Abstract
Cucurbit [8]uril (CB[8]) exhibits high binding affinity to specific peptide sequences, allowing the peptide-CB[8] system to operate effectively in diverse biological applications. However, it is imperative to identify effective regulation factors for the binding of peptides with CB[8], making it a more promising and responsive host-guest system. In this study, we discovered that phosphorylation at the side chain of tyrosine residue can completely disrupt the binding of a tripeptide motif (YLA or MYA) with CB[8]. This discovery introduces a novel enzymatic strategy for regulating the peptide-CB[8] host-guest interaction. Furthermore, it has been applied to detect the activity of phosphatases by supramolecular tandem assays.
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