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

R.P. Temming, L.J. Eggermont, M.B. van Eldijk, J.C.M. van Hest, F.L. van Delft

Research output: Contribution to journalArticleAcademicpeer-review

27 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2772-2779
Number of pages8
JournalOrganic & Biomolecular Chemistry
Volume11
Issue number17
DOIs
Publication statusPublished - 7 May 2013
Externally publishedYes

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