The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles
Open accessAbstract
We apply pulsed dipolar ESR spectroscopy (Ku-band DEER) to elucidate the global conformation of the Parkinson's disease-associated protein, alpha-synuclein (alphaS) bound to small unilamellar phospholipid vesicles, rodlike SDS micelles, or lipid bicelles. By measuring distances as long as approximately 7 nm between introduced pairs of nitroxide spin labels, we show that distances are close to the expectations for a single continuous helix in all cases studied. In particular, we find distances of 7.5 nm between sites 24 and 72; 5.5 nm between sites 24 and 61; and 2 nm between sites 35 and 50. We conclude that alphaS does not retain a "hairpin" structure with two antiparallel helices, as is known to occur with spheroidal micelles, in agreement with our earlier finding that the protein's geometry is determined by the surface topology rather than being constrained by the interhelix linker. While the possibility of local helix discontinuities in the structure of membrane-bound alphaS remains, our data are more consistent with one intact helix. Importantly, we demonstrate that bicelles produce very similar results to liposomes, while offering a major improvement in experimentally accessible distance range and resolution, and thus are an excellent lipid membrane mimetic for the purpose of pulse dipolar ESR spectroscopy.
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Cites
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Self-citationEffects of Parkinson's Disease-Linked Mutations on the Structure of Lipid-Associated α-Synuclein
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Self-citation
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Amyloidogenic Protein–Membrane Interactions: Mechanistic Insight from Model Systems
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Cell Biology and Pathophysiology of α-Synuclein
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The Synaptic Function of α-Synuclein
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Fauvet, B., Mbefo, M. K., Fares, M.-B., Desobry, C., Michael, S., Ardah, M. T., Tsika, E., Coune, P., Prudent, M., Lion, N., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.318949 · Cited by 566
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Metadata
- Authors
- Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., & Eliezer, D.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-09-06
- Volume
- 130
- Issue
- 39
- Pages
- 12856-12857
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2026665110
- Cited by
- 275
- References
- 23
- FWCI
- 12.46
- Type
- journal article
- Language
- en
- Open access
- green
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