From the Departments of Pediatrics and Pharmacology, The Children's Hospital of Philadelphia Research Institute and.
J Biol Chem. 2014 Mar 14;289(11):7929-34. doi: 10.1074/jbc.C113.538249. Epub 2014 Jan 28.
α-Synuclein aggregation is central to the pathogenesis of several brain disorders. However, the native conformations and functions of this protein in the human brain are not precisely known. The native state of α-synuclein was probed by gel filtration coupled with native gradient gel separation, an array of antibodies with non-overlapping epitopes, and mass spectrometry. The existence of metastable conformers and stable monomer was revealed in the human brain.
α-突触核蛋白聚集是几种脑部疾病发病机制的核心。然而，这种蛋白质在人类大脑中的天然构象和功能尚不清楚。通过凝胶过滤与天然梯度凝胶分离、具有非重叠表位的一系列抗体和质谱分析来探测α-突触核蛋白的天然状态。在人脑中共发现了亚稳态构象和稳定单体的存在。
