2-mercaptonicotinic-acid and sodium-borohydride

Restoration of damaged hair structure by replacing lost keratin is still of paramount interest. On account of the fact that native keratin is a highly cross-linked protein with numerous disulfide bonds but just a few nucleophilic thiol groups, binding affinity to hair is comparatively low. Hence, the design of reactive keratin derivatives bearing free sulfhydryl groups that are optionally S-protected and preactivated should enhance permanent binding to hair fibers.. Keratin was extracted from human Caucasian hair and reduced with NaBH. Both modifications induced higher affinity of keratin to hair fibers, resulting in up to 1.7-fold (keratin-MNA) improved binding to natural hair and up to 3.6-fold (keratin-MNA) improved binding to bleached hair. Confocal laser microscopy confirmed the accumulation of keratin derivatives in distinct regions of the cuticle layer. Thiol functionalization seems therefore to be a promising strategy for efficient durable binding of keratin to hair.

Topics: Borohydrides; Hair; Humans; Keratins; Nicotinic Acids; Optical Imaging; Protein Binding; Sulfhydryl Compounds