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Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides
Beilstein Journal of Organic Chemistry ( IF 2.2 ) Pub Date : 2020-11-04 , DOI: 10.3762/bjoc.16.221
Dongsik Yang , Hongjian He , Bing Xu

Here, we report the use of an enzymatic reaction to cleave the branch off branched peptides for inducing the morphological transition of the assemblies of the peptides. The attachment of DEDDDLLI sequences to the ε-amine of the lysine residue of a tetrapeptide produces branched peptides that form micelles. Upon the proteolytic cleavage of the branch, catalyzed by proteinase K, the micelles turn into nanofibers. We also found that the acetylation of the N-terminal of the branch increased the stability of the branched peptides. Moreover, these branched peptides facilitate the delivery of the proteins into cells. This work contributes insights for the development of peptide supramolecular assemblies via enzymatic noncovalent synthesis in cellular environment.

中文翻译:

支链肽的超分子组装的酶促形态转变

在这里,我们报告了使用酶促反应裂解分支肽的分支,以诱导肽组装体的形态转变。DEDDDLLI序列与四肽赖氨酸残基的ε-胺的连接产生了形成胶束的支链肽。在蛋白酶K催化下,分支的蛋白水解裂解后,胶束变成纳米纤维。我们还发现分支的N末端的乙酰化增加了分支肽的稳定性。而且,这些分支的肽促进了蛋白质向细胞内的传递。这项工作有助于在细胞环境中通过酶促非共价合成开发肽超分子组装体。
更新日期:2020-11-04
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