Introduction of abiotic constituents into protein architectures can generate hybrid macromolecules that exhibit novel functions and enhanced pharmacological profiles. Chemical synthesis of such constructs can be achieved using chemoselective ligation protocols. We have elaborated a rapid and site-specific ligation strategy to bioconjugate synthetic oligomers, termed 'peptoids', to N-terminal serine or threonine residues of peptides and proteins, generating native amide linkages at the ligation site. Peptoids are composed of specific sequences of diverse N-substituted glycine monomers and have been shown to populate distinct secondary structures not readily accessible to polypeptides. Modifications of current expressed protein ligation techniques were implemented to generate synthetic variants of a therapeutic polypeptide. The future prospects of peptoid-protein hybrids for materials and biomedical applications will be evaluated.

Peptoid-protein hybrids

248th National Meeting (2014)

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