Alkyl chain length-dependent protein nonadsorption and adsorption properties of crystalline alkyl β-celluloside assemblies.

Cellulose-based crystalline assemblies artificially constructed in a bottom-up manner are attracting increasing attention as chemically stable and functionally designable nano- to macroscale materials. However, basic knowledge of how such crystalline assemblies interact with biomolecules and how to control them via molecular design is still limited. In this study, we investigated the protein adsorption properties of crystalline lamella assemblies composed of alkyl β-cellulosides (namely, ethyl, n-butyl, and n-hexyl β-cellulosides) or plain cellulose, which all have an antiparallel molecular arrangement.