In this study, we demonstrate the use of a noncovalent, molecular recognition strategy to enable site-specific protein templating using a self-assembling protein, clathrin. We have previously reported the use of a heterogeneous protein-protein interaction to create a molecular bridge between the clathrin protein interface and inorganic materials. This interaction was achieved by designing bi-functional peptides that fuse a �clathrin-box� recognition sequence upstream of inorganic-binding sequences. This strategy enabled a variety of inorganic materials to interface with the clathrin protein without requiring any direct chemical or genetic modifications. In our current work, we show that two distinct epitopes on the clathrin protein, the clathrin-box and the W-box, can be successfully used with this biotemplating strategy, creating a versatile and modular platform for biotemplating reactions. This work also opens up the possibility of future simultaneous, heterogeneous nucleation of multiple inorganic materials on a single protein biotemplate with site-specificity for each inorganic species.

Molecular recognition enables biotemplating at distinct protein sites

243rd National Meeting (2012)

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