Mechanistic insights into silk fibroin's adhesive properties via chemical functionalization of serine side chains.

Bombyx mori-derived silk fibroin (SF) has recently gained interest for its intrinsic or engineered adhesive properties. In a previous study by our group, the mechanism of the protein's intrinsic adhesiveness to biological substrates such as leather has been hypothesized to rely on hydrogen bond formation between amino acid side chains of SF and the substrate. In this study, the serine side chains of SF were chemically functionalized with substituents with different hydrogen bonding abilities. The effect of these changes on adhesion to leather was investigated along with protein structural assessments. The results confirm our hypothesis that adhesive interactions are mediated by hydrogen bonds and indicate that the length and nature of the side chains are important for both adhesion and secondary structure formation.