Issue 17, 2013

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

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.

Graphical abstract: N-terminal dual protein functionalization by strain-promoted alkyne–nitrone cycloaddition

Supplementary files

Article information

Article type
Paper
Submitted
09 Jan 2013
Accepted
20 Feb 2013
First published
20 Feb 2013
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2013,11, 2772-2779

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

R. P. Temming, L. Eggermont, M. B. van Eldijk, J. C. M. van Hest and F. L. van Delft, Org. Biomol. Chem., 2013, 11, 2772 DOI: 10.1039/C3OB00043E

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