Screening of Oligopeptides that Recognize Inorganic Crystalline Facets of Metal Nanoparticles.

Abstract

Peptides that possess specific affinity to distinct crystal facets have been reported previously. However, their adsorption behavior in terms of the crystal sizes and shapes is less exploited. Herein, we isolate several phage clones that show the strong affinity to {100} of Pd at a neutral pH from the M13 phage library, and among them the phages that have shape selectivity to the cubic structure are identified by eliminating ones that bind randomly shaped Pd nanoparticles (NPs). Since Pd nanocube-binding phages are eluted by lowering pH values in the biopanning process, the selected phages (and their binding peptides displayed on protein pIII) can be released from Pd surfaces through pH changes. We used this feature to modulate the capping density of selected peptides on NPs. For example, when less peptides are capped on Pd nanocubes by lowering the pH values, the shape of the nanocubes is deformed and some evolve into a concave shape, indicating that Pd atoms are released from the less protected {100} facet selectively due to the higher surface energy. This type of crystalline facet-recognizing peptides can be applied for smart capping agents that not only bind target crystalline planes, but also modify their coverage on the specific surfaces with pH changes. The peptide-capping agents could be useful to fabricate NPs with characteristic shapes through etching and adsorption of atoms on specific crystalline planes of seed nanocrystals.