Proton transfer is central to the functions of nature’s most remarkable biochemical pathways. Contingent on the microenvironments induced by the protein folding of enzymes and biological receptors, mechanisms of proton transfer may be dramatically altered relative to that of bulk water. In an effort to understand the influence of microenvironment on proton-mediated catalysis, we describe the mechanisms of amide proton exchange in a synthetic receptor whose properties resemble those of enzymes. The use of a well-defined host guest chemistry enables steric and electronic influences on proton transfer to be deconvoluted and quantified, providing a detailed description of the receptor microenvironment. This analysis provides an important step in the development of synthetic host catalysts that emulate the efficacy of enzymes.

Protein-like hydrogen exchange in a supramolecular structure

251st National Meeting (2016)

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