Bousset Luc, Brewee Clémence, Melki Ronald, Migliardo Federica
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bat 34, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Department of Physics and Earth Sciences, University of Messina, Viale D'Alcontres 31, 98166 Messina, Italy.
Biochim Biophys Acta. 2014 Jul;1844(7):1307-16. doi: 10.1016/j.bbapap.2014.04.010. Epub 2014 Apr 21.
In the present paper, Quasi Elastic Neutron Scattering (QENS) results, gathered at different energy resolution values at the ISIS Facility (RAL, UK), on α-synuclein in soluble and fibrillar forms as a function of temperature and exchanged wave-vector Q are shown. The measurements reveal a different dynamic behavior of the soluble and fibrillar forms of α-synuclein as a function of thermal stress. In more detail, the dynamics of each protein form reflects its own complex conformational heterogeneity. Furthermore, the effect of a well known bioprotectant, trehalose, that influences α-synuclein fibrillation, on both soluble and fibrillar forms of α-synuclein is discussed.
在本论文中，展示了在英国RAL的ISIS设施上，在不同能量分辨率值下收集的关于可溶性和纤维状α-突触核蛋白随温度和交换波矢Q变化的准弹性中子散射（QENS）结果。测量结果揭示了α-突触核蛋白的可溶性和纤维状形式随热应力变化的不同动力学行为。更详细地说，每种蛋白质形式的动力学反映了其自身复杂的构象异质性。此外，还讨论了一种众所周知的生物保护剂海藻糖对α-突触核蛋白纤维化的影响，以及它对α-突触核蛋白的可溶性和纤维状形式的作用。
