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Substrate-induced assembly of cascade enzymes and catalytic surfactants: nanoarchitectonics at the oil-in-water droplet interface
Chemical Communications ( IF 4.3 ) Pub Date : 2024-07-25 , DOI: 10.1039/d4cc03243h
Priyanka 1 , Manpreet Kaur 1 , Subhabrata Maiti 1
Affiliation  

The heterogeneous distribution of lipids and lipid-bound proteins in a plasma membrane has functional advantages. Herein, in a synthetic system, we demonstrate the assembly of three enzymes involved in cascade reactions, in response to the substrate of the first enzyme at the oil–water interface being stabilized by a Zn(II)-metallosurfactant. Then we show substrate-mediated catalytically-active cluster formation of the metallosurfactant in a binary mixture with another non-catalytic surfactant at the interface. The catalytic ability can be tuned by controlling clustering through the addition of phosphate ions. Overall this work demonstrates functionally diverse supramolecular nanoarchitectonics at the oil–water interface.

中文翻译:


底物诱导的级联酶和催化表面活性剂的组装:水包油液滴界面的纳米结构



质膜中脂质和脂质结合蛋白的异质分布具有功能优势。在此,在一个合成系统中,我们展示了参与级联反应的三种酶的组装,以响应油水界面处第一种酶的底物被锌( II )-金属表面活性剂稳定。然后,我们展示了金属表面活性剂在界面处与另一种非催化表面活性剂的二元混合物中底物介导的催化活性簇的形成。可以通过添加磷酸根离子来控制聚集来调节催化能力。总的来说,这项工作展示了油水界面上功能多样的超分子纳米结构。
更新日期:2024-07-25
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