Fig. 1: Transient residue-resolved interaction of mitochondria with αSyn. | Nature Communications

Fig. 1: Transient residue-resolved interaction of mitochondria with αSyn.

From: Alpha-synuclein interacts with regulators of ATP homeostasis in mitochondria

Fig. 1

Comparison between the chemical shift perturbations and intensity changes of αSyn caused by interaction with either lysed bovine mitochondria (green) or cardiolipin nanodiscs (blue). The data is presented as a rolling average of three points. Peak positions and peak intensities are extracted from 2D [15N,1H] HMQC NMR spectra. a Intensity ratios of peaks in the presence (I) and absence (I0) of nanodiscs or lysed bovine brain mitochondria. b Chemical shift perturbations (CSPs) of peaks in the presence and absence of nanodiscs or lysed bovine brain mitochondria. a, b The interaction with lipid membrane nanodiscs appears to influence the N-terminal region of αSyn, indicating an interaction between the positively charged N-terminal segment of αSyn with the negatively charged cardiolipin, as expected10, with the second half of the sequence showing no changes. The interaction with mitochondria causes relevant changes in all regions of the sequence, indicating multiple transient interactions that may include membrane interactions. Source data are provided as a Source Data file.

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