Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning

dc.contributor.authorHorne, Robert I.
dc.contributor.authorAndrzejewska, Ewa A.
dc.contributor.authorAlam, Parvez
dc.contributor.authorBrotzakis, Z. Faidon
dc.contributor.authorSrivastava, Ankit
dc.contributor.authorAubert, Alice
dc.contributor.authorNowinska, Magdalena
dc.contributor.authorGregory, Rebecca C.
dc.contributor.authorStaats, Roxine
dc.contributor.authorPossenti, Andrea
dc.contributor.authorChia, Sean
dc.contributor.authorSormanni, Pietro
dc.contributor.authorGhetti, Bernardino
dc.contributor.authorCaughey, Byron
dc.contributor.authorKnowles, Tuomas P. J.
dc.contributor.authorVendruscolo, Michele
dc.contributor.departmentPathology and Laboratory Medicine, School of Medicine
dc.date.accessioned2024-08-03T07:30:51Z
dc.date.available2024-08-03T07:30:51Z
dc.date.issued2024
dc.description.abstractMachine learning methods hold the promise to reduce the costs and the failure rates of conventional drug discovery pipelines. This issue is especially pressing for neurodegenerative diseases, where the development of disease-modifying drugs has been particularly challenging. To address this problem, we describe here a machine learning approach to identify small molecule inhibitors of α-synuclein aggregation, a process implicated in Parkinson's disease and other synucleinopathies. Because the proliferation of α-synuclein aggregates takes place through autocatalytic secondary nucleation, we aim to identify compounds that bind the catalytic sites on the surface of the aggregates. To achieve this goal, we use structure-based machine learning in an iterative manner to first identify and then progressively optimize secondary nucleation inhibitors. Our results demonstrate that this approach leads to the facile identification of compounds two orders of magnitude more potent than previously reported ones.
dc.eprint.versionFinal published version
dc.identifier.citationHorne RI, Andrzejewska EA, Alam P, et al. Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning. Nat Chem Biol. 2024;20(5):634-645. doi:10.1038/s41589-024-01580-x
dc.identifier.urihttps://hdl.handle.net/1805/42586
dc.language.isoen_US
dc.publisherSpringer Nature
dc.relation.isversionof10.1038/s41589-024-01580-x
dc.relation.journalNature Chemical Biology
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourcePMC
dc.subjectDrug discovery
dc.subjectParkinson disease
dc.subjectSmall molecule libraries
dc.subjectProtein aggregates
dc.titleDiscovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
dc.typeArticle
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