A first-principles examination of the ice–cellulose interface: towards bioinspired antifreeze design

Abstract

Examination of binding of cellulose to ice using ab initio modeling reveals that new C–O bonds are formed on the basal ice surfaces, where some of the O atoms are exposed at the surface due to missing H bonds. Further analysis suggests that the cellulose unit binds in such a way as to form a tetrahedral arrangement at the ice surface, evidenced by a geometric measure of tetrahedrality. This hypothesis is further validated for both primary and secondary prismatic planes. This leads us to conclude that in the case of cellulose molecules, binding at ice is dependent on preserving its tetrahedral bonding arrangement. Our findings suggest that the idea of tetrahedrality is very widely applicable to coordination ranging from water to ice-binding proteins, highlighting a design criterion for novel ice-binding/antifreeze proteins/materials.