba55e30a8b
Rijkers, D T S
c797cab5-6d4d-457e-88c8-34b162006696
Liskamp, R M J
a73b8f95-0d51-4e54-bc61-92cd4acc3d63
Greathouse, D V
a1be1f6a-2843-4999-88d7-8de1ece68708
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf
de Planque, M R R, Boots, J W P, Rijkers, D T S, Liskamp, R M J, Greathouse, D V and Killian, J A
(2002)
The Effects of Hydrophobic Mismatch between Phosphatidylcholine Bilayers and Transmembrane Alpha-Helical Peptides Depend on the Nature of Interfacially Exposed Aromatic and Charged Residues.
Biochemistry, 41 (26), .
(doi:10.1021/bi0257686).
Abstract
In this study, we investigated the extent to which different aromatic and positively charged side chains, which often flank transmembrane segments of proteins, can influence lipid-peptide interactions. Model systems consisting of phosphatidylcholine and hydrophobic -helical peptides with different flanking residues were investigated. The peptides were incorporated in relatively thick and in relatively thin lipid bilayers to create a peptide-bilayer hydrophobic mismatch, and the compensating effects on lipid structure were analyzed. When relatively long with respect to the thickness of the bilayer, the peptides that are flanked by the aromatic side chains, Trp, Tyr, and Phe, all induce a significant ordering of the lipid acyl chains, while the peptides flanked by the charged residues Lys, Arg, and His do not. However, when the peptides are relatively short with respect to the thickness of the bilayer, their effect on lipid organization does not depend primarily on their aromatic or charged character. Peptides flanked by Trp, Tyr, Lys, or (at low pH) His residues are effective in inducing mismatch-relieving cubic and inverted hexagonal phases, while analogues flanked by Phe, Arg, or (at neutral pH) His residues cannot induce an inverted hexagonal phase. The different responses to mismatch might reflect the different interfacial affinities of the residues that were investigated.
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Published date: April 2002
Organisations:
Nanoelectronics and Nanotechnology
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Local EPrints ID: 264708
URI: http://eprints.soton.ac.uk/id/eprint/264708
PURE UUID: ed511d6c-085d-4ddc-ad4f-b3b7313f641e
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Date deposited: 22 Oct 2007
Last modified: 14 Mar 2024 07:55
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Author:
M R R de Planque
Author:
J W P Boots
Author:
D T S Rijkers
Author:
R M J Liskamp
Author:
D V Greathouse
Author:
J A Killian
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