无序和弹性蛋白样多肽的热压缩：一个温度依赖的、序列特异性的粗粒度模拟模型
Thermal compaction of disordered and elastin-like polypeptides: a temperature-dependent, sequence-specific coarse-grained simulation model
摘要：
弹性蛋白样多肽（ELP）在高温下经历从低温溶剂化相到凝聚相的急剧溶解度转变，这是由较高温度下疏水相互作用强度增加驱动的。转变温度或“浊点”关键取决于ELP的序列组成、序列长度和浓度。在这项工作中，我们提出了一个温度依赖性，隐式溶剂，序列特定的粗粒度（CG）模拟模型，再现的转变温度作为一个函数的序列长度和客体残基身份的各种实验探测ELP可观的准确性。我们的模型建立在自组织的聚合物模型最近推出的内在无序的多肽（SOP-IDP），并引入了半经验的功能形式的疏水相互作用的温度依赖性。除了各种ELP的优良性能，我们证明了我们的模型捕获的热压实在主要疏水性的本质上无序的多肽（IDPs），与实验散射数据一致的能力。与CG表示所提供的高计算效率，我们设想，该模型将非常适合于模拟的大尺度结构，如ELP网络和水凝胶，以及聚集体的IDP。
英文摘要：
Elastin-like polypeptides (ELPs) undergo a sharp solubility transition from low temperature solvated phases to coacervates at elevated temperatures, driven by the increased strength of hydrophobic interactions at higher temperatures. The transition temperature, or 'cloud point', critically depends on sequence composition, sequence length, and concentration of the ELPs. In this work, we present a temperature-dependent, implicit solvent, sequence-specific coarse-grained (CG) simulation model that reproduces the transition temperatures as a function of sequence length and guest residue identity of various experimentally probed ELPs to appreciable accuracy. Our model builds upon the self-organized polymer model introduced recently for intrinsically disordered polypeptides (SOP-IDP), and introduces a semi-empirical functional form for the temperature-dependence of hydrophobic interactions. In addition to the fine performance for various ELPs, we demonstrate the ability of our model to capture the thermal compactions in dominantly hydrophobic intrinsically disordered polypeptides (IDPs), consistent with experimental scattering data. With the high computational efficiency afforded by the CG representation, we envisage that the model will be ideally suited for simulations of large-scale structures such as ELP networks and hydrogels, as well as agglomerates of IDPs.
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