Homo- and Heteropolymer Self-Assembly of Recombinant Trichocytic Keratins

In this study, researchers explored the bacterial expression, purification, and solution characterization of recombinant human hair keratins K31 and K81. They found that these recombinant proteins maintained the ability to form intermediate filaments through obligate heterodimerization. Additionally, they observed novel zero- and one-dimensional nanostructures from the homooligomerization of K81 and K31, respectively. The study highlighted the significance of disulfide crosslinking in the self-assembly of keratins, suggesting that recombinant keratins could overcome the limitations of natural keratins, such as unwanted by-products and limited sequence tunability, while retaining their beneficial properties for applications in tissue engineering, wound healing, and nerve regeneration.