Extended Data Fig. 6: LUVs and the chaperone SecB compete for α-synuclein binding.
From: Regulation of α-synuclein by chaperones in mammalian cells
a, Residue-resolved backbone amide NMR signal attenuation (Irel = I/I0) of α-synuclein caused by the addition of 5 mg ml−1 LUVs (125:1 molar ratio of lipid:protein; dark yellow) and after further addition of 2 equivalents of SecB (yellow). b, Residue-resolved backbone amide NMR signal attenuation (Irel = I/I0) of α-synuclein caused by the addition of 15 mg ml−1 LUVs (375:1 molar ratio lipid:protein; dark yellow) and after further addition of 2 and 6 equivalents of SecB, respectively (yellow), measured at 298 K. c, Residue-resolved backbone amide NMR signal attenuation (Irel = I/I0) of α-synuclein caused by the addition of 2 equivalents of SecB (yellow) and increasing amounts of LUVs with the following ratios: 2.5 mg ml−1, 62.5:1; 4.0 mg ml−1, 100:1; 6.25 mg ml−1, 156:1; 8.5 mg ml−1, 212.5:1. d, Schematic showing the conformational equilibrium of free α-synuclein, its chaperone-bound state and one possible conformation of its LUV-bound state (PDB 1XQ8)19. Notably, these observations are also in full agreement with related studies for HSP9012 and HSP2737. e, Dynamic light scattering (DLS) measurements of LUVs prepared from pig brain polar lipids. Two independent preparations are shown in blue and orange, respectively, with an average diameter of 110 nm.
