Department of Pure and Applied Chemistry, Technology and Innovation Centre, University of Strathclyde, Glasgow, UK.
Department of Chemical and Biomolecular Engineering, University of Notre Dame, Notre Dame, IN, 46556, USA.
Angew Chem Int Ed Engl. 2017 Jun 6;56(24):6828-6832. doi: 10.1002/anie.201701870. Epub 2017 May 10.
The properties of supramolecular materials are dictated by both kinetic and thermodynamic aspects, providing opportunities to dynamically regulate morphology and function. Herein, we demonstrate time-dependent regulation of supramolecular self-assembly by connected, kinetically competing enzymatic reactions. Starting from Fmoc-tyrosine phosphate and phenylalanine amide in the presence of an amidase and phosphatase, four distinct self-assembling molecules may be formed which each give rise to distinct morphologies (spheres, fibers, tubes/tapes and sheets). By varying the sequence or ratio in which the enzymes are added to mixtures of precursors, these structures can be (transiently) accessed and interconverted. The approach provides insights into dynamic self-assembly using competing pathways that may aid the design of soft nanostructures with tunable dynamic properties and life times.
超分子材料的性质由动力学和热力学两个方面决定，这为动态调节形态和功能提供了机会。在此，我们通过连接的、动力学竞争的酶反应来展示超分子自组装的时间依赖性调节。从 Fmoc-酪氨酸磷酸盐和苯丙氨酸酰胺在酰胺酶和磷酸酶的存在下，可能形成四种不同的自组装分子，它们各自产生不同的形态（球体、纤维、管/带和片）。通过改变酶添加到前体混合物中的顺序或比例，可以（暂时）访问和转换这些结构。该方法提供了对使用竞争途径的动态自组装的深入了解，这可能有助于设计具有可调动态特性和寿命的软纳米结构。
