Styrene-maleic acid copolymers (SMAs) have been shown to effectively extract membrane proteins while retaining the protein’s native conformation by forming nanodiscs containing an annulus of the membrane’s native lipids. Recent reports have shown that the esterification of SMA copolymers with various sidechains can drastically alter the efficiency and selectivity of protein extraction. However, much remains unknown on how and why the extent of SMA functionalization and identity of the sidechain alters the protein solubilization process. To probe these relationships, we investigated how a systematic series of monoesterified SMA copolymers bearing hydrophobic alkoxy ethoxylate sidechains of increasing lengths impacts the extraction of trimeric Photosystem I from membranes of the cyanobacterium <i>Thermosynechococcus elongatus. </i> We found that as the length and hydrophobicity of the sidechain, as well as the degree of functionalization, increase Photosystem I is more efficiently extracted. Finally, we demonstrated that the method of copolymer synthesis, solubilization, and storage employed may dramatically impact the structure of the copolymer, and consequently, the efficiency of the protein extraction process.

Esterified sytrene-maleic acid copolymers for the efficient and selective extraction of integral membrane proteins

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