Thiol-containing protein or peptide

Thiol-containing proteins and peptides are defined by the presence of cysteine residues whose side chains bear a thiol (–SH) group[2][6][7]. These thiols are essential for many core biological processes, including antioxidant defense (e.g., glutathione), protein folding via disulfide bond formation, enzymatic catalysis (where cysteine often acts as a reactive nucleophile in active sites), redox signaling, and metal ion coordination[2][3][6]. The structural and functional diversity of thiol-containing proteins allows them to participate in numerous biological pathways, but their identity as a "target" is non-specific: they represent a chemical class, not a single molecular entity. Disruption or modification of protein thiols can contribute to a wide range of diseases—from neurodegeneration to cancer—and many drugs or toxins act by covalently modifying these functional groups[2][3][6][7].

Other names

Sulfhydryl-containing proteinscysteine-containing proteinsSH-containing proteinsthiol-rich proteins

Covalent modification of –SH groups (alkylation, oxidation, metal binding); Redox modulation (altering the oxidative state of thiols); Disulfide bond disruption or formation; Chelation of metal ions