Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
FEBS Lett. 2010 Mar 19;584(6):1139-42. doi: 10.1016/j.febslet.2010.01.058. Epub 2010 Feb 2.
Amyloid deposits, which accumulate in numerous diseases, are the final stage of multi-step protein conformational-conversion and oligomerization processes. The underlying molecular mechanisms are not fully understood, and particularly little is known about the reverse reaction. Here we show that phosphoglycerate kinase amyloid fibrils can be converted back into native protein. We achieved recovery with 60% efficiency, which is comparable to the success rate of the unfolding-refolding studies, and the recovered enzyme was folded, stable and fully active. The key intermediate stages in the recovery process are fibril disassembly and unfolding followed by spontaneous protein folding.
淀粉样沉积物在许多疾病中积累，是多步蛋白质构象转换和寡聚化过程的最终阶段。其潜在的分子机制尚未完全了解，特别是关于其逆转反应知之甚少。在这里，我们表明磷酸甘油酸激酶淀粉样纤维可以转化回天然蛋白质。我们实现了 60%的效率恢复，这与解折叠-重折叠研究的成功率相当，并且恢复的酶是折叠的、稳定的和完全有活性的。恢复过程中的关键中间阶段是纤维的解组装和展开，随后是自发的蛋白质折叠。
