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Updated: Jan 16, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Cerium-mediated site-selective cysteine functionalization
1Department of Chemistry, Seoul National University Seoul 08826 Republic of Korea woonjusong@snu.ac.kr.
Abstract:
The chemical roles of lanthanides in biology are increasingly recognized, yet remain largely unexplored. Unlike most lanthanides, cerium is redox-active and readily adapted for chemical transformation. Herein, we report a cerium-mediated oxidative thiol-ene coupling between cysteine-derived thiols and styrenes under aqueous conditions, yielding β-hydroxysulfide products. Building on this reactivity, we developed a site-selective cysteine modification strategy using a 17-amino acid cerium-binding sequence. Only cysteines optimally positioned near the vacant coordination site undergo efficient and rapid labeling, particularly with electron-deficient styrene derivatives. This work demonstrates cerium-mediated biological activity and highlights its potential as a reactive center for site-selective bioconjugation and broader biochemical and synthetic applications.
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