Star-like Supramolecular Complexes of Reducing-End-Functionalized Cellulose Nanocrystals

In this work, we take advantage of the parallel organization of cellulose chains in cellulose I yielding an inherent chemical asymmetry of cellulose nanocrystals, i.e., reducing vs nonreducing end, to selectively modify only one end of these rigid rodlike crystals to be used as a linking point for the formation of supramolecular structures. We have prepared biotin-functionalized tunicate cellulose nanocrystals at the reducing end capable of forming new complex supramolecular hierarchies by the addition of the protein streptavidin. Biotin-streptavidin coupling was chosen because streptavidin has a multivalency of four and the biotin-streptavidin bond is known to be highly selective and stable. Hence, streptavidin molecules would link up to four cellulose nanocrystals through their biotin-modified reducing end. Two biotin derivatives were studied, consisting of an anchoring group, i.e., amine or hydrazine; the biotin moiety; and the linker between them. Results show that the length of the linker significantly affects the bond between the biotinylated cellulose nanocrystals and streptavidin, and a certain chain length is necessary for the supramolecular assembly of several cellulose nanocrystals by streptavidin.