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Correction published on 2 May 2012, see Membranes 2012, 2(2), 214-215.

Open AccessArticle
Membranes 2011, 1(4), 314-326; doi:10.3390/membranes1040314

Self-Assembling Peptide Surfactants A6K and A6D Adopt a-Helical Structures Useful for Membrane Protein Stabilization

Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos #04–01, Singapore 138669, Singapore
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Received: 22 August 2011 / Revised: 30 September 2011 / Accepted: 10 October 2011 / Published: 21 October 2011
(This article belongs to the Special Issue Membranes for Health and Environmental Applications)
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Abstract

Elucidation of membrane protein structures have been greatly hampered by difficulties in producing adequately large quantities of the functional protein and stabilizing them. A6D and A6K are promising solutions to the problem and have recently been used for the rapid production of membrane-bound G protein-coupled receptors (GPCRs). We propose that despite their short lengths, these peptides can adopt α-helical structures through interactions with micelles formed by the peptides themselves. These α-helices are then able to stabilize α-helical motifs which many membrane proteins contain. We also show that A6D and A6K can form β-sheets and appear as weak hydrogels at sufficiently high concentrations. Furthermore, A6D and A6K together in sodium dodecyl sulfate (SDS) can form expected β-sheet structures via a surprising α-helical intermediate.
Keywords: self-assembling peptides; membrane proteins; peptide surfactants; peptide structure; GPCRs self-assembling peptides; membrane proteins; peptide surfactants; peptide structure; GPCRs
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Zhuang, F.; Oglęcka, K.; Hauser, C.A.E. Self-Assembling Peptide Surfactants A6K and A6D Adopt a-Helical Structures Useful for Membrane Protein Stabilization. Membranes 2011, 1, 314-326.

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