Recognizing peptides and proteins with high affinity and selectivity is a challenge in medicine and biotechnology. While both of these criteria have been met and understood for binding at the N terminus of a polypeptide using cucurbit[n]uril hosts, relatively little is understood about non-terminal interactions. We designed a peptide library to study the effects of neighboring residues upon the binding of cucurbit[7]uril and cucurbit[8]uril. Specifically, we were interested in the effects if the neighboring residues are positively charged or sterically hinder the peptide backbone. This library was prepared by parallel solid-phase synthesis and characterized by mass spectrometry, high-performance liquid chromatography, and UV spectroscopy. Host binding was studied using a parallel fluorescence assay. These results and related directions will be presented.

Effects of neighboring sequence context on cucurbit[n]uril-peptide interactions

253rd National Meeting (2017)

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