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Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane Alpha-Helical Peptides

Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane Alpha-Helical Peptides
Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane Alpha-Helical Peptides
Specific interactions of membrane proteins with the membrane interfacial region potentially define protein position with respect to the lipid environment. We investigated the proposed roles of tryptophan and lysine side chains as "anchoring" residues of transmembrane proteins. Model systems were employed, consisting of phosphatidylcholine lipids and hydrophobic -helical peptides, flanked either by tryptophans or lysines. Peptides were incorporated in bilayers of different thickness, and effects on lipid structure were analyzed. Induction of nonbilayer phases and also increases in bilayer thickness were observed that could be explained by a tendency of Trp as well as Lys residues to maintain interactions with the interfacial region. However, effects of the two peptides were remarkably different, indicating affinities of Trp and Lys for different sites at the interface. Our data support a model in which the Trp side chain has a specific affinity for a well defined site near the lipid carbonyl region, while the lysine side chain prefers to be located closer to the aqueous phase, near the lipid phosphate group. The information obtained in this study may further our understanding of the architecture of transmembrane proteins and may prove useful for refining prediction methods for transmembrane segments.
0021-9258
20839-20846
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Kruijtzer, J A W
2472178c-a206-4952-a330-357b7c93f662
Liskamp, R M J
a73b8f95-0d51-4e54-bc61-92cd4acc3d63
Marsh, D
099462b8-c3c5-4fc9-982d-1e91d379b3cf
Greathouse, D V
a1be1f6a-2843-4999-88d7-8de1ece68708
Koeppe II, R E
b3a8d97c-f7e2-4cd1-8075-322a28644a1c
de Kruijff, B
4fc47b39-64da-4eb4-82f7-63eefac2faba
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Kruijtzer, J A W
2472178c-a206-4952-a330-357b7c93f662
Liskamp, R M J
a73b8f95-0d51-4e54-bc61-92cd4acc3d63
Marsh, D
099462b8-c3c5-4fc9-982d-1e91d379b3cf
Greathouse, D V
a1be1f6a-2843-4999-88d7-8de1ece68708
Koeppe II, R E
b3a8d97c-f7e2-4cd1-8075-322a28644a1c
de Kruijff, B
4fc47b39-64da-4eb4-82f7-63eefac2faba
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf

de Planque, M R R, Kruijtzer, J A W, Liskamp, R M J, Marsh, D, Greathouse, D V, Koeppe II, R E, de Kruijff, B and Killian, J A (1999) Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane Alpha-Helical Peptides The Journal of Biological Chemistry, 274, (30), pp. 20839-20846.

Record type: Article

Abstract

Specific interactions of membrane proteins with the membrane interfacial region potentially define protein position with respect to the lipid environment. We investigated the proposed roles of tryptophan and lysine side chains as "anchoring" residues of transmembrane proteins. Model systems were employed, consisting of phosphatidylcholine lipids and hydrophobic -helical peptides, flanked either by tryptophans or lysines. Peptides were incorporated in bilayers of different thickness, and effects on lipid structure were analyzed. Induction of nonbilayer phases and also increases in bilayer thickness were observed that could be explained by a tendency of Trp as well as Lys residues to maintain interactions with the interfacial region. However, effects of the two peptides were remarkably different, indicating affinities of Trp and Lys for different sites at the interface. Our data support a model in which the Trp side chain has a specific affinity for a well defined site near the lipid carbonyl region, while the lysine side chain prefers to be located closer to the aqueous phase, near the lipid phosphate group. The information obtained in this study may further our understanding of the architecture of transmembrane proteins and may prove useful for refining prediction methods for transmembrane segments.

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More information

Published date: July 1999
Organisations: Nanoelectronics and Nanotechnology

Identifiers

Local EPrints ID: 264713
URI: http://eprints.soton.ac.uk/id/eprint/264713
ISSN: 0021-9258
PURE UUID: 375f45fb-f951-4bf7-977e-b57df8f69956
ORCID for M R R de Planque: ORCID iD orcid.org/0000-0002-8787-0513

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Date deposited: 22 Oct 2007
Last modified: 25 Oct 2017 07:29

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Contributors

Author: J A W Kruijtzer
Author: R M J Liskamp
Author: D Marsh
Author: D V Greathouse
Author: R E Koeppe II
Author: B de Kruijff
Author: J A Killian

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