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Self-association of model transmembrane alpha-helices is modulated by lipid structure

Self-association of model transmembrane alpha-helices is modulated by lipid structure
Self-association of model transmembrane alpha-helices is modulated by lipid structure
We have developed a fluorescence quenching method using peptides containing 3,5-dibromotryrosine to measure oligomerization of model transmembrane a-helices in lipid bilayers. Peptides of the type Ac-LysLysGlyLeu(m)XLeu(n)LysLysAla-amide where X is tryptophan or 3,5-dibromotyrosine were found to form heterodimers in bilayers of phosphatidylcholine in the liquid-crystalline phase. The free energy of dimer formation changed little with increasing number of Leu residues from 16 to 22 but increased with increasing phospholipid fatty acyl chain length, with a slope of about 0.5 kJ mol(-1) per fatty acyl chain carbon. Peptides were excluded from lipid in the gel phase, resulting in increased levels of oligomerization. Addition of cholesterol to form the liquid-ordered state led to increased dimerization but without phase separation. The presence of phosphatidylethanolamine had little effect on dimerization.
membrane-proteins, coiled coils, sarcoplasmic-reticulum, bilayers, fluorescence
0006-2960
12379-12386
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Broadbridge, R.J.
ce42ee45-e84a-47ec-9706-ef63bef12f2a
Sharma, R.P.
aef51420-fc90-49d8-b04c-142214c2961a
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Broadbridge, R.J.
ce42ee45-e84a-47ec-9706-ef63bef12f2a
Sharma, R.P.
aef51420-fc90-49d8-b04c-142214c2961a
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e

Mall, S., Broadbridge, R.J., Sharma, R.P., East, J.M. and Lee, A.G. (2001) Self-association of model transmembrane alpha-helices is modulated by lipid structure. Biochemistry, 40 (41), 12379-12386. (doi:10.1021/bi011075y).

Record type: Article

Abstract

We have developed a fluorescence quenching method using peptides containing 3,5-dibromotryrosine to measure oligomerization of model transmembrane a-helices in lipid bilayers. Peptides of the type Ac-LysLysGlyLeu(m)XLeu(n)LysLysAla-amide where X is tryptophan or 3,5-dibromotyrosine were found to form heterodimers in bilayers of phosphatidylcholine in the liquid-crystalline phase. The free energy of dimer formation changed little with increasing number of Leu residues from 16 to 22 but increased with increasing phospholipid fatty acyl chain length, with a slope of about 0.5 kJ mol(-1) per fatty acyl chain carbon. Peptides were excluded from lipid in the gel phase, resulting in increased levels of oligomerization. Addition of cholesterol to form the liquid-ordered state led to increased dimerization but without phase separation. The presence of phosphatidylethanolamine had little effect on dimerization.

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Published date: 22 September 2001
Keywords: membrane-proteins, coiled coils, sarcoplasmic-reticulum, bilayers, fluorescence

Identifiers

Local EPrints ID: 25077
URI: http://eprints.soton.ac.uk/id/eprint/25077
ISSN: 0006-2960
PURE UUID: 803d6e9c-db35-42e3-bd1c-8968e34f58ac

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Date deposited: 24 Apr 2006
Last modified: 15 Mar 2024 07:00

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Contributors

Author: S. Mall
Author: R.J. Broadbridge
Author: R.P. Sharma
Author: J.M. East
Author: A.G. Lee

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