3 years ago

Biocatalytic Self-Assembly Cascades

Biocatalytic Self-Assembly Cascades
Ivan Ramos Sasselli, Rein V. Ulijn, Charalampos G. Pappas, Yousef M. Abul-Haija, Jugal Kishore Sahoo
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. Finding the right path: Starting from Fmoc-tyrosine phosphate and phenylalanine amide in the presence of an amidase (orange in scheme) and phosphatase (green), four distinct molecules are 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 accessed and interconverted in a controlled manner.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201701870

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