Design and Synthesis of Hetero-Bicephalic Detergents for Native Mass Spectrometry of Membrane Proteins.

ABSTRACT: Native mass spectrometry is playing a central role in characterizing the noncovalent interactions of membrane proteins, enabling the discovery of lipids that regulate membrane protein function and modulate interactions with other molecules. The use of specialized charge-reducing detergents and/or molecular additives is critical to mitigate overactivation during native MS to facilitate proper analysis. Here, we present the design and synthesis of a new class of dual-headgroup detergents featuring two distinct hydrophilic moieties. One headgroup, the spermine moiety, is designed to promote lower charge states of membrane proteins, thereby enhancing the preservation of labile complexes in the mass spectrometer. The other hydrophilic headgroup─either a maltoside or a tetraethylene glycol moiet

SUBMITTER: Chang JY 

PROVIDER: S-EPMC12327940 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature