Department of Biochemistry & Molecular Biology, Dalhousie University, Tupper Medical Building, 5850 College Street, Halifax, NS B3H 1X5, Canada.
Biochem Cell Biol. 2010 Apr;88(2):203-10. doi: 10.1139/O09-129.
The membrane catalysis hypothesis states that a peptide ligand activates its target receptor after an initial interaction with the surrounding membrane. Upon membrane binding and interaction, the ligand is structured such that receptor binding and activation is encouraged. As evidence for this hypothesis, there are numerous studies concerning the conformation that peptides adopt in membrane mimetic environments. This mini-review analyzes the features of ligand peptides with an available high-resolution membrane-induced structure and a characterized membrane-binding region. At the peptide-membrane interface, both amphipathic helices and turn structures are commonly formed in peptide ligands and both hydrophobic and electrostatic interactions can be responsible for membrane binding. Apelin is the ligand to the G-protein coupled receptor (GPCR) named APJ, with various important physiological effects, which we have recently characterized both in solution and bound to anionic micelles. The structural changes that apelin undergoes when binding to micelles provide strong evidence for membrane catalysis of apelin-APJ interactions.
膜催化假说指出，肽配体在与周围膜最初相互作用后，激活其靶受体。在膜结合和相互作用后，配体的结构会促使受体结合和激活。作为该假说的证据，有许多关于肽在膜类似物环境中采用的构象的研究。本篇迷你综述分析了具有可用高分辨率膜诱导结构和特征性膜结合区域的配体肽的特征。在肽-膜界面，两亲性螺旋和转角结构在肽配体中通常形成，疏水性和静电相互作用都可能负责膜结合。Apelin 是 G 蛋白偶联受体（GPCR）APJ 的配体，具有多种重要的生理作用，我们最近在溶液中和与阴离子胶束结合的情况下对其进行了表征。Apelin 与胶束结合时发生的结构变化为 Apelin-APJ 相互作用的膜催化提供了有力证据。
