与膜蛋白结合的小分子的高分辨率质谱分析。
High-resolution mass spectrometry of small molecules bound to membrane proteins.
作者信息
Gault Joseph, Donlan Joseph A C, Liko Idlir, Hopper Jonathan T S, Gupta Kallol, Housden Nicholas G, Struwe Weston B, Marty Michael T, Mize Todd, Bechara Cherine, Zhu Ya, Wu Beili, Kleanthous Colin, Belov Mikhail, Damoc Eugen, Makarov Alexander, Robinson Carol V
机构信息
Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
Department of Biochemistry, University of Oxford, Oxford, UK.
出版信息
Nat Methods. 2016 Apr;13(4):333-6. doi: 10.1038/nmeth.3771. Epub 2016 Feb 22.
Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length.
已知小分子可稳定膜蛋白并调节其功能和寡聚状态，但此类相互作用往往难以精确界定。在此，我们开发并应用了一种基于高分辨率轨道阱质谱的方法来分析完整的膜蛋白-配体复合物。利用该平台，我们解析了多种结合事件的复杂性，量化了小分子结合情况，并揭示了对仅在酰基链长度上存在差异的内源性脂质的选择性。
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