N-terminal dual protein functionalization by strain-promoted alkyne-nitrone cycloaddition

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Abstract

Strain-promoted alkyne-nitrone cycloadditon (SPANC) was optimized as a versatile strategy for dual functionalization of peptides and proteins. The usefulness of the dual labeling protocol is first exemplified by the simultaneous introduction of a chloroquine and a stearyl moiety, two endosomal escape-improving functional groups, into the cell-penetrating peptide hLF (human lactoferrin). Additionally, we demonstrate that dual labeling of proteins is feasible by combining metal-free and copper-catalyzed click chemistry. First, SPANC is applied to enhanced green fluorescent protein to introduce both biotin and a terminal alkyne. The terminal acetylene then serves as a convenient anchor point for the CuAAC reaction with azido-containing fluorescein, thereby demonstrating the potential of combined SPANC and CuAAC for the straightforward, dual functionalization of proteins. © 2013 The Royal Society of Chemistry.

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Temming, R. P., Eggermont, L., Van Eldijk, M. B., Van Hest, J. C. M., & Van Delft, F. L. (2013). N-terminal dual protein functionalization by strain-promoted alkyne-nitrone cycloaddition. Organic and Biomolecular Chemistry, 11(17), 2772–2779. https://doi.org/10.1039/c3ob00043e

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