On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization.
Sala, Renata L
McCune, Jade A
J Am Chem Soc
American Chemical Society
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Chen, X., Huang, Z., Sala, R. L., McLean, A., Wu, G., Sokołowski, K., King, K., et al. (2022). On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization.. J Am Chem Soc https://doi.org/10.1021/jacs.2c02287
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.
European Commission Horizon 2020 (H2020) Marie Sk?odowska-Curie actions (845640)
Engineering and Physical Sciences Research Council (EP/L027151/1)
European Research Council (726470)
Engineering and Physical Sciences Research Council (EP/R512461/1)
External DOI: https://doi.org/10.1021/jacs.2c02287
This record's URL: https://www.repository.cam.ac.uk/handle/1810/340392
Attribution 4.0 International
Licence URL: https://creativecommons.org/licenses/by/4.0/