PNNL

Abstract

The exquisite self-assembly of proteins and peptides in nature into highly ordered functional materials has inspired innovative approaches to biomimetic materials design and synthesis. Here we report the assembly of peptoids—a class of highly stable sequence-defined synthetic polymers—into biomimetic materials on mica surfaces. The assembling 12-mer peptoid contains alternating acidic and aromatic residues, and the presence of Ca2+ cations creates peptoid-peptoid and peptoid-mica interactions that drive assembly. In situ atomic force microscopy (AFM) shows that peptoids first assemble into discrete nanoparticles, these particles then transform into hexagonally-patterned nanoribbons on mica surfaces. AFM-based dynamic force spectroscopy (DFS) studies show that peptoid-mica interactions are much stronger than peptoidpeptoid interactions in the presence of Ca2+, illuminating the physical parameters that drive peptoid assembly. We further demonstrate the display of functional groups at the N-terminus of assembling peptoid sequence to produce biomimetic materials with similar hierarchical structures. This research demonstrates that surface-directed peptoid assembly can be used as a robust platform to develop biomimetic coating materials for applications.