title: Chemical Protein Modification through Cysteine.
abstract: 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 abundance--both 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.
authors.affiliation: Organic & Biomimetic Chemistry Research Group, Department of Organic and Macromolecular Chemistry, Ghent University, Krijgslaan 281, 9000, Gent, Belgium.
authors.forename: Smita B
authors.initials: SB
authors.lastname: Gunnoo
authors.affiliation: Organic & Biomimetic Chemistry Research Group, Department of Organic and Macromolecular Chemistry, Ghent University, Krijgslaan 281, 9000, Gent, Belgium. annemieke.madder@ugent.be.
authors.forename: Annemieke
authors.initials: A
authors.lastname: Madder
mesh_terms: D003545:Cysteine / Q000737:chemistry / Q000378:metabolism*; D008301:Maleimides / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008301:Maleimides; D011506:Proteins; C043592:maleimide; D003545:Cysteine
keywords: chemical protein modification; cysteine; proteins; site-selectivity; sulfur