Dataset Information

Native Mass Spectrometry of Soluble Proteins with Sodium Chloride enabled by a Dendritic Detergent

ABSTRACT: Salts are pivotal for ligand binding but hamper the analysis of proteins through native mass spectrometry due to adduct formation and consequent signal suppression. Here, we show how to facilitate native mass spectrometry of soluble proteins and protein–ligand complexes in the presence of sodium chloride by means of the dendritic detergent [G1]. Adding this detergent to samples prior electrospray ionization enables high-quality mass spectra of proteins and complexes with ligands such as cofactors and lipids in sodium chloride-containing solutions. Nuclear magnetic resonance spectroscopy indicates concentration-dependent salt complexation by the detergent in solution, which liberates desalted protein ions to the gas phase. Our findings add to the growing repertoire of methods that enable investigations with mass spectrometry under more physiological biochemical conditions. The ease of this method will widely facilitate native mass spectrometry of soluble protein samples that necessitate the presence of salt in solutions.

INSTRUMENT(S):

ORGANISM(S): Equus Caballus (horse) Bos Taurus (bovine) Oryctolagus Cuniculus (rabbit) Pseudomonas Aeruginosa Pao1 Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Skeletal Muscle Cell, Blood Serum

SUBMITTER: Francesco Fiorentino