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Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions

Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
Membrane model systems consisting of phosphatidylcholines and hydrophobic -helical peptides with tryptophan flanking residues, a characteristic motif for transmembrane protein segments, were used to investigate the contribution of tryptophans to peptide-lipid interactions. Peptides of different lengths and with the flanking tryptophans at different positions in the sequence were incorporated in relatively thick or thin lipid bilayers. The organization of the systems was assessed by NMR methods and by hydrogen/deuterium exchange in combination with mass spectrometry. Previously, it was found that relatively short peptides induce nonlamellar phases and that relatively long analogues order the lipid acyl chains in response to peptide-bilayer mismatch. Here it is shown that these effects do not correlate with the total hydrophobic peptide length, but instead with the length of the stretch between the flanking tryptophan residues. The tryptophan indole ring was consistently found to be positioned near the lipid carbonyl moieties, regardless of the peptide-lipid combination, as indicated by magic angle spinning NMR measurements. These observations suggest that the lipid adaptations are not primarily directed to avoid a peptide-lipid hydrophobic mismatch, but instead to prevent displacement of the tryptophan side chains from the polar-apolar interface. In contrast, long lysine-flanked analogues fully associate with a bilayer without significant lipid adaptations, and hydrogen/deuterium exchange experiments indicate that this is achieved by simply exposing more (hydrophobic) residues to the lipid headgroup region. The results highlight the specific properties that are imposed on transmembrane protein segments by flanking tryptophan residues.
5341-5348
de Planque, M R R
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Bonev, B B
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Demmers, J A A
74e4fc59-6a42-4ef8-be40-696cdd68e457
Greathouse, D V
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Koeppe II, R E
b3a8d97c-f7e2-4cd1-8075-322a28644a1c
Separovic, F
1ca03f7a-0a45-465f-a683-33928d272fcd
Watts, A
e234f61d-ba7f-4ef8-a632-9fec7c896c5b
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Bonev, B B
772027f3-c3dd-407e-abd3-712519324509
Demmers, J A A
74e4fc59-6a42-4ef8-be40-696cdd68e457
Greathouse, D V
a1be1f6a-2843-4999-88d7-8de1ece68708
Koeppe II, R E
b3a8d97c-f7e2-4cd1-8075-322a28644a1c
Separovic, F
1ca03f7a-0a45-465f-a683-33928d272fcd
Watts, A
e234f61d-ba7f-4ef8-a632-9fec7c896c5b
Killian, J A
b54a7210-377f-4cb2-a738-5dcdb953a9bf

de Planque, M R R, Bonev, B B, Demmers, J A A, Greathouse, D V, Koeppe II, R E, Separovic, F, Watts, A and Killian, J A (2003) Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry, 42 (18), 5341-5348. (doi:10.1021/bi27000r).

Record type: Article

Abstract

Membrane model systems consisting of phosphatidylcholines and hydrophobic -helical peptides with tryptophan flanking residues, a characteristic motif for transmembrane protein segments, were used to investigate the contribution of tryptophans to peptide-lipid interactions. Peptides of different lengths and with the flanking tryptophans at different positions in the sequence were incorporated in relatively thick or thin lipid bilayers. The organization of the systems was assessed by NMR methods and by hydrogen/deuterium exchange in combination with mass spectrometry. Previously, it was found that relatively short peptides induce nonlamellar phases and that relatively long analogues order the lipid acyl chains in response to peptide-bilayer mismatch. Here it is shown that these effects do not correlate with the total hydrophobic peptide length, but instead with the length of the stretch between the flanking tryptophan residues. The tryptophan indole ring was consistently found to be positioned near the lipid carbonyl moieties, regardless of the peptide-lipid combination, as indicated by magic angle spinning NMR measurements. These observations suggest that the lipid adaptations are not primarily directed to avoid a peptide-lipid hydrophobic mismatch, but instead to prevent displacement of the tryptophan side chains from the polar-apolar interface. In contrast, long lysine-flanked analogues fully associate with a bilayer without significant lipid adaptations, and hydrogen/deuterium exchange experiments indicate that this is achieved by simply exposing more (hydrophobic) residues to the lipid headgroup region. The results highlight the specific properties that are imposed on transmembrane protein segments by flanking tryptophan residues.

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Published date: 2003
Organisations: Nanoelectronics and Nanotechnology

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Local EPrints ID: 264693
URI: http://eprints.soton.ac.uk/id/eprint/264693
PURE UUID: a69b1fa2-b21b-4167-b2ba-ea52a82aeaed
ORCID for M R R de Planque: ORCID iD orcid.org/0000-0002-8787-0513

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Date deposited: 17 Oct 2007
Last modified: 17 Dec 2019 01:43

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Contributors

Author: M R R de Planque ORCID iD
Author: B B Bonev
Author: J A A Demmers
Author: D V Greathouse
Author: R E Koeppe II
Author: F Separovic
Author: A Watts
Author: J A Killian

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