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This study proposed a network model for the cross-linked structure of keratin-associated proteins in hair and wool fibers, suggesting notable differences between the two, potentially affecting hair fiber elasticity.

This study observed that repeated perm treatments decrease disulfide bonds in hair due to their conversion largely into cysteic acid, affecting the waving efficiency depending on the reduction agent used.

This study found that novel thiol-reactive cross-linking agents, particularly APA, significantly improved the tensile strength and elasticity of human hair fibers by effectively regenerating disulfide bridges, with potential applications for advanced hair repair treatments in the cosmetic industry.

This study provides insight into the specific disulfide bond interactions between keratins and keratin associated proteins, suggesting non-random cysteine interactions crucial for stabilizing hair fiber structure.

In this study, treatment with aqueous KCN selectively converted disulfide bonds to monosulfide crosslinks in hair, leading to changes in microstructural properties and rubberlike elasticity under specific laboratory conditions.