{"id":16887,"date":"2026-01-08T14:03:17","date_gmt":"2026-01-08T14:03:17","guid":{"rendered":"https:\/\/www.sygnaturediscovery.com\/blog\/alpha-synuclein-an-intriguing-little-protein-mini-review\/"},"modified":"2026-01-08T14:03:17","modified_gmt":"2026-01-08T14:03:17","slug":"alpha-synuclein-an-intriguing-little-protein-mini-review","status":"publish","type":"blog","link":"https:\/\/www.sygnaturediscovery.com\/fr\/blog\/alpha-synuclein-an-intriguing-little-protein-mini-review\/","title":{"rendered":"Alpha Synuclein : An Intriguing Little Protein (Mini Review)"},"content":{"rendered":"\n

In this mini review we discuss Alpha Synuclein (\u03b1Syn), a small, yet curious 140 amino acid long protein that was originally named because of its localisation on synaptic vesicles from the electric lobe of the Pacific Electric Ray,\u00a0Torpedo californica<\/em>\u00a0[1]. Shortly afterwards, \u03b1Syn was reported as the non-amyloid-\u03b2-component (NAC) of amyloid plaques of Alzheimer\u2019s patients [2] and subsequently, missense mutations in \u03b1Syn\u2019s\u00a0SNCA<\/em>\u00a0(aka\u00a0PARK1<\/em>) gene have been linked to \u201csynucleinopathy\u201d diseases that include Parkinson\u2019s disease, Dementia with Lewy bodies and Alzheimer\u2019s disease (reviewed in [3]\u2013[5]).<\/h2>\n\n\n\n

Indeed, Parkinson\u2019s disease is the second most common neurodegenerative disorder that affects >10 million people worldwide, but unfortunately, to date no disease modifying therapies are available. The economic impact of Parkinson\u2019s disease in just the USA alone is estimated to be around $52 billion which, coupled with the devastating effects of these diseases, means that \u03b1Syn is the subject of significant research efforts aiming to develop novel therapeutics, along with methods that will allow an early diagnosis of the conditions.<\/p>\n\n\n\n

\u03b1Syn is predominantly expressed in the brain [6] and is found at high levels in the presynaptic boutons of axons [7]. It has also been detected in erythroid cells [8] and at low levels in other tissues but, in spite of intense study, the precise physiological roles and function of \u03b1Syn still remain unclear (see [4] for a review on the current status of what is known about the function of \u03b1Syn). One theory that is gaining support is that \u03b1Syn functions to promote membrane curvature, thereby contributing to synaptic trafficking and vesicle budding [9], [10].<\/p>\n\n\n\n

Structurally, \u03b1Syn is an intriguing protein. Its N-terminal sequence is divided into seven highly conserved 11-mer repeats with a KTKGEV consensus sequence (residues 1\u201395), which, similar to apolipoproteins, form an amphipathic alpha-helix with 3 turns, and mediate association of \u03b1Syn with lipid membranes. This region also contains the NAC domain (residues 60\u201395), an area believed to be responsible for \u03b1Syn aggregation [2] and sensing of lipid properties [11]. Of particular note is that all identified mutations that are associated with synucleinopathies are located in this region: A30P, A30G, E46K, H50Q, G51D, A53E, A53V and A53T [12]\u2013[20] six of which cluster within eight residues, suggesting that lipid binding or lack thereof may be linked to \u03b1Syn pathology. The C-terminus of \u03b1Syn (residues 96\u2013140) is highly acidic and largely unstructured [21]\u2013[23] and is the target of various post-translational modifications [24]. The C- terminus has been implicated in modulating \u03b1Syns interaction with proteins, metal ions, polycation and polyamine, regulating both its membrane binding and nuclear localisation and protecting \u03b1Syn from aggregation (see [3] and references therein). Acetylation of the N-terminal methionine has been shown to be important for oligomerisation of \u03b1Syn in diseased states [25].<\/p>\n\n\n\n

\"\"
Figure 1: Upon binding to lipid membranes the N-terminus of \u03b1-Synuclein folds into two amphipathic helices. Illustrated by the micelle-bound form of \u03b1-Synuclein (PDB:1XQ8) showing the N-terminus (1 \u2013 59), the NAC (60 \u2013 95) and C-terminus (96 \u2013 140). The right-hand table highlights the seven 11-mer repeat sequences. The disease-linked mutations are located in the 2nd and 4th 11-mer sequences. Adapted from [3] and [26].<\/figcaption><\/figure>\n\n\n\n

In Parkinson\u2019s disease, there is mounting evidence that tiny amounts of misfolded \u03b1Syn species can spread between cells (perhaps in a prion-like manner) and seed the aggregation of the normal, functional \u03b1Syn to form amyloidal plaques [27]. The fibrils of aggregated \u03b1Syn comprise a major part of the amyloid aggregates, present in so-called Lewy bodies. These, and the intermediate oligomeric aggregates present during the course of the aggregation process, are toxic to dopaminergic neurons and thus contribute to degeneration in Parkinson\u2019s.<\/p>\n\n\n\n

There are many NMR, X-Ray and Cryo-EM structures of \u03b1Syn monomer and fibrils in the PDB. (e.g. 1XQ8 [23], 2N0A [28] and 7C1D [29] . However, the picture emerging from these studies is complex. For example, the Cryo-EM studies have identified four distinct types of full length \u03b1Syn fibril to date, known as type 1a \u2018rod\u2019, type 1b \u2018twister\u2019, type 2a and type 2b polymorphs [30].<\/p>\n\n\n\n

For the majority of these structural programmes the \u03b1Syn was expressed in and purified from\u00a0E. coli<\/em>\u00a0with anion exchange chromatography often being included, due to the low 4.67 pI of \u03b1Syn. Stephens et al [31] provide an excellent review of the different methods that have been used to produce monomeric \u03b1Syn with comment on the impact of various steps (such as low pH) on its subsequent functionality.<\/p>\n\n\n\n

\"\"
Figure 2: Amino acid sequence and calculated properties of human wild type \u03b1-Synuclein<\/figcaption><\/figure>\n\n\n\n

Within the Protein Science and Structural Biology department at Sygnature Discovery we have been purifying various forms of \u03b1Syn and other fibril forming proteins for several years. The feedback that we have had is that the monomeric human wild type \u03b1Syn we make is of the highest quality with excellent batch to batch consistency and stability, that displays no self-seeding when used as a substrate within seed aggregation and RT-QuIC assays.<\/p>\n\n\n\n

If this is of interest to your project please dont hesitate to get in touch with us to discuss your particular needs.<\/a><\/p>\n\n\n\n

References<\/h2>\n\n\n\n

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[2] K. U\u00e9da et al., \u2018Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.\u2019, Proc. Natl. Acad. Sci., vol. 90, no. 23, pp. 11282\u201311286, Dec. 1993, doi: 10.1073\/pnas.90.23.11282.<\/p>\n\n\n\n

[3] J. Burr\u00e9, \u2018The Synaptic Function of \u03b1-Synuclein\u2019, J. Parkinsons. Dis., vol. 5, no. 4, pp. 699\u2013713, Oct. 2015, doi: 10.3233\/JPD-150642.<\/p>\n\n\n\n

[4] L. M. A. Oliveira et al., \u2018Alpha-synuclein research: defining strategic moves in the battle against Parkinson\u2019s disease\u2019, npj Park. Dis., vol. 7, no. 1, p. 65, Dec. 2021, doi: 10.1038\/s41531-021-00203-9.<\/p>\n\n\n\n

[5] H. Grosso Jasutkar, S. E. Oh, and M. M. Mouradian, \u2018Therapeutics in the Pipeline Targeting \u03b1 -Synuclein for Parkinson\u2019s Disease\u2019, Pharmacol. Rev., vol. 74, no. 1, pp. 207\u2013237, Jan. 2022, doi: 10.1124\/pharmrev.120.000133.<\/p>\n\n\n\n

[6] R. Jakes, M. G. Spillantini, and M. Goedert, \u2018Identification of two distinct synucleins from human brain\u2019, FEBS Lett., vol. 345, no. 1, pp. 27\u201332, May 1994, doi: 10.1016\/0014-5793(94)00395-5.<\/p>\n\n\n\n

[7] A. Iwai et al., \u2018The precursor protein of non-A\u03b2 component of Alzheimer\u2019s disease amyloid is a presynaptic protein of the central nervous system\u2019, Neuron, vol. 14, no. 2, pp. 467\u2013475, Feb. 1995, doi: 10.1016\/0896-6273(95)90302-X.<\/p>\n\n\n\n

[8] M. Nakai et al., \u2018Expression of \u03b1-synuclein, a presynaptic protein implicated in Parkinson\u2019s disease, in erythropoietic lineage\u2019, Biochem. Biophys. Res. Commun., vol. 358, no. 1, pp. 104\u2013110, Jun. 2007, doi: 10.1016\/j.bbrc.2007.04.108.<\/p>\n\n\n\n

[9] S. Chandra, X. Chen, J. Rizo, R. Jahn, and T. C. S\u00fcdhof, \u2018A Broken \u03b1-Helix in Folded \u03b1-Synuclein\u2019, J. Biol. Chem., vol. 278, no. 17, pp. 15313\u201315318, Apr. 2003, doi: 10.1074\/jbc.M213128200.<\/p>\n\n\n\n

[10] J. Varkey et al., \u2018Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins\u2019, J. Biol. Chem., vol. 285, no. 42, pp. 32486\u201332493, Oct. 2010, doi: 10.1074\/jbc.M110.139576.<\/p>\n\n\n\n

[11] G. Fusco et al., \u2018Direct observation of the three regions in \u03b1-synuclein that determine its membrane-bound behaviour\u2019, Nat. Commun., vol. 5, no. 1, p. 3827, Sep. 2014, doi: 10.1038\/ncomms4827.<\/p>\n\n\n\n

[12] M. H. Polymeropoulos et al., \u2018Mutation in the \u03b1-Synuclein Gene Identified in Families with Parkinson\u2019s Disease\u2019, Science (80-. )., vol. 276, no. 5321, pp. 2045\u20132047, Jun. 1997, doi: 10.1126\/science.276.5321.2045.<\/p>\n\n\n\n

[13] R. Kr\u00fcger et al., \u2018AlaSOPro mutation in the gene encoding \u03b1-synuclein in Parkinson\u2019s disease\u2019, Nat. Genet., vol. 18, no. 2, pp. 106\u2013108, Feb. 1998, doi: 10.1038\/ng0298-106.<\/p>\n\n\n\n

[14] J. J. Zarranz et al., \u2018The new mutation, E46K, of \u03b1-synuclein causes parkinson and Lewy body dementia\u2019, Ann. Neurol., vol. 55, no. 2, pp. 164\u2013173, Feb. 2004, doi: 10.1002\/ana.10795.<\/p>\n\n\n\n

[15] S. Appel-Cresswell et al., \u2018Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson\u2019s disease\u2019, Mov. Disord., vol. 28, no. 6, pp. 811\u2013813, Jun. 2013, doi: 10.1002\/mds.25421.<\/p>\n\n\n\n

[16] C. Proukakis et al., \u2018A novel -synuclein missense mutation in Parkinson disease\u2019, Neurology, vol. 80, no. 11, pp. 1062\u20131064, Mar. 2013, doi: 10.1212\/WNL.0b013e31828727ba.<\/p>\n\n\n\n

[17] S. Lesage et al., \u2018G51D \u03b1-synuclein mutation causes a novel Parkinsonian-pyramidal syndrome\u2019, Ann. Neurol., vol. 73, no. 4, pp. 459\u2013471, Apr. 2013, doi: 10.1002\/ana.23894.<\/p>\n\n\n\n

[18] P. Pasanen et al., \u2018A novel \u03b1-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson\u2019s disease-type pathology\u2019, Neurobiol. Aging, vol. 35, no. 9, pp. 2180.e1-2180.e5, Sep. 2014, doi: 10.1016\/j.neurobiolaging.2014.03.024.<\/p>\n\n\n\n

[19] H. Yoshino et al., \u2018Homozygous alpha-synuclein p.A53V in familial Parkinson\u2019s disease\u2019, Neurobiol. Aging, vol. 57, pp. 248.e7-248.e12, Sep. 2017, doi: 10.1016\/j.neurobiolaging.2017.05.022.<\/p>\n\n\n\n

[20] H. Liu et al., \u2018A Novel SNCA A30G Mutation Causes Familial Parkinson\u02bcs Disease\u2019, Mov. Disord., vol. 36, no. 7, pp. 1624\u20131633, Jul. 2021, doi: 10.1002\/mds.28534.<\/p>\n\n\n\n

[21] R. Bussell and D. Eliezer, \u2018A Structural and Functional Role for 11-mer Repeats in \u03b1-Synuclein and Other Exchangeable Lipid Binding Proteins\u2019, J. Mol. Biol., vol. 329, no. 4, pp. 763\u2013778, Jun. 2003, doi: 10.1016\/S0022-2836(03)00520-5.<\/p>\n\n\n\n

[22] W. S. Davidson, A. Jonas, D. F. Clayton, and J. M. George, \u2018Stabilization of \u03b1-Synuclein Secondary Structure upon Binding to Synthetic Membranes\u2019, J. Biol. Chem., vol. 273, no. 16, pp. 9443\u20139449, Apr. 1998, doi: 10.1074\/jbc.273.16.9443.<\/p>\n\n\n\n

[23] T. S. Ulmer, A. Bax, N. B. Cole, and R. L. Nussbaum, \u2018Structure and Dynamics of Micelle-bound Human \u03b1-Synuclein\u2019, J. Biol. Chem., vol. 280, no. 10, pp. 9595\u20139603, Mar. 2005, doi: 10.1074\/jbc.M411805200.<\/p>\n\n\n\n

[24] A. Oueslati, M. Fournier, and H. A. Lashuel, \u2018Role of post-translational modifications in modulating the structure, function and toxicity of \u03b1-synuclein\u2019, 2010, pp. 115\u2013145.<\/p>\n\n\n\n

[25] A. J. Trexler and E. Rhoades, \u2018N-terminal acetylation is critical for forming \u03b1-helical oligomer of \u03b1-synuclein\u2019, Protein Sci., vol. 21, no. 5, pp. 601\u2013605, May 2012, doi: 10.1002\/pro.2056.<\/p>\n\n\n\n

[26] H. A. Lashuel, C. R. Overk, A. Oueslati, and E. Masliah, \u2018The many faces of \u03b1-synuclein: from structure and toxicity to therapeutic target\u2019, Nat. Rev. Neurosci., vol. 14, no. 1, pp. 38\u201348, Jan. 2013, doi: 10.1038\/nrn3406.<\/p>\n\n\n\n

[27] J. A. Steiner, E. Quansah, and P. Brundin, \u2018The concept of alpha-synuclein as a prion-like protein: ten years after\u2019, Cell Tissue Res., vol. 373, no. 1, pp. 161\u2013173, Jul. 2018, doi: 10.1007\/s00441-018-2814-1.<\/p>\n\n\n\n

[28] M. D. Tuttle et al., \u2018Solid-state NMR structure of a pathogenic fibril of full-length human \u03b1-synuclein\u2019, Nat. Struct. Mol. Biol., vol. 23, no. 5, pp. 409\u2013415, May 2016, doi: 10.1038\/nsmb.3194.<\/p>\n\n\n\n

[29] H. Long et al., \u2018Wild-type \u03b1-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding\u2019, Proc. Natl. Acad. Sci., vol. 118, no. 20, May 2021, doi: 10.1073\/pnas.2012435118.<\/p>\n\n\n\n

[30] R. M. Meade, D. P. Fairlie, and J. M. Mason, \u2018Alpha-synuclein structure and Parkinson\u2019s disease \u2013 lessons and emerging principles\u2019, Mol. Neurodegener., vol. 14, no. 1, p. 29, Dec. 2019, doi: 10.1186\/s13024-019-0329-1.<\/p>\n\n\n\n

[31] A. D. Stephens, D. Matak-Vinkovic, A. Fernandez-Villegas, and G. S. Kaminski Schierle, \u2018Purification of Recombinant \u03b1-synuclein: A Comparison of Commonly Used Protocols\u2019, Biochemistry, vol. 59, no. 48, pp. 4563\u20134572, Dec. 2020, doi: 10.1021\/acs.biochem.0c00725<\/p>\n","protected":false},"excerpt":{"rendered":"","protected":false},"featured_media":16888,"template":"","category":[817,818,1407,815],"class_list":["post-16887","blog","type-blog","status-publish","has-post-thumbnail","hentry","category-domaines-therapeutiques","category-neuroscience","category-protein-expression-and-purification","category-proteines-et-structure"],"acf":[],"yoast_head":"\nAlpha Synuclein : An Intriguing Little Protein (Mini Review) - Sygnature<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.sygnaturediscovery.com\/fr\/blog\/alpha-synuclein-an-intriguing-little-protein-mini-review\/\" \/>\n<meta property=\"og:locale\" content=\"fr_CA\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Alpha Synuclein : An Intriguing Little Protein (Mini Review) - 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