Assembly and Biomineralization of Polymorphic Gold-Peptide Superstructures Using Tyrosine-Rich Short Peptides

초록

Peptides show tremendous promise in synthesizing metal-peptide superstructures with tailored shapes and functions. However, bottom-up control of the polymorphs of these superstructures using a single short peptide without molecular modification has not been mechanistically clarified. Therefore, an approach to constructing gold-peptide superstructures with unprecedented structural diversity using a tyrosine-rich short peptide is developed, based on the assembling and mineralizing attributes of tyrosine. One-step UV irradiation of peptide/gold-salt systems enables on-site mineralization of gold ions, permitting controlled solvent-dependent fabrication of various superstructures. 0D colloids, 2D sheets, 3D superspheres, and 3D hollow capsules are produced via one-pot reactions in a pH-10 buffer, at the interface of a toluene-water biphasic system, in water, and in toluene-in-water emulsions, respectively, whereas 1D rod/fibril structures are produced using rapidly assembling peptides (A, F, I, L, N, V, Y, and D as X in YY-X-YY) in a two-step process. Several peptide derivatives, which also exhibit assembling and biomineralizing abilities and form various superstructures, validate the functionality of the tyrosine-rich peptide. This study sheds light on the design and development of diverse gold-peptide superstructures for applications including catalysis, sensing, imaging, and photothermal therapy.

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