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Updated: May 16, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
Expanding coordination chemistry from protein to protein assembly
Nusrat J M Sanghamitra1, Takafumi Ueno
1Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Yoshida, Kyoto 606-8501, Japan.
Abstract:
Bioinorganic chemistry is of growing importance in the fields of nanomaterial science and biotechnology. Coordination of metals by biological systems is a crucial step in intricate enzymatic reactions such as photosynthesis, nitrogen fixation and biomineralization. Although such systems employ protein assemblies as molecular scaffolds, the important roles of protein assemblies in coordination chemistry have not been systematically investigated and characterized. Many researchers are joining the field of bioinorganic chemistry to investigate the inorganic chemistry of protein assemblies. This area is emerging as an important next-generation research field in bioinorganic chemistry. This article reviews recent progress in rational design of protein assemblies in coordination chemistry for integration of catalytic reactions using metal complexes, preparation of mineral biomimetics, and mechanistic investigations of biomineralization processes with protein assemblies. The unique chemical properties of protein assemblies in the form of cages, tubes, and crystals are described in this review.
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