We have developed mimics of enzymes that have several important features. They operate in water solution, and one type is able to direct oxidation reactions whose selectivity is dominated by the geometry of the catalyst/substrate complex, overriding the intrinsic reactivity of the substrate. Our goal in this work is to “liberate chemistry from the tyranny of functional groups.”

Another type of biomimetic catalyst is based on hydrophilic polymers with hydrophobic cores. This class is able to imitate the ability of enzymes to use the advantages of water for hydrophobic binding but use the non-aqueous interior of the protein to promote rapid catalytic reactions, producing “a drop of DMSO suspended in water.” The result is an acceleration of the synthesis of tryptophan by transamination with an acceleration of 240,000-fold caused by the polymer. Recently the system has been improved by using non-covalent complexes of coenzyme mimics to accelerate tryptophan synthesis by 725,000-fold.