Peptide Assemblies Mimicking Chaperones for Protein Trafficking,Bioconjugate Chemistry

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Peptide Assemblies Mimicking Chaperones for Protein Trafficking
Bioconjugate Chemistry ( IF 4.0 ) Pub Date : 2021-02-17 , DOI: 10.1021/acs.bioconjchem.1c00032
Dongsik Yang ₁ , Hongjian He ₁ , Beom Jin Kim ₁ , Bing Xu ₁

Affiliation

Although peptide assemblies have been explored extensively, the self-assembly of negatively charged peptides (NCPs) received little attention. Stimulated by the fact that acidic stretch is a common feature in the intrinsically disordered regions of histone chaperones, we explored the use of the assemblies of NCPs for trafficking histone proteins. Our results show that the peptides that contain glutamic acid (E)-repeat, at neutral or basic pH, self-assemble to form micelles in solution. Circular dichroism indicates that increasing pH favored the peptides to populate more in disordered and α helix conformations. Being innocuous to cells, the assemblies of these NCPs traffic histone 2B (H2B) to mitochondria. Structure–activity study indicates that self-assembly, proper stereochemistry, and acidic repeats are necessary for trafficking H2B. This work, as the first example of peptide assemblies for protein trafficking, illustrates a supramolecular approach for controlling cellular processes and provides insights for mimicking chaperones and controlling protein–protein interactions.

中文翻译：

模拟蛋白质运输伴侣的肽组装体

尽管肽组装已被广泛探索，但带负电肽（NCP）的自组装却很少受到关注。受酸性拉伸是组蛋白伴侣本质无序区域的一个常见特征的刺激，我们探索了使用 NCP 组装来运输组蛋白。我们的结果表明，含有谷氨酸 (E) 重复序列的肽在中性或碱性 pH 值下会在溶液中自组装形成胶束。圆二色性表明，增加 pH 值有利于肽以无序构象和 α 螺旋构象更多地聚集。这些 NCP 的组装体对细胞无害，可将组蛋白 2B (H2B) 运输至线粒体。结构-活性研究表明自组装、适当的立体化学和酸性重复对于 H2B 运输是必要的。这项工作作为蛋白质运输肽组装的第一个例子，说明了控制细胞过程的超分子方法，并为模拟伴侣和控制蛋白质-蛋白质相互作用提供了见解。

更新日期：2021-03-17

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