Strategies for improved hair binding: Keratin fractions and the impact of cationic substructures

Keratin extracts and hydrolysates from varying sources, their chemical modifications and compositions thereof have shown potential in the restoration of hair properties. Within this study on reactivity of thiol groups and the shielding effect of anionic charges the binding of keratin-associated proteins (KAP) and α-keratins (Ker) extracted from human hair to natural and permed hair fibers was evaluated. Selectively extracted KAP and Ker were preactivated with 6-mercaptonicotinamide in a quantity of 194 ± 21 μmol/g for KAP and 169 ± 27 μmol/g for Ker resulting in 1.9- and 1.4-fold enhanced binding to natural hair, respectively. The amount of accumulated Ker on hair fibers was furthermore increased by 1.7-fold in presence of 25 mM L-arginine. Perming of hair impaired binding characteristics of Ker with negligible effects for preactivation, whereas unmodified and preactivated KAP showed results comparable to natural hair. Strongly enhanced penetrability after perming was reflected by the mean penetration depth for fluorescein of 25 μm compared to 5 μm for natural fibers.