This paper describes a novel assay for measuring the relative extent of peptide binding in a large parallel format and the use of this assay to explore the effects of sequence context on the binding of tryptophan (Trp)-containing peptides by the synthetic receptor comprising the noncovalent complex between cucurbituril and methyl viologen (i.e. Q8√MV). The extent of quenching of Trp fluorescence upon binding to Q8√MV was used to measure the relative extent of binding and thus the relative affinities of 104 Trp-containing peptides, in parallel, using a fluorescence plate reader. This study resulted in the remarkable observation that the identity of the amino acid residues at positions adjacent to the Trp-binding site has little if any influence on the binding affinity. This finding suggests that Q8√MV should be effective for the recognition of Trp residues within a broad range of peptide sequences.
Document Object Identifier (DOI)
Ali, O. A., Olson, E. M., & Urbach, A. R. (2013). Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbituril-methyl viologen complex. Supramolecular Chemistry, 25, 863-868. doi: 10.1080/10610278.2013.810338