Reversible, Short α-Peptide Assembly for Controlled Capture and Selective Release of Enantiomers,Journal of the American Chemical Society

当前位置： X-MOL 学术 › J. Am. Chem. Soc. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Reversible, Short α-Peptide Assembly for Controlled Capture and Selective Release of Enantiomers
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2016-05-03 , DOI: 10.1021/jacs.6b02401
Xi Chen ₁ , Ying He ₁ , Yongju Kim ₁ , Myongsoo Lee ₁

Affiliation

Although significant progress has been achieved with short peptide nanostructures, the construction of switchable membrane assemblies remains a great challenge. Here we report short α-peptide assemblies that undergo thermo-reversible switching between assembly and disassembly states, triggered by the conformational change of laterally grafted short peptides from a folded α-helix to a random coil conformation. The α-helical peptide based on two oligoether dendron side groups forms flat disks, while the peptide helix based on three dendron side groups forms hollow vesicles. The vesicular membrane can spontaneously capture a racemic mixture through the self-formation of vesicular containers upon heating and enantioselectively release the chiral guest molecule through preferential diffusion across the vesicular walls.

中文翻译：

用于对映异构体的受控捕获和选择性释放的可逆、短 α-肽组装

尽管短肽纳米结构已经取得了重大进展，但可切换膜组件的构建仍然是一个巨大的挑战。在这里，我们报告了短 α-肽组装体，它们在组装和拆卸状态之间经历热可逆转换，由横向接枝的短肽从折叠的 α-螺旋到无规卷曲构象的构象变化触发。基于两个低聚醚树突侧基的α-螺旋肽形成扁平圆盘，而基于三个树突侧基的肽螺旋形成空泡。囊泡膜可以通过囊泡容器在加热时的自形成自发捕获外消旋混合物，并通过优先扩散穿过囊泡壁对映选择性地释放手性客体分子。

更新日期：2016-05-03

点击分享查看原文

点击收藏

阅读更多本刊新发论文本刊介绍/投稿指南