Elastin-like peptides (ELPs) are thermoresponsive biopolymers inspired by the characteristic repetitive sequences of natural elastin; they show promise as drug carriers. Takeru Nose and co-workers report the effect of amino acid substitution on the self-assembly of the short ELP (FPGVG)₅ and its analogues. Substituting or introducing an amino acid that increases the bulkiness of the N-terminal is seen to enhance the self-assembling ability of (FPGVG)₅ analogues, likely because of hydrophobicity-induced intermolecular interactions. Substituting a single Phe residue drastically changes the temperature responsiveness of the analogues, suggesting that aromatic amino acids play an important role in the self-assembly of these systems. DOI: 10.1002/bip.23521

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弹性蛋白样肽 (ELP) 是一种受天然弹性蛋白特征性重复序列启发的热响应性生物聚合物；他们显示出作为药物携带者的希望。Takeru Nose 及其同事报告了氨基酸取代对短 ELP (FPGVG) ₅及其类似物自组装的影响。取代或引入增加N-末端体积的氨基酸被认为增强了(FPGVG) ₅类似物的自组装能力，这可能是由于疏水性诱导的分子间相互作用。取代单个 Phe 残基极大地改变了类似物的温度响应性，表明芳香族氨基酸在这些系统的自组装中起重要作用。DOI：10.1002/bip.23521