Self-Assembling Peptide Surfactants A6K and A6D Adopt a-Helical Structures Useful for Membrane Protein Stabilization.
| Autor: | Zhuang F; Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos #04-01, Singapore 138669, Singapore. frzhuang.yrp@ibn.a-star.edu.sg., Oglęcka K; Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos #04-01, Singapore 138669, Singapore. koglecka@ibn.a-star.edu.sg., Hauser CA; Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos #04-01, Singapore 138669, Singapore. chauser@ibn.a-star.edu.sg. |
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| Jazyk: | angličtina |
| Zdroj: | Membranes [Membranes (Basel)] 2011 Oct 21; Vol. 1 (4), pp. 314-26. Date of Electronic Publication: 2011 Oct 21. |
| DOI: | 10.3390/membranes1040314 |
| Abstrakt: | 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. |
| Databáze: | MEDLINE |
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