Peptide molecules have been studied as one of most promising self-assembly materials because they are not only composed of over tens of natural or non-natural amino acids, but also have limitless and designable sequence combinations of amino acids for the various self-assembled nanostructures. It is commonly known that main driving forces for self-assembly of biomolecules are non-covalent bonding such as Van der Waals force, electrostatic interaction, hydrophobic interaction, hydrogen bonding, π-π interaction, etc. and their harmonic combinations. Meanwhile, awful discovery of catalytic properties of novel metal nanoparticles expanded their biomedical applicability as an artificial enzyme. Nanocrystals of Au, Pt, Pd, etc. can replace the representative redox enzymes such as peroxidase, oxidase, reductase, etc. and they have been mainly applied to the various types of biosensor platforms. In this study, we introduce the peptide self-assembled nanostructures coupled with gold nanocrystals and their intrinsic catalytic performances. The peptide for self-assembly is one of tyrosine-rich peptide(TRP) composed of 7 amino acids, which facilely transforms to the variety of self-assembled nanostructures induced by metal ion, representatively gold ion under specific temperature and buffer conditions. Besides, gold nanocrystals are well-known as the peroxidase-like nanocatalyst as well as the nanocatalyst that can facilitate chemical reducing agents. We can expect that the coupling of gold nanocrystal with self-assembly of TRP accomplish the proton-coupled electron transfer (PECT) effect related with improving kinetics and lowering the activation energy. To evaluate catalytic activity of peptide self-assembled nanostructures coupled with gold nanocrystals, they were applied to the reduction of p-nitrophenol as the chemical catalyst and TMB oxidation instead of any peroxidase as the novel biocatalyst for the biosensors.

Gold nanostructures stabilized with peptide self-assembly for chemical and biological applications

251st National Meeting (2016)

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