Abstract
Membrane proteins are key in a large number of physiological and pathological processes. Their study often involves a prior detergent solubilization step, which strips away the membrane and can jeopardize membrane protein integrity. A recent alternative to detergents encompasses maleic acid based copolymers (xMAs), which disrupt the lipid bilayer and form lipid protein nanodiscs (xMALPs) soluble in aqueous buffer. Although xMALPs are often referred to as native nanodiscs, little is known about the resemblance of their lipid and protein content to the native bilayer. Here we have analyzed prokaryotic and eukaryotic xMALPs using lipidomics and in-gel analysis. Our results show that the xMALPs content varies with the chemical properties of the used xMA.
Highlights
Membrane proteins are key in a large number of physiological and pathological processes
In order to compare the effect of the styrene versus maleic acid ratio, we chose for styrene maleic acid (SMA) with ratios 3:1 and 2.3:1
styrene maleimide quaternary ammonium (SMA-QA) is compatible with low pH9, whereas solubilization by diisobutylene maleic acid (DIBMA) is stimulated by higher pH10
Summary
Membrane proteins are key in a large number of physiological and pathological processes. A recent alternative to detergents encompasses maleic acid based copolymers (xMAs), which disrupt the lipid bilayer and form lipid protein nanodiscs (xMALPs) soluble in aqueous buffer. In addition to SMA, several other maleic acid copolymers (xMAs) have been synthesized as nanodisc-forming agents (Fig. 1) These new xMAs have improved chemical properties or incorporate chemical modifications that broaden the downstream applications of xMA lipid protein nanodiscs (xMALPs). Diisobutylene maleic acid (DIBMA) has aliphatic alkyl chains instead of aromatic groups, avoiding ultraviolet (UV) absorption and allowing the use of optical spectroscopic techniques such as circular dichroism Another example is SMA-SH4, the structure of which contains thiol groups that can act as chemical handles for reaction with fluorophores or other functional moieties. They enabled the structure determination of the alternative complex III by cryogenic electron microscopy[5] and the elucidation of naturally occurring oligomeric states of various MPs6
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