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Stepwise Mechanism of Temperature-Dependent Coacervation of the Elastin-like Peptide Analogue Dimer, (C(WPGVG)3)2
Biochemistry ( IF 2.9 ) Pub Date : 2018-02-01 00:00:00 , DOI: 10.1021/acs.biochem.7b01144 Daiki Tatsubo 1 , Keitaro Suyama 2 , Masaya Miyazaki 3 , Iori Maeda 4 , Takeru Nose 1, 2
Biochemistry ( IF 2.9 ) Pub Date : 2018-02-01 00:00:00 , DOI: 10.1021/acs.biochem.7b01144 Daiki Tatsubo 1 , Keitaro Suyama 2 , Masaya Miyazaki 3 , Iori Maeda 4 , Takeru Nose 1, 2
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Elastin-like peptides (ELPs) are distinct, repetitive, hydrophobic sequences, such as (VPGVG)n, that exhibit coacervation, the property of reversible, temperature-dependent self-association and dissociation. ELPs can be found in elastin and have been developed as new scaffold biomaterials. However, the detailed relationship between their amino acid sequences and coacervation properties remains obscure because of the structural flexibility of ELPs. In this study, we synthesized a novel, dimeric ELP analogue (H-C(WPGVG)3-NH2)2, henceforth abbreviated (CW3)2, and analyzed its self-assembly properties and structural factors as indicators of coacervation. Turbidity measurements showed that (CW3)2 demonstrated coacervation at a concentration much lower than that of its monomeric form and another ELP. In addition, the coacervate held water-soluble dye molecules. Thus, potent and distinct coacervation was obtained with a remarkably short sequence of (CW3)2. Furthermore, fluorescence microscopy, dynamic light scattering, and optical microscopy revealed that the coacervation of (CW3)2 was a stepwise process. The structural factors of (CW3)2 were analyzed by molecular dynamics simulations and circular dichroism spectroscopy. These measurements indicated that helical structures primarily consisting of proline and glycine became more disordered at high temperatures with concurrent, significant exposure of their hydrophobic surfaces. This extreme change in the hydrophobic surface contributes to the potent coacervation observed for (CW3)2. These results provide important insights into more efficient applications of ELPs and their analogues, as well as the coacervation mechanisms of ELP and elastin.
中文翻译：
弹性蛋白样肽类似物二聚体（C（WPGVG）3）2的温度依赖性凝聚的逐步机理
弹性蛋白样肽（ELPs）是独特的，重复的疏水序列，例如（VPGVG）n，表现出凝聚作用，可逆的，依赖温度的自缔合和解离特性。ELP可以在弹性蛋白中找到，并已被开发为新型支架生物材料。但是，由于ELP的结构灵活性，其氨基酸序列与凝聚性能之间的详细关系仍然不清楚。在这项研究中，我们合成了一种新型的二聚体ELP类似物（HC（WPGVG）3 -NH 2）2，此后简称为（CW3）2，并分析了其自组装特性和结构因素作为凝聚的指标。浊度测量结果表明，（CW3）2在比其单体形式和另一种ELP浓度低得多的浓度下表现出凝聚作用。另外，凝聚层保持水溶性染料分子。因此，以非常短的（CW3）2序列获得了有效而独特的凝聚。此外，荧光显微镜，动态光散射和光学显微镜显示（CW3）2凝聚是一个逐步的过程。（CW3）2的结构因素通过分子动力学模拟和圆二色光谱分析。这些测量结果表明，主要由脯氨酸和甘氨酸组成的螺旋结构在高温下变得更加无序，同时疏水表面同时大量暴露。疏水性表面的这种极端变化有助于观察到（CW3）2的强凝聚。这些结果为更有效地应用ELP及其类似物，以及ELP和弹性蛋白的凝聚机制提供了重要的见识。
更新日期：2018-02-01
中文翻译：
弹性蛋白样肽类似物二聚体（C（WPGVG）3）2的温度依赖性凝聚的逐步机理
弹性蛋白样肽（ELPs）是独特的，重复的疏水序列，例如（VPGVG）n，表现出凝聚作用，可逆的，依赖温度的自缔合和解离特性。ELP可以在弹性蛋白中找到，并已被开发为新型支架生物材料。但是，由于ELP的结构灵活性，其氨基酸序列与凝聚性能之间的详细关系仍然不清楚。在这项研究中，我们合成了一种新型的二聚体ELP类似物（HC（WPGVG）3 -NH 2）2，此后简称为（CW3）2，并分析了其自组装特性和结构因素作为凝聚的指标。浊度测量结果表明，（CW3）2在比其单体形式和另一种ELP浓度低得多的浓度下表现出凝聚作用。另外，凝聚层保持水溶性染料分子。因此，以非常短的（CW3）2序列获得了有效而独特的凝聚。此外，荧光显微镜，动态光散射和光学显微镜显示（CW3）2凝聚是一个逐步的过程。（CW3）2的结构因素通过分子动力学模拟和圆二色光谱分析。这些测量结果表明，主要由脯氨酸和甘氨酸组成的螺旋结构在高温下变得更加无序，同时疏水表面同时大量暴露。疏水性表面的这种极端变化有助于观察到（CW3）2的强凝聚。这些结果为更有效地应用ELP及其类似物，以及ELP和弹性蛋白的凝聚机制提供了重要的见识。
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