Intrinsically disordered proteins access a range of hysteretic phase separation behaviors
Intrinsically disordered proteins access a range of hysteretic phase separation behaviors
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DOI：
10.1126/sciadv.aax5177
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发表时间：
2019-10-01
期刊：
影响因子：
13.6
通讯作者：
Chilkoti, Ashutosh
中科院分区：
文献类型：
--
作者：
Quiroz, Felipe Garcia;Li, Nan K.;Chilkoti, Ashutosh
本质无序蛋白质(IDPs)的相分离行为被认为类似于经历平衡的低或高临界溶液温度(分别为LCST和UCST)相变的聚合物的相分离行为。然而，这种观点忽略了蛋白质组件可能的非平衡性质。在这里，通过研究由编码LCST或UCST相行为的重复基序组成的IDP聚合物(IDPP)，我们发现IdP可以获得广泛的非平衡、滞后相行为。通过实验和模拟，我们证明了IDPPS中的滞后是可调的，并且它是通过在不可溶相中日益稳定的链间相互作用而出现的。为了探索滞后IDPP的用途，我们设计了具有可调稳定性的自组装纳米结构。这些发现揭示了IDPs丰富的相分离行为，并说明了滞后作为编程自组装材料中非平衡相行为的设计参数。
The phase separation behavior of intrinsically disordered proteins (IDPs) is thought of as analogous to that of polymers that undergo equilibrium lower or upper critical solution temperature (LCST and UCST, respectively) phase transition. This view, however, ignores possible nonequilibrium properties of protein assemblies. Here, by studying IDP polymers (IDPPs) composed of repeat motifs that encode LCST or UCST phase behavior, we discovered that IDPs can access a wide spectrum of nonequilibrium, hysteretic phase behaviors. Experimentally and through simulations, we show that hysteresis in IDPPs is tunable and that it emerges through increasingly stable interchain interactions in the insoluble phase. To explore the utility of hysteretic IDPPs, we engineer self-assembling nanostructures with tunable stability. These findings shine light on the rich phase separation behavior of IDPs and illustrate hysteresis as a design parameter to program nonequilibrium phase behavior in self-assembling materials.