The rapidly growing role of proteins as therapeutic agents and cell-specific targeting groups has created a high demand for new bioconjugation strategies. To be useful, these reactions must be capable of modifying one or a limited number of functional groups on the surface of a complex biomolecule without the use of protecting groups. They must also proceed in aqueous media at mild temperatures and at near-neutral pH. As a result of these requirements, there remain relatively few techniques that can be used for bioconjugate formation. In this presentation, two different chemical strategies will be presented for the single-step modification of the N-terminal positions of proteins and peptides. Both methods are tolerant of free cysteine residues and glycan groups, and thus they can be applied to a very wide substrate scope. As the vast majority of proteins possess free N-termini, these strategies are envisioned to be useful for the preparation of many new types of protein-based materials. The application of these techniques for the efficient preparation of well-defined protein-polymer conjugates will serve as the focus of the presentation.

New bioconjugation strategies for the site-selective modification of protein N-termini

247th National Meeting (2014)

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