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Transl. Med."],"published-print":{"date-parts":[[2026,4,1]]},"abstract":"<jats:p>\n                    Synucleinopathies is an umbrella term for multiple neurological disorders, including Parkinson\u2019s disease (PD), Lewy body dementia (LBD), and multiple system atrophy (MSA). A central pathological hallmark of synucleinopathies is the aggregation of \u03b1-synuclein (\u03b1S, a neuronal protein) and its prion-like spread. Therefore, inhibition of \u03b1S aggregation and spread is considered a viable therapeutic approach for the treatment of synucleinopathies. Foldamers are synthetic ligands that mimic the secondary structure of proteins. Using an oligoquinoline (OQ) scaffold\u2013based foldamer approach, we have previously identified a foldamer (SK-129) that potently inhibits \u03b1S aggregation. Here, using a wide range of biophysical, cellular, and in vivo methods, we showed that SK-129 rescued synucleinopathy phenotypes in cellular,\n                    <jats:italic toggle=\"yes\">Caenorhabditis elegans<\/jats:italic>\n                    , and human induced pluripotent stem cell (iPSC)\u2013derived neuron models. SK-129 specifically bound to neurotoxic \u03b1S oligomers with ~6-fold higher affinity (\n                    <jats:italic toggle=\"yes\">K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    \u00a0= 221\u00a0\u00b1\u00a029 nM) than to physiological \u03b1S monomer, validating \u03b1S oligomers as a therapeutic target. Furthermore, SK-129 efficiently crossed the blood-brain barrier (BBB) and exhibited favorable pharmaceutical properties in mice. Treatment with SK-129 prevented brain histopathology and increased survival in a mouse model expressing human A53T mutant \u03b1S without showing any apparent cytotoxicity. SK-129 inhibited \u03b1S aggregation mediated by exosomes derived from\n                    <jats:italic toggle=\"yes\">C. elegans<\/jats:italic>\n                    or patients with PD in HEK293T reporter cells. SK-129 completely inhibited the coaggregation of \u03b1S-tau, a pathological biomarker for LBD in both cellular and mouse models. Overall, we report a potent foldamer with therapeutic potential for PD and LBD.\n                  <\/jats:p>","DOI":"10.1126\/scitranslmed.adu1050","type":"journal-article","created":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T17:58:19Z","timestamp":1775066299000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":4,"title":["Foldamers rescue synucleinopathy phenotypes in multiple in vitro and in vivo models"],"prefix":"10.1126","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0190-8665","authenticated-orcid":true,"given":"Ryan A.","family":"Dohoney","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, F. W. Olin Hall, 2190 E. Iliff Ave., University of Denver, Denver, CO 80210, USA."},{"name":"Knoebel Institute for Healthy Aging, 2155 E. 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