Structure-property relationships of meta-kerateine biomaterials derived from human hair.

Abstract

The structure-property relationships of kerateine materials were studied by separating crude hair extracts into two protein sub-fractions, referred to as α- and γ-kerateines, followed by their de novo recombination into meta-kerateine hydrogels, sponges and films. The kerateine fractions were characterized using electrophoresis and mass spectrometry, which revealed that the α-fraction contained complexes of type I and type II keratins and that the γ-fraction was primarily protein fragments of the α-fraction along with three proteins of the KAP-1 family. Meta-kerateine materials with increased amounts of γ-kerateines showed diminished physical, mechanical and biological characteristics. Most notably, materials with higher γ-content formed less elastic and less solid-like hydrogels and sponges that were less hydrolytically stable. In addition, a model biological assay showed that meta-kerateine films with greater amounts of γ-kerateines were less supportive of hepatocyte attachment. Investigation into the mechanism of attachment revealed that hepatocyte adhesion to meta-kerateines is not mediated by the β1 integrin subunit, despite the presence of LDV binding motifs within the type I α-keratins. This work to define the role of protein composition on biomaterial function is essential for the optimization of keratin biomaterials for biomedical applications.