An advantageous alternative to the use of detergents in biochemical studies on membrane proteins are the recently developed styrene-maleic acid (SMA) amphipathic copolymers. In our recent study [1] we demonstrated that using this approach, most T cell membrane proteins were fully solubilized (presumably in small nanodiscs), while two types of raft proteins, GPI-anchored proteins and Src family kinases, were mostly present in much larger (>250 nm) membrane fragments markedly enriched in typical raft lipids, cholesterol and lipids containing saturated fatty acid residues. In the present study we demonstrate that disintegration of membranes of several other cell types by means of SMA copolymer follows a similar pattern and we provide a detailed proteomic and lipidomic characterization of these SMA-resistant membrane fragments (SRMs).

Institute of Molecular Genetics of the Czech Academy of Sciences Vídeňská 1083 142 20 Praha 4 Czechia

Institute of Physiology of the Czech Academy of Sciences Vídeňská 1083 142 20 Praha 4 Czechia

Proteomics Core Facility Faculty of Science Charles University BIOCEV Prumyslova 595 Vestec CZ 25242 Czechia; Institute for Environmental Studies Faculty of Science Charles University Benatska 2 Prague 2 CZ 128 01 Czechia

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Novel class of peptides disintegrating biological membranes to aid in the characterization of membrane proteins

Sulfonated polystyrenes: pH and Mg2+-insensitive amphiphilic copolymers for detergent-free membrane protein isolation