Damian Marjorie, Perino Sandrine, Polidori Ange, Martin Aimée, Serre Laurence, Pucci Bernard, Banères Jean-Louis
Institut des Biomolécules Max Mousseron, UMR 5247 CNRS-Universités Montpellier I et II, Faculté de Pharmacie, 15 Av. Ch. Flahault, BP 14491, 34093 Montpellier Cedex 5, France.
FEBS Lett. 2007 May 15;581(10):1944-50. doi: 10.1016/j.febslet.2007.03.091. Epub 2007 Apr 9.
Structural characterization of membrane proteins is hampered by the instability of the isolated proteins in detergent solutions. Here, we describe a new class of phospholipid-like surfactants that stabilize the G protein-coupled receptor, BLT1. These compounds, called C(13)U(9), C(13)U(19), C(15)U(25) and C(17)U(16), were synthesized by radical polymerization of Tris(hydroxymethyl) acrylamidomethane in the presence of thioglycerol, first endowed with two hydrocarbon chains with variable lengths (13-17 carbon atoms), as transfer reagent. C(13)U(19), C(17)U(16) or C(15)U(25) significantly enhanced the stability of BLT1 in solution compared to what was obtained with common detergents. These molecules therefore represent a promising step towards the structural characterization of BLT1 and possibly other membrane proteins.
膜蛋白的结构表征受到其在去污剂溶液中分离时的不稳定性的阻碍。在此，我们描述了一类新型的类磷脂表面活性剂，它们能够稳定G蛋白偶联受体BLT1。这些化合物，称为C(13)U(9)、C(13)U(19)、C(15)U(25)和C(17)U(16)，是通过在硫代甘油存在下，由三（羟甲基）丙烯酰胺甲烷进行自由基聚合反应合成的，首先赋予两条长度可变的烃链（13 - 17个碳原子）作为转移试剂。与使用普通去污剂相比，C(13)U(19)、C(17)U(16)或C(15)U(25)显著提高了BLT1在溶液中的稳定性。因此，这些分子代表了朝着BLT1以及可能其他膜蛋白的结构表征迈出的有希望的一步。
