Bolanos-Garcia Victor Martin, Renault Anne, Beaufils Sylvie
Department of Biochemistry, University of Cambridge, Cambridge CB2 1TN, United Kingdom.
Biophys J. 2008 Mar 1;94(5):1735-45. doi: 10.1529/biophysj.107.115220. Epub 2007 Nov 9.
Exchangeable apolipoproteins are located in the surface of lipoprotein particles and regulate lipid metabolism through direct protein-protein and protein-lipid interactions. These proteins are characterized by the presence of tandem repeats of amphiphatic alpha-helix segments and a high surface activity in monolayers and lipoprotein surfaces. A noteworthy aspect in the description of the function of exchangeable apolipoproteins is the requirement of a quantitative account of the relation between their physicochemical and structural characteristics and changes in the mesoscopic system parameters such as the maximum surface pressure and relative stability at interfaces. To comply with this demand, we set out to establish the relations among alpha-helix amphiphilicity, surface concentration, and surface rheology of apolipoproteins ApoA-I, ApoA-II, ApoC-I, ApoC-II, and ApoC-III adsorbed at the air-water interface. Our studies render further insights into the interfacial properties of exchangeable apolipoproteins, including the kinetics of their adsorption and the physical properties of the interfacial layer.
可交换载脂蛋白位于脂蛋白颗粒表面，通过直接的蛋白质 - 蛋白质和蛋白质 - 脂质相互作用调节脂质代谢。这些蛋白质的特征在于存在两亲性α - 螺旋段的串联重复序列，并且在单层和脂蛋白表面具有高表面活性。在描述可交换载脂蛋白功能时，一个值得注意的方面是需要定量说明其物理化学和结构特征与介观系统参数变化之间的关系，例如最大表面压力和界面处的相对稳定性。为了满足这一需求，我们着手建立吸附在空气 - 水界面的载脂蛋白ApoA - I、ApoA - II、ApoC - I、ApoC - II和ApoC - III的α - 螺旋亲水性、表面浓度和表面流变学之间的关系。我们的研究进一步深入了解了可交换载脂蛋白的界面性质，包括它们的吸附动力学和界面层的物理性质。
