Extended Data Fig. 7: CD binding assays of αSyn WT, ΔΔ and P1P2- GS to DMPS LUVs.
From: A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function
a, Far-UV CD spectra of 25 μM WT αSyn (blue) or ΔΔ (red) incubated in the absence or presence of liposomes (100:1 (M/M) DMPS:αSyn). b, Change of CD signal of WT αSyn (blue), ΔΔ (red) or P1P2-GS (orange) at 220 nm as a function of [DMPS]/[αSyn] ratio. Data were fitted (solid lines) to a single-step binding model, yielding the affinity (KD) and stoichiometry value (L, the number of DMPS molecules in the bilayer that are involved in binding to one molecule of αSyn). c, Far-UV CD spectra of 25 μM WT αSyn (blue) or P1P2-GS (orange) incubated in the absence or presence of 100 times molar excess of DMPS LUVs. d, Dynamic light scattering of DMPS liposomes showing they have a hydrodynamic radius (Rh) of on 81 nm. Data for graphs in a,c,d are available as Source data.
