Terminal Tryptophan-Directed Anisotropic Self-Assembly for Precise Protein Nanostructure Regulation

A common challenge in nanotechnology is synthesizing nanomaterials with well-defined structures. In particular, it remains a major unresolved challenge to precisely regulate the structure and function of protein nanomaterials, which are structurally diverse, highly ordered, and complex and offer an innovative means that enables a high performance in various nanodevices, which is rarely achievable with other nanomaterials. Here an innovative approach is proposed to fabricating multi-dimensional (0- to 3D) protein nanostructures with functional and structural specialties via molecular-level regulation. This approach is based on a stable, consistent, anisotropic self-assembly of Tobacco mosaic virus (TMV) coat protein-derived engineered building blocks where genetically added tryptophan residues are externally tailored. The unique structural characteristics of each nanostructure above are demonstrated in detail through various analyses (electron microscopy, atomic force microscopy, dynamic light scattering, and small-angle X-ray scattering) and further investigated through molecular dynamics simulations, indicating that this control, anisotropic, and molecular assembly-based approach to regulating protein nanostructures holds great potential for customizing a variety of nanomaterials with unique functions and structures.