Brouillette C G, Anantharamaiah G M, Engler J A, Borhani D W
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, AL 35294-0005, USA.
Biochim Biophys Acta. 2001 Mar 30;1531(1-2):4-46. doi: 10.1016/s1388-1981(01)00081-6.
Human apolipoprotein (apo) A-I has been the subject of intense investigation because of its well-documented anti-atherogenic properties. About 70% of the protein found in high density lipoprotein complexes is apo A-I, a molecule that contains a series of highly homologous amphipathic alpha-helices. A number of significant experimental observations have allowed increasing sophisticated structural models for both the lipid-bound and the lipid-free forms of the apo A-I molecule to be tested critically. It seems clear, for example, that interactions between amphipathic domains in apo A-I may be crucial to understanding the dynamic nature of the molecule and the pathways by which the lipid-free molecule binds to lipid, both in a discoidal and a spherical particle. The state of the art of these structural studies is discussed and placed in context with current models and concepts of the physiological role of apo A-I and high-density lipoprotein in atherosclerosis and lipid metabolism.
人类载脂蛋白（apo）A-I因其具有充分记录的抗动脉粥样硬化特性而成为深入研究的对象。在高密度脂蛋白复合物中发现的约70%的蛋白质是apo A-I，该分子包含一系列高度同源的两亲性α螺旋。大量重要的实验观察结果使得越来越复杂的apo A-I分子脂质结合形式和无脂质形式的结构模型能够得到严格测试。例如，很明显，apo A-I中两亲性结构域之间的相互作用对于理解该分子的动态性质以及无脂质分子在盘状和球状颗粒中与脂质结合的途径可能至关重要。本文讨论了这些结构研究的现状，并将其与apo A-I和高密度脂蛋白在动脉粥样硬化和脂质代谢中的生理作用的当前模型和概念相结合。
