Selective and reversible photochemical derivatization of cysteine residues in peptides and proteins?

Chemical Science Pub Date: 2014-01-02 DOI: 10.1039/C3SC51691A

Abstract

The selective derivatization of solvent-exposed cysteine residues in peptides and proteins is achieved by brief irradiation of an aqueous solution containing 3-(hydroxymethyl)-2-naphthol derivatives (NQMPs) with a 350 nm fluorescent lamp. NQMP can be conjugated with various moieties, such as PEG, dyes, carbohydrates, or possess a fragment for further selective derivatization, e.g., biotin, azide, alkyne, etc. Attractive features of this labeling approach include an exceptionally fast rate of the reaction and a requirement for a low equivalence of the reagent. The NQMP-thioether linkage is stable under ambient conditions, and survives protein digestion and MS analysis. Irradiation of an NQMP-labeled protein in a dilute solution (<40 μM) or in the presence of a vinyl ether results in a traceless release of the substrate. The reversible biotinylation of bovine serum albumin, as well as the capture and release of this protein using NeutrAvidin Agarose resin beads has been demonstrated.

Graphical abstract: Selective and reversible photochemical derivatization of cysteine residues in peptides and proteins
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