Enzymatic synthesis and protein adsorption properties of crystalline nanoribbons composed of cellulose oligomer derivatives with primary amino groups.

The in vitro enzymatic synthesis of cellulose and its derivatives has attracted growing interest for fabricating novel cellulose-based supramolecular assemblies with unique physicochemical and functional properties. However, their potential biomedical applications have not been sufficiently demonstrated despite their useful features of designable structures and tailor-made surface functionalities. Herein, we demonstrated the production of crystalline nanoribbons composed of cellulose oligomer derivatives with primary amino groups via cellodextrin phosphorylase-catalyzed single-step reactions using α-d-glucose l-phosphate monomers and 2-aminoethyl-β-d-glucoside primers. Then, the fundamental properties of protein adsorption onto the surface-aminated nanoribbons were systematically investigated. It was found that the primary amino groups on the nanoribbon surfaces effectively attracted negatively charged proteins but not positively charged ones. Furthermore, it was demonstrated that the nanoribbons did not show apparent cytotoxicity against cultured cells. Taken together, our findings open a new avenue for the facile production of cellulose-based supramolecular assemblies with tailor-made functionality for future biomedical applications.