Abstract
One effective solution in the analysis of complex mixtures, including protein or cell hydrolysates, is based on chemoselective derivatization of a selected group of compounds by using selective tags to facilitate detection. Another method is based on the capture of the desired compounds by properly designed solid supports, resulting in sample enrichment. Cysteine is one of the rarest amino acids, but at least one cysteine residue is present in more than 91% of human proteins, which clearly confirms its important role in biological systems. Some cysteine-containing peptides may serve as significant molecular biomarkers, which may emerge as key indices in the management of patients with particular diseases. In the current review, we describe recent advances in the development of cysteine-containing peptide modification techniques based on solution and solid phase derivatization and enrichment strategies.
Highlights
Investigation of peptide and protein biomarkers of cellular and tissue proteomes is limited, due to the complex nature of the samples
The thiol group of cysteine shows high reactivity—it is active redox and has strong nucleophilic properties—resulting from the large atomic radius of sulfur and the low dissociation energy of the thiol bond [6]
Investigation of peptide and protein biomarkers of cellular and tissue proteomes is limited by the complex nature of the samples
Summary
Investigation of peptide and protein biomarkers of cellular and tissue proteomes is limited, due to the complex nature of the samples. The development of enrichment methods for some groups of peptides, based on chemoselective fractionation or derivatization is an important task which may facilitate proteomics studies [1,2]. The cysteine residue plays an important role in the structure of proteins. Among other things, it is responsible for binding metal ions and holding them in place. The cysteine side chain (sulfhydryl) functional group can be oxidized, leading to the formation of a disulfide bridge between the two cysteines, which strengthens the tertiary and quaternary structures of the protein. The thiol group of cysteine shows high reactivity—it is active redox and has strong nucleophilic properties (the most nucleophilic group among the functional groups of amino acids [5])—resulting from the large atomic radius of sulfur and the low dissociation energy of the thiol bond [6]. Strong nucleophilic properties make cysteine modified by electrophilic and thiol-disulfide reagents
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