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Chemistry. 2016 Nov 21;22(48):17112-17129. doi: 10.1002/chem.201602298. Epub 2016 Oct 25.

Site-Selective Disulfide Modification of Proteins: Expanding Diversity beyond the Proteome.

Kuan SL1,2, Wang T1,3, Weil T1,2.

Author information

1
Institute of Organic Chemistry III, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
2
Max Planck Institute for Polymer Research, Ackermannweg 10, 55128, Mainz, Germany.
3
School of Materials Science and Engineering, Southwest Jiaotong University, Chengdu, 610031, P.R. China.

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.

KEYWORDS:

bioactive hybrids; disulfide rebridging; drug delivery; multimodal proteins; site-selective protein modifications

PMID:
27778400
PMCID:
PMC5600100
DOI:
10.1002/chem.201602298
[Indexed for MEDLINE]
Free PMC Article

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