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. 2021 Oct 6;11(10):1466. doi: 10.3390/biom11101466

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Proposed mechanism for DJ-1’s impact on ac-αSyn glycation. (Left) Glyc-ac-αSyn spontaneously forms oligomers that are in equilibrium with glyc-ac-αSyn monomers. Glyc-ac-αSyn does not form amyloid fibrils, although the oligomers have been shown to be harmful to neurons. (Right) Upon addition of DJ-1, DJ-1 scavenges glyc-ac-αSyn oligomers, preventing their interactions with glyc-ac-αSyn monomers. This allows glyc-ac-αSyn monomers to be free in solution. Removal of DJ-1 from the system restores the glyc-ac-αSyn monomer–oligomer interactions.