Privé Gilbert G
Ontario Cancer Institute, 101 College Street, Toronto, Ontario, Canada M5G 1L7.
Curr Opin Struct Biol. 2009 Aug;19(4):379-85. doi: 10.1016/j.sbi.2009.07.008. Epub 2009 Aug 12.
An ideal detergent would be able to maintain a membrane protein in a soluble state with no measurable effect on the functional, structural, and thermodynamic properties of the protein relative to the bilayer-embedded state. Unfortunately, the detergents that are commonly used by membrane protein biochemists fall short of this standard. Although remarkable advances have been made in membrane protein structural biology, there remains a need for improved detergents that provide a more natural substitute for the membrane environment. Lipopeptide detergents (LPDs) are a new class of amphiphile designed to be better mimics of the bilayer at the hydrophobic surfaces of solubilized membrane proteins. LPDs consist of an alpha-helical peptide backbone that supports alkyl chains anchored at either end of the helix. The LPD monomers self-assemble into cylindrical micelles with a membrane-like packing of the inner core of alkyl chains.
理想的去污剂应能使膜蛋白保持可溶状态，且相对于嵌入双层膜的状态，对蛋白的功能、结构和热力学性质没有可测量的影响。不幸的是，膜蛋白生物化学家常用的去污剂未达到这一标准。尽管膜蛋白结构生物学已取得显著进展，但仍需要改进去污剂，以便为膜环境提供更天然的替代物。脂肽去污剂（LPD）是一类新型两亲分子，旨在更好地模拟溶解的膜蛋白疏水表面的双层膜。LPD由一个α-螺旋肽主链组成，该主链支撑着锚定在螺旋两端的烷基链。LPD单体自组装成圆柱形胶束，其烷基链内核具有类似膜的堆积方式。
