Controlling Mineralization with Protein-Functionalized Peptoid Nanotubes

摘要

Sequence-defined foldamers that self-assemble into well-defined architecturesare promising scaffolds to template inorganic mineralization. However,it has been challenging to achieve robust control of nucleation andgrowth without sequence redesign or extensive experimentation. Here,peptoid nanotubes functionalized with a panel of solid-binding proteins areused to mineralize homogeneously distributed and monodisperse anatasenanocrystals from the water-soluble TiBALDH precursor. Crystallite size issystematically tuned between 1.4 and 4.4 nm by changing protein coverageand the identity and valency of the genetically engineered solid-bindingsegments. The approach is extended to the synthesis of gold nanoparticlesand, using a protein encoding both material-binding specificities, tothe fabrication of titania/gold nanocomposites capable of photocatalysisunder visible-light illumination. Beyond uncovering critical roles for hierarchicalorganization and denticity on solid-binding protein mineralizationoutcomes, the strategy described herein should prove valuable for thefabrication of hierarchical hybrid materials incorporating a broad range ofinorganic components.