On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization,Journal of the American Chemical Society

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On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2022-05-10 , DOI: 10.1021/jacs.2c02287
Xiaoyi Chen ₁ , Zehuan Huang ₁ , Renata L Sala ₁ , Alan M McLean ₁ , Guanglu Wu ₁ , Kamil Sokołowski ₁ , Katie King ₁ , Jade A McCune ₁ , Oren A Scherman ₁

Affiliation

Peptide dimerization is ubiquitous in natural protein conjugates and artificial self-assemblies. A major challenge in artificial systems remains achieving quantitative peptide heterodimerization, critical for next-generation biomolecular purification and formulation of therapeutics. Here, we employ a synthetic host to simultaneously encapsulate an aromatic and a noncanonical l-perfluorophenylalanine-containing peptide through embedded polar−π interactions, constructing an unprecedented series of heteropeptide dimers. To demonstrate the utility, this heteropeptide dimerization strategy was applied toward on-resin recognition of N-terminal aromatic residues in peptides as well as insulin, both exhibiting high recycling efficiency (>95%). This research unveils a generic approach to exploit quantitative heteropeptide dimers for the design of supramolecular (bio)systems.

中文翻译：

通过宿主增强的异二聚化对芳香寡肽和蛋白质的树脂上识别

肽二聚化在天然蛋白质缀合物和人工自组装中普遍存在。人工系统的一个主要挑战仍然是实现定量肽异二聚化，这对于下一代生物分子纯化和治疗剂的制定至关重要。在这里，我们使用合成宿主通过嵌入的极性-π 相互作用同时封装芳香族和非经典的含l-全氟苯丙氨酸的肽，构建了前所未有的杂肽二聚体系列。为了证明实用性，这种异肽二聚化策略被应用于N的树脂上识别-肽和胰岛素中的末端芳香族残基，两者都表现出高回收效率（> 95％）。这项研究揭示了一种利用定量异肽二聚体设计超分子（生物）系统的通用方法。

更新日期：2022-05-10

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