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Current \u03b1syn biomarkers are limited to binary detection of pathogenic \u03b1syn in peripheral tissue biopsies or fluids, limiting differential diagnosis. Hence, there is an urgent need for methods that allow strain-specific detection and characterization of \u03b1syn strain architecture. Notably, luminescent conjugated oligothiophenes (LCOs) have been successfully used to detect distinct protein strain conformers in prion diseases and Alzheimer\u2019s disease, highlighting their utility in differentiating disease-specific amyloid structures. Species-dependent differences in \u03b1syn structure are increasingly recognized as one of the critical aspects that shape how fibrils form, propagate and interact with molecular LCO probes. Here, we evaluate the potential of the LCO h-FTAA to differentiate species-specific \u03b1syn strains and conduct a translational investigation using peripheral cardiac tissue of a gut-first synucleinopathy rodent model. Our in vitro data demonstrate strain-specific probe\u2013fibril interactions, reflecting a differential strain architecture and cellular micro-environment. While h-FTAA binds with comparable efficiency to mouse (mo-) and human (hu-) pre-formed fibrils (PFFs), h-FTAA exhibits markedly lower quantum yield when bound to moPFFs versus huPFFs. Spectral imaging revealed h-FTAA-moPFF binding produces blue-shifted maxima (505\u2013550 nm), contrasting with the red-shifted maxima (545\u2013580 nm) of huPFFs. Fluorescence lifetime imaging microscopy confirmed h-FTAA\u2019s intrinsic sensitivity to species-dependent variations through distinct temporal fluorescence signatures (moPFFs: ~0.60\u20131.5 ns vs. huPFFs: ~0.65\u20131.0 ns). Our translational investigation showed h-FTAA binding to peripheral cardiac pathology exhibits comparable red-shifted emission, but distinct fluorescence lifetimes of h-FTAA-bound aggregates in moPFF-injected (~1.0\u20131.4 ns) versus huPFF-injected (~0.69\u20130.8 ns) rats. Interestingly, we observed distinct blue-shifted emission profiles in a few selected regions of the heart of moPFF-injected rodents, further characterized by extra-long fluorescence decay shifts (~1.5\u20131.9 ns), reflecting differences in both aggregate conformation and maturity in moPFF-induced compared with huPFF-induced rats. Taken together, our findings underscore the potential of LCO ligands, like h-FTAA, to enable more precise disease staging and diagnosis through peripheral biopsies, complementing existing \u03b1syn biomarker methods.<\/jats:p>","DOI":"10.3390\/ijms27093807","type":"journal-article","created":{"date-parts":[[2026,4,24]],"date-time":"2026-04-24T14:28:23Z","timestamp":1777040903000},"page":"3807","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Human and Mouse Alpha-Synuclein Fibrillation: Impact on h-FTAA Binding and Advancing Strain-Specific Biomarkers in PD Animal Models"],"prefix":"10.3390","volume":"27","author":[{"given":"Priyanka","family":"Swaminathan","sequence":"first","affiliation":[{"name":"Department of Physics, Faculty of Natural Sciences, Norwegian University of Science and Technology (NTNU), Gl\u00f8shaugen, Realfagbygget, NO-7491 Trondheim, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vasileios","family":"Theologidis","sequence":"additional","affiliation":[{"name":"Department of Clinical Medicine\u2014Core Center for Molecular Morphology, Section for Stereology and Microscopy, Aarhus University, 8000 Aarhus, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hjalte","family":"Gram","sequence":"additional","affiliation":[{"name":"Danish Research Institute of Translational Neuroscience (DANDRITE), Department of Biomedicine, Aarhus University, 8000 Aarhus, Denmark"},{"name":"PACE\u2014Lundbeck Foundation Parkinson\u2019s Disease Research Center, Aarhus University Hospital, 8200 Aarhus, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8153-8651","authenticated-orcid":false,"given":"Debdeep","family":"Chatterjee","sequence":"additional","affiliation":[{"name":"Department of Physics, Chemistry and Biology, Link\u00f6ping University, SE-581 83 Link\u00f6ping, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5827-3587","authenticated-orcid":false,"given":"Per","family":"Hammarstr\u00f6m","sequence":"additional","affiliation":[{"name":"Department of Physics, Chemistry and Biology, Link\u00f6ping University, SE-581 83 Link\u00f6ping, Sweden"},{"name":"Science for Life Laboratory, Link\u00f6ping University, SE-581 83 Link\u00f6ping, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9384-1279","authenticated-orcid":false,"given":"Nathalie","family":"Van Den Berge","sequence":"additional","affiliation":[{"name":"Department of Clinical Medicine\u2014Core Center for Molecular Morphology, Section for Stereology and Microscopy, Aarhus University, 8000 Aarhus, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6649-7871","authenticated-orcid":false,"given":"Mikael","family":"Lindgren","sequence":"additional","affiliation":[{"name":"Department of Physics, Faculty of Natural Sciences, Norwegian University of Science and Technology (NTNU), Gl\u00f8shaugen, Realfagbygget, NO-7491 Trondheim, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,4,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"19509","DOI":"10.1074\/jbc.274.28.19509","article-title":"\u03b1-Synuclein Fibrillogenesis Is Nucleation-dependent: Implications for the pathogenesis of Parkinson\u2019s disease","volume":"274","author":"Wood","year":"1999","journal-title":"J. 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