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Updated: Mar 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Site-Selective Disulfide Modification of Proteins: Expanding Diversity beyond the Proteome
Seah Ling Kuan1,2, Tao Wang1,3, Tanja Weil1,2
1Institute of Organic Chemistry III, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
Abstract:
The synthetic transformation of polypeptides with molecular accuracy holds great promise for providing functional and structural diversity beyond the proteome. Consequently, the last decade has seen an exponential growth of site-directed chemistry to install additional features into peptides and proteins even inside living cells. The disulfide rebridging strategy has emerged as a powerful tool for site-selective modifications since most proteins contain disulfide bonds. In this Review, we present the chemical design, advantages and limitations of the disulfide rebridging reagents, while summarizing their relevance for synthetic customization of functional protein bioconjugates, as well as the resultant impact and advancement for biomedical applications.
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