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Parkinson\u2019s disease and dementia with Lewy bodies can be characterized as synucleinopathies due to the abnormal accumulation of the protein alpha-synuclein (\u03b1-Syn). Studies have shown amyloidogenic proteins such as \u03b1-Syn and tau can exist as polymorphic aggregates, a theory widely studied mostly in their fibrillar morphology. It is now well understood that an intermediate state of aggregates, oligomers, are the most toxic species. We have shown \u03b1-Syn, when modified by different physiological inducers, result in distinct oligomeric conformations of \u03b1-Syn. Polymorphic \u03b1-Syn oligomers exhibit distinct properties such as aggregate size, conformation, and differentially interact with tau. In this study, we confirm \u03b1-Syn oligomeric polymorphs furthermore using in-house novel \u03b1-Syn toxic conformation monoclonal antibodies (SynTCs). It is unclear the biological relevance of \u03b1-Syn oligomeric polymorphisms. Utilizing a combination of biochemical, biophysical, and cell-based assays, we characterize \u03b1-Syn oligomeric polymorphs. We found \u03b1-Syn oligomeric polymorphs exhibit distinct immunoreactivity and SynTCs exhibit differential selectivity and binding affinity for \u03b1-Syn species. Isothermal titration calorimetry experiments suggest distinct \u03b1-Syn:SynTC binding enthalpies in a species-specific manner. Additionally, we found SynTCs differentially reduce \u03b1-Syn oligomeric polymorph-mediated neurotoxicity and propagation in primary cortical neurons in a polymorph-specific manner. These studies demonstrate the biological significance of polymorphic \u03b1-Syn oligomers along with the importance of polymorph-specific antibodies that target toxic \u03b1-Syn aggregates. Monoclonal antibodies that can target the conformational heterogeneity of \u03b1-Syn oligomeric species and reduce their mediated toxicity have promising immunotherapeutic potential.<\/jats:p>","DOI":"10.1007\/s12035-023-03211-3","type":"journal-article","created":{"date-parts":[[2023,1,28]],"date-time":"2023-01-28T03:37:52Z","timestamp":1674877072000},"page":"2691-2705","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Polymorphic Alpha-Synuclein Oligomers: Characterization and Differential Detection with Novel Corresponding Antibodies"],"prefix":"10.1007","volume":"60","author":[{"given":"Kenya","family":"Moore","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Urmi","family":"Sengupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicha","family":"Puangmalai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nemil","family":"Bhatt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6216-8640","authenticated-orcid":false,"given":"Rakez","family":"Kayed","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2023,1,28]]},"reference":[{"key":"3211_CR1","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.3389\/fnins.2019.01399","volume":"13","author":"LD Bernal-Conde","year":"2020","unstructured":"Bernal-Conde LD et al (2020) Alpha-synuclein physiology and pathology: a perspective on cellular structures and organelles. 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The other authors declare no competing interests.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}]}}