Suyama Keitaro, Murashima Masayuki, Maeda Iori, Nose Takeru
Faculty of Arts and Science, Kyushu University, Fukuoka 819-0395, Japan.
Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka 819-0395, Japan.
Biomacromolecules. 2023 Nov 13;24(11):5265-5276. doi: 10.1021/acs.biomac.3c00779. Epub 2023 Oct 22.
Elastin-like peptides (ELPs) exhibit temperature-dependent reversible self-assembly. Repetitive sequences derived from elastin, such as Val-Pro-Gly-Val-Gly (VPGVG), are essential for the self-assembly of ELPs. Previously, we developed (FPGVG) (F5), in which the first valine residue in the VPGVG sequence was replaced with phenylalanine, which showed strong self-aggregation ability. This suggests that interactions through the aromatic amino acid residues of ELPs could play an important role in self-assembly. In this study, we investigated the thermoresponsive behavior of F5 analogs in the presence of aromatic compounds. Turbidimetry, spectroscopy, and fluorescence measurements demonstrated that aromatic compounds interacted with F5 analogs below the transition temperature and enhanced the self-assembly ability of ELPs by stabilizing amyloid-like structures. Furthermore, quantitative high-performance liquid chromatography analyses showed that the F5 analogs could adsorb and remove hydrophobic aromatic compounds from aqueous solutions during aggregate formation. These results suggested that the F5 analogs can be applicable as scavengers of aromatic compounds.
类弹性蛋白肽（ELP）表现出温度依赖性的可逆自组装。源自弹性蛋白的重复序列，如缬氨酸-脯氨酸-甘氨酸-缬氨酸-甘氨酸（VPGVG），对ELP的自组装至关重要。此前，我们开发了（FPGVG）（F5），其中VPGVG序列中的第一个缬氨酸残基被苯丙氨酸取代，它表现出很强的自聚集能力。这表明ELP通过芳香族氨基酸残基的相互作用可能在自组装中起重要作用。在本研究中，我们研究了在芳香族化合物存在下F5类似物的热响应行为。比浊法、光谱法和荧光测量表明，芳香族化合物在转变温度以下与F5类似物相互作用，并通过稳定淀粉样结构增强了ELP的自组装能力。此外，高效液相色谱定量分析表明，F5类似物在聚集体形成过程中可以从水溶液中吸附并去除疏水性芳香族化合物。这些结果表明，F5类似物可作为芳香族化合物的清除剂。
