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Inorganic Design of Protein Assemblies as Supramolecular Platforms

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Abstract

In the last decade, there has been great deal of progress in the study of self-assembly processes of protein assemblies as biotemplates to create and construct one-dimensional arrays of nanocrystalline metals and semiconductors. Successful attempts in fabricating the protein-based bioelectronics could serve as a promising alternative to synthetic template based nanomaterials. Another perspective of protein assemblies is its use in the field of tissue engineering either as scaffold for cell adhesion and proliferation or as a foreign (bio)nanofunctionality to communicate with the macromolecules present in the extracellular or intracellular milieu and participate in the precise control of vital cell functions. Three-dimensionally arranged protein monomers to form bionanotubes are promising in terms of innate biocompatibility, easy bio-conjugation to incorporate multiple functionalities and well-defined nano-scale lengths. Such unique chemical properties of protein assemblies are described in this review.

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Authors and Affiliations

  1. Institute for Integrated Cell-Material Sciences, Kyoto University, Yoshida, Sakyo-ku, Kyoto, 606-8501, Japan

    Nusrat J. M. Sanghamitra & Susumu Kitagawa

  2. Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan

    Hiroshi Inaba & Susumu Kitagawa

  3. Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama, 226-8501, Japan

    Takafumi Ueno

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  1. Nusrat J. M. Sanghamitra
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  2. Hiroshi Inaba
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  3. Susumu Kitagawa
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  4. Takafumi Ueno
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Correspondence to Takafumi Ueno.

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This paper is dedicated to Prof. Dr. Hiroshi Nishihara for his outstanding contribution to the field of metal-containing polymers.

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Sanghamitra, N.J.M., Inaba, H., Kitagawa, S. et al. Inorganic Design of Protein Assemblies as Supramolecular Platforms. J Inorg Organomet Polym 23, 50–60 (2013). https://doi.org/10.1007/s10904-012-9728-2

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