B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles

A label-free approach for measuring interactions of proteins with lipid membranes

“…In their manuscript in this issue of Cell Reports Methods , Sadi and colleagues 10 developed an alternative method, binding to lipid vesicles (B2LiVe), for determination of partitioning of amphitrophic proteins to lipid membranes. The nuclear magnetic resonance (NMR)-based approach involves selective excitation of amide resonances of proteins, which avoids interference from other components in the experimental system.…”

“…Here, data for apo-myoglobin are shown from Sadi et al. 10 (C) To determine affinity constants, the fraction of membrane-bound proteins, derived from data in (B), were plotted against lipid concentration. The binding curves are shown for apo-Mb (cyan), translocation domain of diptheria toxin (violet), and pore-forming toxin anthrolysin O (green).…”

“…The binding curves are shown for apo-Mb (cyan), translocation domain of diptheria toxin (violet), and pore-forming toxin anthrolysin O (green). 10 (A) was created with BioRender ( https://biorender.com/ ). …”