Self-assembly of molecules often results in new emerging properties. Even very short peptides can self-assemble into structures with a variety of physical and structural characteristics. Remarkably, many peptide assemblies show high catalytic activity in model reactions reaching efficiencies comparable to those found in natural enzymes by weight. In this review, we discuss different strategies used to rationally develop self-assembled peptide catalysts with natural and unnatural backbones as well as with metal-containing cofactors.
Self-assembly
enables formation of incredibly diverse supramolecular
structures with practically important functions from simple and inexpensive
building blocks. Here, we show how a semirational, bottom-up approach
to create emerging properties can be extended to a design of highly
enantioselective catalytic nanoassemblies. The designed peptides comprising
as few as two amino acid residues spontaneously self-assemble in the
presence of metal ions to form supramolecular, vesicle-like nanoassemblies
that promote transfer hydrogenation of ketones in an aqueous phase
with excellent conversion rates and enantioselectivities (>90%
ee).
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