Nature has evolved numerous methods for the self-assembly of nanoscale architectures such as DNA and proteins with high levels of precision. This reproducibility makes them attractive for use as templates for the patterning of inorganic nanostructures. To date, much attention in biotemplating has been focused on 0-D or 1-D structures. Proteins offer an immense library of naturally available architectures and assembly schemes that will make 2-D and 3-D patterning possible. The intracellular transport protein clathrin assembles into higher order structures that offer access to a variety of architectures, both in 2-D and 3-D, depending on the environmental conditions (pH, concentration, buffer ionic strength) during assembly. The ability of this single protein to assemble into multiple structures makes clathrin an ideal model system for investigating the underlying kinetic and thermodynamic principles of self-assembly which will lead to the ability to create a variety of templates from one starting material. To interface these biological templates with inorganic materials, we design bi-functional peptide linkers that serve as molecular bridges between the clathrin protein and inorganic materials. By designing a family of bi-functional peptides, we will develop a flexible, modular system for biotemplating multiple materials onto a single protein template making this approach applicable to a broad range of applications.

Clathrin: A protein-based scaffold for biotemplating 2D and 3D nanostructures

239th National Meeting (2010)

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