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Site‐Selective Disulfide Modification of Proteins: Expanding Diversity beyond the Proteome
Author(s) -
Kuan Seah Ling,
Wang Tao,
Weil Tanja
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201602298
Subject(s) - proteome , disulfide bond , diversity (politics) , posttranslational modification , computational biology , chemistry , biochemistry , biology , enzyme , sociology , anthropology
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.