Nature's enzymes are extremely efficient catalysts. Their remarkable properties result from precise preorganization of the local solvent environment and functional groups around the catalytic sites, and close participation of metal ions, prosthetic groups, and cofactors. <i>De novo</i> design of functional proteins is still out of reach of modern chemistry, to a significant extent due to the complexity of the problem of protein folding. However, the globular structures and nanoscale dimensions of natural biopolymers provide useful boundary conditions for the rational design of enzyme mimics. The functional group tolerance and efficiency of “click” chemistry provided us with easy access to a broad range of enzyme-inspired macromolecules and functional surfactant assemblies rationally designed to broadly approximate some of the unique features of biopolymers. The catalytic activity and selective mass transfer ability of such systems are often unattainable with traditional homogeneous or heterogeneous catalysts.

Soft materials for catalysis and encapsulation: From micelles to complex macromolecular architectures

254th National Meeting (2017)

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