Journal: Cell Reports Methods
Article Title: B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles
doi: 10.1016/j.crmeth.2023.100624
Figure Lengend Snippet: Membrane partitioning of the P233 and P414 peptides followed by 1D- 1 H NMR, tryptophan fluorescence, and far-UV CD (A–D) The experiments were performed in the presence of POPC:POPG:chol 7:2:1 SUV. Data for P233 and P414 as a function of lipid concentration are displayed in magenta and blue, respectively. Membrane partitioning followed by 1D- 1 H NMR is represented on a linear scale (A) and on a logarithmic scale (B). The ratio of tryptophan fluorescence intensity (320 nm/370 nm) (C) and the ellipticity at 222 ± 2 nm in the far-UV region (D) as a function of lipid concentration are shown. Error bars in (A and B) are calculated from the standard deviation of noise in 1D-NMR spectra. The signal loss in (A) and (B) of the tryptophan indol proton (open circles) followed by NMR is similar to that of the amide envelope (closed circles). Data in (C and D) are mean ± SEM.
Article Snippet: The P414 peptide , Genosphere Biotechnologies , P414.
Techniques: Membrane, Fluorescence, Concentration Assay, Standard Deviation