Noncovalent Modulation of the Inverse Temperature Transition and Self-Assembly of Elastin-b-Collagen-like Peptide Bioconjugates.
Noncovalent Modulation of the Inverse Temperature Transition and Self-Assembly of Elastin-b-Collagen-like Peptide Bioconjugates.
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DOI：
10.1021/jacs.5b09941
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发表时间：
2015-12-16
影响因子：
15
通讯作者：
Kiick KL
中科院分区：
文献类型：
--
作者：
Luo T;Kiick KL
用细胞外基质的肽结构域产生的刺激响应纳米结构为成像和药物输送提供了巨大的机会。尽管已经证明了弹性蛋白样(多)肽和胶原样肽在此类应用中的单独效用，但令人惊讶的是尚未报道将这些基序组合在短肽缀合物中的协同优势。在这里，我们介绍了热响应性弹性蛋白样肽（ELP）与三螺旋形成胶原蛋白样肽（CLP）的缀合，产生ELP-CLP缀合物，该缀合物在CLP三螺旋形成后显示出ELP结构域的逆转变温度显着降低。缀合物的较低转变温度使得能够在生理温度下轻松形成明确的囊泡，并在 CLP 结构域解折叠后在升高的温度下意外地重新溶解囊泡。鉴于 CLP 修饰胶原蛋白的能力已得到证实，我们的结果不仅为控制 ELP 的逆转变行为提供了一种简单且通用的途径，而且还为这些热响应纳米结构在生物相关环境中的未来机会提出了建议。
Stimuli-responsive nanostructures produced with peptide domains from the extracellular matrix offer great opportunities for imaging and drug delivery. Although the individual utility of elastin-like (poly)-peptides and collagen-like peptides in such applications has been demonstrated, the synergistic advantages of combining these motifs in short peptide conjugates have surprisingly not been reported. Here, we introduce the conjugation of a thermoresponsive elastin-like peptide (ELP) with a triple-helix-forming collagen-like peptide (CLP) to yield ELP–CLP conjugates that show a remarkable reduction in the inverse transition temperature of the ELP domain upon formation of the CLP triple helix. The lower transition temperature of the conjugate enables the facile formation of well-defined vesicles at physiological temperature and the unexpected resolubilization of the vesicles at elevated temperatures upon unfolding of the CLP domain. Given the demonstrated ability of CLPs to modify collagens, our results not only provide a simple and versatile avenue for controlling the inverse transition behavior of ELPs, but also suggest future opportunities for these thermoresponsive nanostructures in biologically relevant environments.