Investigation of High-Cellulose-Affinity Polymers with Pendant Amino Acids and Their Binding Properties in Water

Cellulose is an abundant and sustainable natural polymer with potential for advanced applications. Although high-cellulose-affinity molecules, such as carbohydrate-binding modules (CBMs) found in glycosidases, including cellulases, have been extensively studied, synthetic polymers that mimic CBM-like affinity remain largely unexplored. This study investigated the binding behavior of synthetic polymers with pendant amino acid moieties toward cellulose using surface plasmon resonance (SPR). A polymer series, with varying types and degrees of amino acid methyl ester substitution, was synthesized and evaluated using SPR with cellulose in water. Polymers bearing histidine, phenylalanine, leucine, and isoleucine moieties exhibited high affinity. Their equilibrium dissociation constants were in the micromolar range, confirming strong and specific binding.