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. 2021 Feb 10;12:927. doi: 10.1038/s41467-021-21027-4

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Binding curves of αS to OPM-GMs SUVs monitored via the signal attenuation of the peaks in the ¹H-¹⁵N-HSQC spectra of αS (50 μM) as a function of the concentration of SUVs. The signal attenuations have been averaged over the individual residues of the N-terminal region (black) and the region spanning residues 65–97 (red), and error bars report the standard deviation of these values. The resulting K_D values are 424.5 μM (L = 17.5) and 3945 μM (L = 3.8) for the N-terminal region and the region spanning residues 65–97, respectively. b NMR CEST profiles along the sequence measured using a saturation bandwidth of 350 Hz (Fig. S5 for measurements performed with a bandwidth of 170 Hz) for the interaction between αS and OPM-GMs. Black, orange and green lines refer to the averaged CEST profiles measured using offsets at ±1.5, ±3.0, and ±5.0 kHz, respectively. Error bars report the standard deviation estimated on the triplicate measurements. C Interaction between αS and IPM-GMs (see (a) for details). The resulting binding affinities are 5.8 μM (L = 12.2) and 16.0 μM (L = 34.5) for the N terminus and the region 65–97, respectively. d NMR CEST analysis of the interaction between αS and IPM-GMs measured using a saturation bandwidth of 350 Hz (Fig. S5 for measurements performed with a bandwidth of 170 Hz). Details as in b. Error bars report the standard deviation estimated on the triplicate measurements. e Statistical analysis of the number of docked vesicles on IPM-GM surfaces (filled bars) imaged in the focal plane at different concentrations of αS and constant concentration of SUVs (2 μM). For comparison, data measured using IPM are reported with striped bars. The symbols § and §§, indicate p values of 0.028 and 0.0005, respectively, calculated with the unpaired t test using Welch’s correction. Error bars report the standard deviation estimated on the triplicate measurements. f Residence times of docked vesicles on the IPM-GM surfaces (filled bars) at different concentrations of αS and constant concentration of SUVs (2 μM). For comparison, data measured using IPM are reported with striped bars. The symbols ** and ***, indicate p values of 0.02 and 0.03, respectively, calculated with the unpaired t test using Welch’s correction. Error bars report the standard deviation estimated on the triplicate measurements.