Journal
CHEMBIOCHEM
Volume 17, Issue 7, Pages 529-553Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201500667
Keywords
chemical protein modification; cysteine; proteins; site-selectivity; sulfur
Funding
- IWT (Agentschap voor Innovatie door Wetenschap en Technologie)
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The modification of proteins with non-protein entities is important for a wealth of applications, and methods for chemically modifying proteins attract considerable attention. Generally, modification is desired at a single site to maintain homogeneity and to minimise loss of function. Though protein modification can be achieved by targeting some natural amino acid side chains, this often leads to ill-defined and randomly modified proteins. Amongst the natural amino acids, cysteine combines advantageous properties contributing to its suitability for site-selective modification, including a unique nucleophilicity, and a low natural abundanceboth allowing chemo- and regioselectivity. Native cysteine residues can be targeted, or Cys can be introduced at a desired site in a protein by means of reliable genetic engineering techniques. This review on chemical protein modification through cysteine should appeal to those interested in modifying proteins for a range of applications.
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