{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T13:16:01Z","timestamp":1787836561446,"version":"build-2784847793"},"reference-count":66,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2023,11,9]],"date-time":"2023-11-09T00:00:00Z","timestamp":1699488000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["726368"],"award-info":[{"award-number":["726368"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Heterologous interactions between different amyloid-forming proteins, also called cross-interactions, may have a critical impact on disease-related amyloid formation. \u03b2-hairpin conformers of amyloid-forming proteins have been shown to affect homologous interactions in the amyloid self-assembly process. Here, we applied two \u03b2-hairpin-forming peptides derived from immunoglobulin light chains as models to test how heterologous \u03b2-hairpins modulate the fibril formation of Parkinson\u2019s disease-associated protein \u03b1-synuclein (\u03b1Syn). The peptides SMAhp and LENhp comprise \u03b2-strands C and C\u2032 of the \u03ba4 antibodies SMA and LEN, which are associated with light chain amyloidosis and multiple myeloma, respectively. SMAhp and LENhp bind with high affinity to the \u03b2-hairpin-binding protein \u03b2-wrapin AS10 according to isothermal titration calorimetry and NMR spectroscopy. The addition of SMAhp and LENhp affects the kinetics of \u03b1Syn aggregation monitored by Thioflavin T (ThT) fluorescence, with the effect depending on assay conditions, salt concentration, and the applied \u03b2-hairpin peptide. In the absence of agitation, substoichiometric concentrations of the hairpin peptides strongly reduce the lag time of \u03b1Syn aggregation, suggesting that they support the nucleation of \u03b1Syn amyloid fibrils. The effect is also observed for the aggregation of \u03b1Syn fragments lacking the N-terminus or the C-terminus, indicating that the promotion of nucleation involves the interaction of hairpin peptides with the hydrophobic non-amyloid-\u03b2 component (NAC) region.<\/jats:p>","DOI":"10.3390\/ijms242216132","type":"journal-article","created":{"date-parts":[[2023,11,9]],"date-time":"2023-11-09T08:08:58Z","timestamp":1699517338000},"page":"16132","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Nucleation of \u03b1-Synuclein Amyloid Fibrils Induced by Cross-Interaction with \u03b2-Hairpin Peptides Derived from Immunoglobulin Light Chains"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2421-0304","authenticated-orcid":false,"given":"Laetitia F.","family":"Heid","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5151-6424","authenticated-orcid":false,"given":"Tatsiana","family":"Kupreichyk","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"},{"name":"Institute of Biological Information Processing (IBI-7) and JuStruct, J\u00fclich Center for Structural Biology, Forschungszentrum J\u00fclich, 52425 J\u00fclich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie P.","family":"Sch\u00fctzmann","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walfried","family":"Schneider","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Stoldt","sequence":"additional","affiliation":[{"name":"Institute of Biological Information Processing (IBI-7) and JuStruct, J\u00fclich Center for Structural Biology, Forschungszentrum J\u00fclich, 52425 J\u00fclich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4301-5416","authenticated-orcid":false,"given":"Wolfgang","family":"Hoyer","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, 40204 D\u00fcsseldorf, Germany"},{"name":"Institute of Biological Information Processing (IBI-7) and JuStruct, J\u00fclich Center for Structural Biology, Forschungszentrum J\u00fclich, 52425 J\u00fclich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,11,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of a-synuclein: From structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1038\/s41531-021-00203-9","article-title":"Alpha-synuclein research: Defining strategic moves in the battle against Parkinson\u2019s disease","volume":"7","author":"Oliveira","year":"2021","journal-title":"NPJ Park. Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/B978-0-444-63945-5.00017-9","article-title":"Prion-like propagation of pathology in Parkinson disease","volume":"153","author":"Brundin","year":"2018","journal-title":"Handb. Clin. Neurol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1146\/annurev-biochem-072611-130030","article-title":"Systemic amyloidoses","volume":"82","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_6","first-page":"2523","article-title":"Amyloid formation in light chain amyloidosis","volume":"12","year":"2012","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/bs.ircmb.2016.08.014","article-title":"The Nucleation of Protein Aggregates\u2014From Crystals to Amyloid Fibrils","volume":"329","author":"Buell","year":"2017","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s12551-017-0353-8","article-title":"Recent progress on understanding the mechanisms of amyloid nucleation","volume":"10","author":"Chatani","year":"2018","journal-title":"Biophys. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nchembio.1750","article-title":"Lipid vesicles trigger a-synuclein aggregation by stimulating primary nucleation","volume":"11","author":"Galvagnion","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"e2012171118","DOI":"10.1073\/pnas.2012171118","article-title":"Structural insights into a-synuclein monomer-fibril interactions","volume":"118","author":"Kumari","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2866","DOI":"10.1021\/ja412105t","article-title":"The presence of an air-water interface affects formation and elongation of a-synuclein fibrils","volume":"136","author":"Campioni","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.neuron.2019.10.010","article-title":"Amyloid-beta (Ab) plaques promote seeding and spreading of alpha-synuclein and tau in a mouse model of Lewy body disorders with Ab pathology","volume":"105","author":"Bassil","year":"2020","journal-title":"Neuron"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1007\/s11064-006-9140-9","article-title":"Interaction between Ab peptide and a synuclein: Molecular mechanisms in overlapping pathology of Alzheimer\u2019s and Parkinson\u2019s in dementia with Lewy body disease","volume":"31","author":"Mandal","year":"2006","journal-title":"Neurochem. Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1073\/pnas.1610371113","article-title":"Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson\u2019s disease","volume":"113","author":"Horvath","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1007\/s00401-018-1832-0","article-title":"Interaction of amyloidogenic proteins in pancreatic b cells from subjects with synucleinopathies","volume":"135","author":"Marcilla","year":"2018","journal-title":"Acta Neuropathol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/978-1-4939-1486-9_2","article-title":"Design of monomeric water-soluble b-hairpin and b-sheet peptides","volume":"1216","author":"Jimenez","year":"2014","journal-title":"Methods Mol. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"165103","DOI":"10.1063\/1.4826461","article-title":"The universality of b-hairpin misfolding indicated by molecular dynamics simulations","volume":"139","author":"Shao","year":"2013","journal-title":"J. Chem. Phys."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"18283","DOI":"10.1021\/ja903814q","article-title":"Human islet amyloid polypeptide monomers form ordered b-hairpins: A possible direct amyloidogenic precursor","volume":"131","author":"Dupuis","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Gill, A.C. (2014). b-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0087354"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1021\/jp808914c","article-title":"Influence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Ab peptides with implications for rates of fibril formation","volume":"113","author":"Reddy","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1016\/j.jmb.2013.06.021","article-title":"Ab monomers transiently sample oligomer and fibril-like configurations: Ensemble characterization using a combined MD\/NMR approach","volume":"425","author":"Rosenman","year":"2013","journal-title":"J. Mol. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.jmb.2011.05.014","article-title":"Monte Carlo study of the formation and conformational properties of dimers of Abeta42 variants","volume":"410","author":"Mitternacht","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"243142","DOI":"10.1063\/1.4936910","article-title":"Transient b-hairpin formation in a-synuclein monomer revealed by coarse-grained molecular dynamics simulation","volume":"143","author":"Yu","year":"2015","journal-title":"J. Chem. Phys."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"6311","DOI":"10.1021\/jp301619v","article-title":"Dynamics of metastable b-hairpin structures in the folding nucleus of amyloid b-protein","volume":"116","author":"Cruz","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1110\/ps.041292205","article-title":"On the nucleation of amyloid b-protein monomer folding","volume":"14","author":"Lazo","year":"2005","journal-title":"Protein Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1733","DOI":"10.1039\/C5CC08107F","article-title":"Allosteric stabilization of the amyloid-b peptide hairpin by the fluctuating N-terminal","volume":"52","author":"Xu","year":"2016","journal-title":"Chem. Commun."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.molcel.2011.05.013","article-title":"Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins","volume":"43","author":"Halfmann","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"11835","DOI":"10.1073\/pnas.1612362113","article-title":"Exploring the aggregation free energy landscape of the amyloid-b protein (1-40)","volume":"113","author":"Zheng","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.1016\/j.bpj.2013.04.056","article-title":"Differences in b-strand populations of monomeric Ab40 and Ab42","volume":"104","author":"Ball","year":"2013","journal-title":"Biophys. J."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"10478","DOI":"10.1021\/acs.jpcb.5b05593","article-title":"Structures of the Alzheimer\u2019s wild-type Ab1-40 dimer from atomistic simulations","volume":"119","author":"Tarus","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1021\/ja905595k","article-title":"Oligomers of the prion protein fragment 106-126 are likely assembled from b-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide\u2019s monomeric conformation","volume":"132","author":"Grabenauer","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"155101","DOI":"10.1063\/1.4798460","article-title":"a-helix to b-hairpin transition of human amylin monomer","volume":"138","author":"Singh","year":"2013","journal-title":"J. Chem. Phys."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2208","DOI":"10.1016\/j.bpj.2010.07.014","article-title":"Stable and metastable states of human amylin in solution","volume":"99","author":"Reddy","year":"2010","journal-title":"Biophys. J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"4655","DOI":"10.1021\/bi036248t","article-title":"Folding into a b-hairpin can prevent amyloid fibril formation","volume":"43","author":"Hosia","year":"2004","journal-title":"Biochemistry"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6003","DOI":"10.1021\/bi0474867","article-title":"Ab40-Lactam(D23\/K28) models a conformation highly favorable for nucleation of amyloid","volume":"44","author":"Sciarretta","year":"2005","journal-title":"Biochemistry"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"11331","DOI":"10.1039\/D0SC04051G","article-title":"Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of a-synuclein","volume":"11","author":"Agerschou","year":"2020","journal-title":"Chem. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Agerschou, E.D., Sch\u00fctzmann, M.P., Reppert, N., W\u00f6rdehoff, M.M., Shaykhalishahi, H., Buell, A.K., and Hoyer, W. (2021). b-Turn exchanges in the a-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation. Biophys. Chem., 269.","DOI":"10.1016\/j.bpc.2020.106519"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"9070","DOI":"10.1021\/acsnano.5b03175","article-title":"Cell-membrane-mimicking lipid-coated nanoparticles confer Raman enhancement to membrane proteins and reveal membrane-attached amyloid-b conformation","volume":"9","author":"Bhowmik","year":"2015","journal-title":"ACS Nano"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2344","DOI":"10.1038\/s41598-017-02454-0","article-title":"Nano-assembly of amyloid b peptide: Role of the hairpin fold","volume":"7","author":"Maity","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1021\/cn2001188","article-title":"An azobenzene photoswitch sheds light on turn nucleation in amyloid-b self-assembly","volume":"3","author":"Doran","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"12756","DOI":"10.1002\/anie.201406357","article-title":"A hexameric peptide barrel as building block of amyloid-b protofibrils","volume":"53","author":"Lendel","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-b oligomers by protein engineering","volume":"107","author":"Sandberg","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"9685","DOI":"10.1021\/jacs.8b05925","article-title":"Hetero-oligomeric amyloid assembly and mechanism: Prion fragment PrP(106-126) catalyzes the islet amyloid polypeptide b-hairpin","volume":"140","author":"Ilitchev","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"11811","DOI":"10.1038\/s41598-017-11671-6","article-title":"A Toxic Conformer of Ab42 with a Turn at 22-23 is a Novel Therapeutic Target for Alzheimer\u2019s Disease","volume":"7","author":"Izuo","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1021\/bi802046n","article-title":"Structural characterization of a soluble amyloid b-peptide oligomer","volume":"48","author":"Yu","year":"2009","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"18340","DOI":"10.1021\/jacs.3c03980","article-title":"A hairpin motif in the amyloid-b peptide is important for formation of disease-related oligomers","volume":"145","author":"Khaled","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4757","DOI":"10.1021\/acschemneuro.9b00516","article-title":"Catalytic prion-like cross-talk between a key Alzheimer\u2019s disease tau-fragment R3 and the type 2 diabetes peptide IAPP","volume":"10","author":"Arya","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/S1074-7613(00)00043-1","article-title":"Inhibition of amyloid fiber assembly by both BiP and its target peptide","volume":"13","author":"Davis","year":"2000","journal-title":"Immunity"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1002\/pro.5560040309","article-title":"Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins","volume":"4","author":"Stevens","year":"1995","journal-title":"Protein Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1110\/ps.8.3.509","article-title":"Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains","volume":"8","author":"Raffen","year":"1999","journal-title":"Protein Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"12657","DOI":"10.1074\/jbc.M109230200","article-title":"Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH","volume":"277","author":"Souillac","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3109\/13506120309041731","article-title":"A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding","volume":"10","author":"Khurana","year":"2003","journal-title":"Amyloid"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1006\/jsbi.2000.4248","article-title":"Review: Immunoglobulin light chain amyloidosis--the archetype of structural and pathogenic variability","volume":"130","author":"Bellotti","year":"2000","journal-title":"J. Struct. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1291","DOI":"10.1016\/S0161-5890(98)00002-9","article-title":"Variable domain structure of kappaIV human light chain Len: High homology to the murine light chain McPC603","volume":"34","author":"Huang","year":"1997","journal-title":"Mol. Immunol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4227","DOI":"10.1002\/anie.201309001","article-title":"Sequestration of a b-hairpin for control of a-synuclein aggregation","volume":"53","author":"Mirecka","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"12781","DOI":"10.1021\/acs.jpcb.6b08485","article-title":"Uncovering the binding and specificity of b-wrapins for amyloid-b and a-synuclein","volume":"120","author":"Orr","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1002\/cbic.201402552","article-title":"A b-hairpin-binding protein for three different disease-related amyloidogenic proteins","volume":"16","author":"Shaykhalishahi","year":"2015","journal-title":"ChemBioChem"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.compchemeng.2018.02.013","article-title":"Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of b-wrapins","volume":"116","author":"Orr","year":"2018","journal-title":"Comput. Chem. Eng."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"W\u00f6rdehoff, M.M., and Hoyer, W. (2018). a-Synuclein aggregation monitored by Thioflavin T fluorescence assay. Bio Protoc., 8.","DOI":"10.21769\/BioProtoc.2941"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.ab.2010.02.001","article-title":"Strategies to increase the reproducibility of protein fibrillization in plate reader assays","volume":"400","author":"Giehm","year":"2010","journal-title":"Anal. Biochem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"7671","DOI":"10.1073\/pnas.1315346111","article-title":"Solution conditions determine the relative importance of nucleation and growth processes in a-synuclein aggregation","volume":"111","author":"Buell","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3235","DOI":"10.1074\/jbc.M208249200","article-title":"Cellular polyamines promote the aggregation of a-synuclein","volume":"278","author":"Antony","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"3018","DOI":"10.1016\/j.jmb.2017.09.005","article-title":"Opposed Effects of Dityrosine Formation in Soluble and Aggregated alpha-Synuclein on Fibril Growth","volume":"429","author":"Wordehoff","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1002\/prot.20449","article-title":"The CCPN data model for NMR spectroscopy: Development of a software pipeline","volume":"59","author":"Vranken","year":"2005","journal-title":"Proteins"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"e46112","DOI":"10.7554\/eLife.46112","article-title":"An engineered monomer binding-protein for a-synuclein efficiently inhibits the proliferation of amyloid fibrils","volume":"8","author":"Agerschou","year":"2019","journal-title":"eLife"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/22\/16132\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:20:14Z","timestamp":1760131214000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/22\/16132"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11,9]]},"references-count":66,"journal-issue":{"issue":"22","published-online":{"date-parts":[[2023,11]]}},"alternative-id":["ijms242216132"],"URL":"https:\/\/doi.org\/10.3390\/ijms242216132","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,11,9]]}}}