On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization.
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Peer-reviewed
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Abstract
Peptide dimerization is ubiquitous in natural protein conjugates and artificial self-assemblies. A major challenge in artificial systems remains achieving quantitative peptide heterodimerization, critical for next-generation biomolecular purification and formulation of therapeutics. Here, we employ a synthetic host to simultaneously encapsulate an aromatic and a noncanonical l-perfluorophenylalanine-containing peptide through embedded polar-π interactions, constructing an unprecedented series of heteropeptide dimers. To demonstrate the utility, this heteropeptide dimerization strategy was applied toward on-resin recognition of N-terminal aromatic residues in peptides as well as insulin, both exhibiting high recycling efficiency (>95%). This research unveils a generic approach to exploit quantitative heteropeptide dimers for the design of supramolecular (bio)systems.
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1520-5126
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EPSRC (2342310)
Engineering and Physical Sciences Research Council (EP/L027151/1)
European Research Council (726470)
Engineering and Physical Sciences Research Council (EP/R512461/1)