{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T06:19:20Z","timestamp":1778653160683,"version":"3.51.4"},"reference-count":79,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2021,7,21]],"date-time":"2021-07-21T00:00:00Z","timestamp":1626825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["CRC 969, A2"],"award-info":[{"award-number":["CRC 969, A2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The 140 amino acid protein \u03b1-synuclein (\u03b1S) is an intrinsically disordered protein (IDP) with various roles and locations in healthy neurons that plays a key role in Parkinson\u2019s disease (PD). Contact with biomembranes can lead to \u03b1-helical conformations, but can also act as s seeding event for aggregation and a predominant \u03b2-sheet conformation. In PD patients, \u03b1S is found to aggregate in various fibrillary structures, and the shift in aggregation and localization is associated with disease progression. Besides full-length \u03b1S, several related polypeptides are present in neurons. The role of many \u03b1S-related proteins in the aggregation of \u03b1S itself is not fully understood Two of these potential aggregation modifiers are the \u03b1S splicing variant \u03b1S \u0394exon3 (\u03943) and the paralog \u03b2-synuclein (\u03b2S). Here, polarized ATR-FTIR spectroscopy was used to study the membrane interaction of these proteins individually and in various combinations. The method allowed a continuous monitoring of both the lipid structure of biomimetic membranes and the aggregation state of \u03b1S and related proteins. The use of polarized light also revealed the orientation of secondary structure elements. While \u03b1S led to a destruction of the lipid membrane upon membrane-catalyzed aggregation, \u03b2S and \u03943 aggregated significantly less, and they did not harm the membrane. Moreover, the latter proteins reduced the membrane damage triggered by \u03b1S. There were no major differences in the membrane interaction for the different synuclein variants. In combination, these observations suggest that the formation of particular protein aggregates is the major driving force for \u03b1S-driven membrane damage. The misbalance of \u03b1S, \u03b2S, and \u03943 might therefore play a crucial role in neurodegenerative disease.<\/jats:p>","DOI":"10.3390\/biom11081067","type":"journal-article","created":{"date-parts":[[2021,7,21]],"date-time":"2021-07-21T11:53:23Z","timestamp":1626868403000},"page":"1067","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Synuclein Family Members Prevent Membrane Damage by Counteracting \u03b1-Synuclein Aggregation"],"prefix":"10.3390","volume":"11","author":[{"given":"Christian","family":"Scheibe","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christiaan","family":"Karreman","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Konstanz, 78457 Konstanz, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9824-4991","authenticated-orcid":false,"given":"Stefan","family":"Schildknecht","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Konstanz, 78457 Konstanz, Germany"},{"name":"Department of Life Sciences, Albstadt-Sigmaringen University of Applied Sciences, 72488 Sigmaringen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3778-8693","authenticated-orcid":false,"given":"Marcel","family":"Leist","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Konstanz, 78457 Konstanz, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0546-9038","authenticated-orcid":false,"given":"Karin","family":"Hauser","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/S1474-4422(18)30295-3","article-title":"Global, regional, and national burden of Parkinson\u2019s disease, 1990\u20132016: A systematic analysis for the Global Burden of Disease Study 2016","volume":"17","author":"Dorsey","year":"2018","journal-title":"Lancet Neurol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1080\/07391102.2003.10506918","article-title":"A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders","volume":"21","author":"Uversky","year":"2003","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1042\/BCJ20170200","article-title":"\u03b1-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking","volume":"474","author":"Lou","year":"2017","journal-title":"Biochem. J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"11915","DOI":"10.1523\/JNEUROSCI.3821-06.2006","article-title":"\u03b1-Synuclein Overexpression in PC12 and Chromaffin Cells Impairs Catecholamine Release by Interfering with a Late Step in Exocytosis","volume":"26","author":"Larsen","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neuron.2009.12.023","article-title":"Increased Expression of \u03b1-Synuclein Reduces Neurotransmitter Release by Inhibiting Synaptic Vesicle Reclustering after Endocytosis","volume":"65","author":"Nemani","year":"2010","journal-title":"Neuron"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"e00592","DOI":"10.7554\/eLife.00592","article-title":"Native \u03b1-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2\/VAMP2","volume":"2","author":"Diao","year":"2013","journal-title":"ELife"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1016\/j.cub.2014.08.027","article-title":"\u03b1-Synuclein Multimers Cluster Synaptic Vesicles and Attenuate Recycling","volume":"24","author":"Wang","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1073\/pnas.97.2.571","article-title":"Acceleration of oligomerization, not fibrillization, is a shared property of both \u03b1-synuclein mutations linked to early-onset Parkinson\u2019s disease: Implications for pathogenesis and therapy","volume":"97","author":"Conway","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"PROTOFIBRILS, PORES, FIBRILS, AND NEURODEGENERATION: Separating the Responsible Protein Aggregates from The Innocent Bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein Misfolding, Functional Amyloid, and Human Disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Van Rooijen, B.D., Claessens, M.M., and Subramaniam, V. (2010). Membrane Permeabilization by Oligomeric alpha-Synuclein: In Search of the Mechanism. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0014292"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"282","DOI":"10.3390\/biom5020282","article-title":"Seeking a mechanism for the toxicity of oligomeric alpha-synuclein","volume":"5","author":"Roberts","year":"2015","journal-title":"Biomolecules"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4336","DOI":"10.1021\/acschemneuro.0c00588","article-title":"Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins","volume":"11","author":"Sciacca","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.bbapap.2019.05.003","article-title":"\u03b1-Synuclein aggregation at low concentrations","volume":"1867","author":"Afitska","year":"2019","journal-title":"Biochim. Biophys. Acta (BBA) Proteins Proteom."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"9443","DOI":"10.1074\/jbc.273.16.9443","article-title":"Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes","volume":"273","author":"Davidson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3827","DOI":"10.1038\/ncomms4827","article-title":"Direct observation of the three regions in \u03b1-synuclein that determine its membrane-bound behaviour","volume":"5","author":"Fusco","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"19666","DOI":"10.1073\/pnas.0807826105","article-title":"Structure of membrane-bound \u03b1-synuclein from site-directed spin labeling and computational refinement","volume":"105","author":"Jao","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.1021\/bi900114z","article-title":"\u03b1-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix","volume":"48","author":"Trexler","year":"2009","journal-title":"Biochemistry"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and Dynamics of Micelle-bound Human \u03b1-Synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2312","DOI":"10.1002\/cbic.201700355","article-title":"Simultaneous IR-Spectroscopic Observation of alpha-Synuclein, Lipids, and Solvent Reveals an Alternative Membrane-Induced Oligomerization Pathway","volume":"18","author":"Fallah","year":"2017","journal-title":"ChemBiochem A Eur. J. Chem. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/s12017-009-8082-1","article-title":"Interaction Between alpha-Synuclein and Metal Ions, Still Looking for a Role in the Pathogenesis of Parkinson\u2019s Disease","volume":"11","author":"Bisaglia","year":"2009","journal-title":"Neuromol. Med."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3245","DOI":"10.1110\/ps.04879704","article-title":"Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain","volume":"13","author":"Lowe","year":"2004","journal-title":"Protein Sci."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Bai, J., Zhang, Z.T., Liu, M.L., and Li, C.G. (2016). Alpha-synuclein-lanthanide metal ions interaction: Binding sites, conformation and fibrillation. BMC Biophys., 9.","DOI":"10.1186\/s13628-016-0026-1"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1016\/j.ccr.2012.03.013","article-title":"Copper, zinc and iron in neurodegenerative diseases (Alzheimer\u2019s, Parkinson\u2019s and prion diseases)","volume":"256","author":"Kozlowski","year":"2012","journal-title":"Coord. Chem. Rev."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"5783","DOI":"10.1021\/bi052151q","article-title":"A Study of the Regional Effects of \u03b1-Synuclein on the Organization and Stability of Phospholipid Bilayers","volume":"45","author":"Madine","year":"2006","journal-title":"Biochemistry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1038\/s41467-018-03111-4","article-title":"C-terminal calcium binding of \u03b1-synuclein modulates synaptic vesicle interaction","volume":"9","author":"Stephens","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the \u03b1-Synuclein Gene Identified in Families with Parkinson\u2019s Disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of \u03b1-synuclein causes parkinson and Lewy body dementia","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann. Neurol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1002\/mds.25502","article-title":"Somatic alpha-synuclein mutations in Parkinson\u2019s disease: Hypothesis and preliminary data","volume":"28","author":"Proukakis","year":"2013","journal-title":"Mov. Disord."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/ana.23894","article-title":"G51D \u03b1-synuclein mutation causes a novel Parkinsonian\u2013pyramidal syndrome","volume":"73","author":"Lesage","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"S29","DOI":"10.1016\/S1353-8020(13)70010-5","article-title":"Update on novel familial forms of Parkinson\u2019s disease and multiple system atrophy","volume":"20","author":"Fujioka","year":"2014","journal-title":"Parkinsonism Relat. Disord."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"10328","DOI":"10.1073\/pnas.1604645113","article-title":"Mutations associated with familial Parkinson\u2019s disease alter the initiation and amplification steps of \u03b1-synuclein aggregation","volume":"113","author":"Flagmeier","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1021\/acschemneuro.8b00579","article-title":"Different Effects of \u03b1-Synuclein Mutants on Lipid Binding and Aggregation Detected by Single Molecule Fluorescence Spectroscopy and ThT Fluorescence-Based Measurements","volume":"10","author":"Ruf","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/0888-7543(95)80208-4","article-title":"The NACP\/synuclein gene: Chromosomal assignment and screening for alterations in Alzheimer disease","volume":"26","author":"Campion","year":"1995","journal-title":"Genomics"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1097\/01.wnr.0000224773.66904.e7","article-title":"Low alpha-synuclein 126 mRNA levels in dementia with Lewy bodies and Alzheimer disease","volume":"17","author":"Beyer","year":"2006","journal-title":"NeuroReport"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.jmb.2012.08.008","article-title":"Quantifying Interactions of \u03b2-Synuclein and \u03b3-Synuclein with Model Membranes","volume":"423","author":"Ducas","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1126\/science.1252884","article-title":"Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins","volume":"344","author":"Wilhelm","year":"2014","journal-title":"Science"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0014-5793(94)00395-5","article-title":"Identification of two distinct synucleins from human brain","volume":"345","author":"Jakes","year":"1994","journal-title":"FEBS Lett."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"267A","DOI":"10.1016\/j.bpj.2013.11.1571","article-title":"Oligomerisation of Alpha-Synuclein at Physiological Concentrations","volume":"106","author":"Iljina","year":"2014","journal-title":"Biophys. J."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"19573","DOI":"10.1073\/pnas.1005005107","article-title":"\u03b1\u03b2\u03b3-Synuclein triple knockout mice reveal age-dependent neuronal dysfunction","volume":"107","author":"Polydoro","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"11970","DOI":"10.1074\/jbc.M109541200","article-title":"Biophysical Properties of the Synucleins and Their Propensities to Fibrillate: INHIBITION OF \u03b1-SYNUCLEIN ASSEMBLY BY \u03b2- AND \u03b3-SYNUCLEINS*","volume":"277","author":"Uversky","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"16368","DOI":"10.1074\/jbc.M117.780528","article-title":"A pH-dependent switch promotes \u03b2-synuclein fibril formation via glutamate residues","volume":"292","author":"Moriarty","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"9096","DOI":"10.1021\/bi048778a","article-title":"Forcing Nonamyloidogenic \u03b2-Synuclein To Fibrillate","volume":"44","author":"Yamin","year":"2005","journal-title":"Biochemistry"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7854","DOI":"10.1039\/C8CC03002B","article-title":"Kinetic barriers to \u03b1-synuclein protofilament formation and conversion into mature fibrils","volume":"54","author":"Brown","year":"2018","journal-title":"Chem. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1212\/01.WNL.0000139870.14385.3C","article-title":"\u03b2-Synuclein gene alterations in dementia with Lewy bodies","volume":"63","author":"Ohtake","year":"2004","journal-title":"Neurology"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.mcn.2013.09.002","article-title":"Counter-regulation of alpha- and beta-synuclein expression at the transcriptional level","volume":"57","author":"Wright","year":"2013","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1021\/ar050073t","article-title":"The aggregation and fibrillation of alpha-synuclein","volume":"39","author":"Fink","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"36010","DOI":"10.1038\/srep36010","article-title":"Beta-Synuclein suppresses both the initiation and amplification steps of alpha-synuclein aggregation via competitive binding to surfaces","volume":"6","author":"Brown","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"15164","DOI":"10.1038\/srep15164","article-title":"Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein","volume":"5","author":"Janowska","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1038\/sj.gt.3302349","article-title":"An antiaggregation gene therapy strategy for Lewy body disease utilizing \u03b2-synuclein lentivirus in a transgenic model","volume":"11","author":"Hashimoto","year":"2004","journal-title":"Gene Ther."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0896-6273(01)00462-7","article-title":"\u03b2-Synuclein Inhibits \u03b1-Synuclein Aggregation: A Possible Role as an Anti-Parkinsonian Factor","volume":"32","author":"Hashimoto","year":"2001","journal-title":"Neuron"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s12031-002-0012-8","article-title":"Development of a new treatment for Alzheimer\u2019s disease and parkinson\u2019s disease using anti-aggregatory \u03b2-synuclein-derived peptides","volume":"19","author":"Windisch","year":"2002","journal-title":"J. Mol. Neurosci."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1800109","DOI":"10.1002\/pmic.201800109","article-title":"Interactions between the Intrinsically Disordered Proteins beta-Synuclein and alpha-Synuclein","volume":"18","author":"Williams","year":"2018","journal-title":"Proteomics"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1002\/ana.23905","article-title":"\u03b2-synuclein aggregates and induces neurodegeneration in dopaminergic neurons","volume":"74","author":"Taschenberger","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/1750-1326-9-43","article-title":"Alpha-synuclein and tau: Teammates in neurodegeneration?","volume":"9","author":"Moussaud","year":"2014","journal-title":"Mol. Neurodegener."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/s12035-012-8330-5","article-title":"Alpha-Synuclein Posttranslational Modification and Alternative Splicing as a Trigger for Neurodegeneration","volume":"47","author":"Beyer","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1016\/j.neurobiolaging.2014.02.009","article-title":"Differential aggregation properties of alpha-synuclein isoforms","volume":"35","author":"Bungeroth","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1073\/pnas.1324209111","article-title":"Splice isoform and pharmacological studies reveal that sterol depletion relocalizes \u03b1-synuclein and enhances its toxicity","volume":"111","author":"Valastyan","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1111\/j.1365-2990.2004.00572.x","article-title":"Differential expression of \u03b1-synuclein isoforms in dementia with Lewy bodies","volume":"30","author":"Beyer","year":"2004","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_61","first-page":"601","article-title":"Enfermedad de Parkinson espor\u00e1dica y familiar: Estudio comparativo","volume":"116","author":"Pastor","year":"2001","journal-title":"Med. Cl\u00edn."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3079","DOI":"10.1021\/bi500027x","article-title":"Equilibrium and Dynamic Spectroscopic Studies of the Interaction of Monomeric \u03b2-Lactoglobulin with Lipid Vesicles at Low pH","volume":"53","author":"Zhang","year":"2014","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"17","DOI":"10.3233\/BSI-180173","article-title":"Orientation of lipids in solid supported lipid bilayers studied by polarized ATR-FTIR spectroscopy","volume":"7","author":"Scheibe","year":"2018","journal-title":"Biomed. Spectrosc. Imaging"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1007\/s00204-021-03024-0","article-title":"A human stem cell-derived test system for agents modifying neuronal N-methyl-D-aspartate-type glutamate receptor Ca(2+)-signalling","volume":"95","author":"Klima","year":"2021","journal-title":"Arch. Toxicol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"736","DOI":"10.2144\/98245bm08","article-title":"Fusion PCR, a one-step variant of the \u201cmegaprimer\u201d method of mutagenesis","volume":"24","author":"Karreman","year":"1998","journal-title":"Biotechniques"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0022-2836(91)90856-2","article-title":"Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor","volume":"219","author":"Dubendorff","year":"1991","journal-title":"J. Mol. Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0304-4157(99)00004-0","article-title":"Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes","volume":"1422","author":"Goormaghtigh","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"11898","DOI":"10.1021\/bi034235+","article-title":"Attenuated Total Reflection Fourier Transform Infrared Spectroscopy:\u2009 A Method of Choice for Studying Membrane Proteins and Lipids","volume":"42","author":"Tatulian","year":"2003","journal-title":"Biochemistry"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1021\/jp105870z","article-title":"In Situ FTIR ATR Spectroscopic Study of the Interaction of Immobilized Human Serum Albumin with Cholate in Aqueous Environment","volume":"115","author":"Hassler","year":"2011","journal-title":"J. Phys. Chem. C"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.chemphys.2011.08.007","article-title":"Time-resolved FTIR spectroscopy for monitoring protein dynamics exemplified by functional studies of Ras protein bound to a lipid bilayer","volume":"396","author":"Gerwert","year":"2012","journal-title":"Chem. Phys."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4448","DOI":"10.1021\/bi00013a038","article-title":"Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy","volume":"34","author":"Tatulian","year":"1995","journal-title":"Biochemistry"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1016\/j.bbamem.2013.04.012","article-title":"ATR-FTIR: A \u201crejuvenated\u201d tool to investigate amyloid proteins","volume":"1828","author":"Sarroukh","year":"2013","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"117563","DOI":"10.1016\/j.saa.2019.117563","article-title":"Influence of phenothiazine molecules on the interactions between positively charged poly-l-lysine and negatively charged DPPC\/DPPG membranes","volume":"227","author":"Trombik","year":"2020","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1007\/s00401-006-0104-6","article-title":"\u03b1-Synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers","volume":"112","author":"Beyer","year":"2006","journal-title":"Acta Neuropathol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/S0022-2836(02)00735-0","article-title":"\u03b1-Synuclein, Especially the Parkinson\u2019s Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils","volume":"322","author":"Lashuel","year":"2002","journal-title":"J. Mol. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Schmidt, F., Levin, J., Kamp, F., Kretzschmar, H., Giese, A., and Botzel, K. (2012). Single-Channel Electrophysiology Reveals a Distinct and Uniform Pore Complex Formed by alpha-Synuclein Oligomers in Lipid Membranes. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0042545"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1016\/j.bbamem.2012.07.007","article-title":"Alpha-synuclein pore forming activity upon membrane association","volume":"1818","author":"Tosatto","year":"2012","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"7065","DOI":"10.1073\/pnas.1601899113","article-title":"Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of alpha-synuclein","volume":"113","author":"Galvagnion","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"100271","DOI":"10.1016\/j.jbc.2021.100271","article-title":"Temperature is a key determinant of alpha- and beta-synuclein membrane interactions in neurons","volume":"296","author":"Ramalingam","year":"2021","journal-title":"J. Biol. Chem."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/8\/1067\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:32:52Z","timestamp":1760164372000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/8\/1067"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,21]]},"references-count":79,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2021,8]]}},"alternative-id":["biom11081067"],"URL":"https:\/\/doi.org\/10.3390\/biom11081067","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,21]]}}}