Disulfide bond in keratin (null)

Disulfide bonds in keratin refer to covalent connections formed between the thiol (-SH) groups of cysteine residues within keratin polypeptides, resulting in cystine linkages. These bonds are critical for the assembly, organization, and mechanical strength of keratin intermediate filaments in structures such as hair, skin, nails, wool, and other epidermal appendages[1][2][3][4][7]. The extensive network of disulfide bonds in keratin stabilizes its structure, confers rigidity and flexibility, and allows keratin-rich tissues to resist mechanical stress[4][7]. The disruption or modification of these bonds underlies common cosmetic procedures (such as hair perming), as well as genetic and acquired structural disorders of the skin and hair[1][2][5]. Disulfide bonds are a property of the polymer matrix, not an isolated target for small molecule therapeutics, although they can be chemically manipulated[5]. Keratin disulfide bonding underpins the toughness of materials such as horn, wool, and human hair and is regulated dynamically during keratin filament formation and tissue differentiation[1][3][4][7].

Other names

Disulphide bonds in α-keratindisulfide linkage in keratincystine bridges in keratin

Redox reactions that reduce (break) or oxidize (reform) disulfide bonds in keratin, altering physical properties (e.g., texture, curliness of hair)