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.

膜蛋白是许多生理和病理过程的关键。他们的研究通常涉及预先的洗涤剂溶解步骤，该步骤会剥离膜并可能危及膜蛋白的完整性。最近的洗涤剂替代品包括基于马来酸的共聚物 (xMAs)，它会破坏脂质双层并形成可溶于水性缓冲液的脂质蛋白纳米圆盘 (xMALPs)。尽管 xMALP 通常被称为原生纳米圆盘，但人们对其脂质和蛋白质含量与原生双层的相似性知之甚少。在这里，我们使用脂质组学和凝胶内分析分析了原核和真核 xMALP。我们的结果表明 xMALPs 含量随所用 xMA 的化学性质而变化。