Oxidized EGCG redirects α-synuclein aggregation through shear-selected interactions

Oxidized EGCG (oxEGCG) binds α-synuclein and inhibits fibrillation, while shear flow partially reverts oxEGCG-driven changes but preferentially retains interactions near the NAC–C-terminal boundary.

• Why it matters: It remains unclear whether EGCG’s anti-aggregation effects come from EGCG itself or from oxidized species, and which molecular interactions persist during α-synuclein assembly under flow.
• What they did: Using HPLC, LC-MS, TEM, and solution NMR, the study compared unoxidized EGCG versus oxEGCG, and used Rheo-NMR to track α-synuclein during shear-promoted assembly.
• The result: oxEGCG-dependent perturbations partially reverted toward free α-synuclein under shear, while NAC–C-terminal boundary interactions were preferentially retained, coinciding with oligomer formation and short, thick fibrils.

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