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… Click to show full abstract
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.
               
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