Nanoparticles and photochemistry for native-like transmembrane protein footprinting

Jie Sun, Xiaoran Roger Liu, Shuang Li, Peng He, Weikai Li () and Michael L. Gross ()
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Jie Sun: Washington University in St. Louis
Xiaoran Roger Liu: Washington University in St. Louis
Shuang Li: Washington University School of Medicine
Peng He: Washington University School of Medicine
Weikai Li: Washington University School of Medicine
Michael L. Gross: Washington University in St. Louis

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Mass spectrometry-based footprinting can probe higher order structure of soluble proteins in their native states and serve as a complement to high-resolution approaches. Traditional footprinting approaches, however, are hampered for integral membrane proteins because their transmembrane regions are not accessible to solvent, and they contain hydrophobic residues that are generally unreactive with most chemical reagents. To address this limitation, we bond photocatalytic titanium dioxide (TiO2) nanoparticles to a lipid bilayer. Upon laser irradiation, the nanoparticles produce local concentrations of radicals that penetrate the lipid layer, which is made permeable by a simultaneous laser-initiated Paternò–Büchi reaction. This approach achieves footprinting for integral membrane proteins in liposomes, helps locate both ligand-binding residues in a transporter and ligand-induced conformational changes, and reveals structural aspects of proteins at the flexible unbound state. Overall, this approach proves effective in intramembrane footprinting and forges a connection between material science and biology.

Date: 2021
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DOI: 10.1038/s41467-021-27588-8

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