Through biocombinatorial techniques, peptides have been isolated with affinity for inorganic materials; however, the interactions by which these sequences recognize and bind their target surfaces is not fully understood. Furthermore, exploiting these interactions is possible, leading to advanced functionalities. We have employed the Pd-specific Pd4 peptide to generate peptide monolayer-capped Pd nanocatalysts that are functional under non-traditional ambient conditions. Via site-selective amino acid substitutions of alanine and cysteine, multiple correlations between the peptide sequence and the nanoparticle size and catalytic activity are observed. These results suggest that unique peptide-surface interactions may occur to facilitate inorganic surface binding and stability of the nanoparticles, which could be exploited to enhance/optimize the catalytic functionality. These results are significant as they begin to elucidate peptide-metal interactions that are critical for bio-inspired materials, which could lead to the development of highly specific and functional biotic-abiotic interfaces at the atomic level.

Exploiting peptide sequence effects to enhance the catalytic reactivity of nanoparticles

245th National Meeting (2013)

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