Does liquid-liquid phase separation drive peptide folding?

Does liquid-liquid phase separation drive peptide folding?
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液 - 液相分离会驱动肽折叠吗?

DOI:
10.1039/d0sc04993j
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发表时间:
2020-12-29
期刊:
影响因子:
8.4
通讯作者:
Serrano AL
Serrano AL
中科院分区:
化学1区
文献类型:
--
作者:
Edun DN;Flanagan MR;Serrano AL

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脯氨酸-精氨酸(PR)二肽重复序列已被证明经历液-液相分离,并且是越来越多的可以组装成无膜细胞器的内在无序蛋白质的一个例子。这些结构已被假定为致病蛋白质聚集的成核位点。因此,需要更好地理解液滴内局部浓度增加和体积拥挤对肽二级结构的影响。在本文中,我们使用傅里叶变换红外(FTIR)和二维红外(2D)光谱显示,由PR 20形成的液滴伴随着与折叠成聚脯氨酸螺旋结构一致的酰胺-I光谱的变化。二维红外光谱揭示了折叠的内在无序肽时,隔离成一个模型“无膜”的细胞器。
Proline–arginine (PR) dipeptide repeats have been shown to undergo liquid–liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as nucleation sites for pathogenic protein aggregation. As such, a better understanding of the effects that the increased local concentration and volumetric crowding within droplets have on peptide secondary structure is necessary. Herein we use Fourier transform infrared (FTIR) and two-dimensional infrared (2DIR) spectroscopy to show that formation of droplets by PR20 accompanies changes in the amide-I spectra consistent with folding into poly-proline helical structures. Two-dimensional infrared spectroscopy reveals folding of an intrinsically disordered peptide when sequestered into a model “membrane-less” organelle.
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发表时间: 2005-06-16
影响因子: 3.3
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