The 1st International Symposium On “Molecular Engine”
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Chiba University
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Nature proteins have assembled in various shapes of a ring, a cage, tubular fibril, etc., which leads to the specific function of each protein assembly pattern. Inspiring from that, many researchers have discovered new methods to modify protein at the molecular level to prepare new biomaterial by protein assemblies. Recently, our group has developed a new strategy for the construction of new artificial protein material from protein crystal using the cross-linking technique. Through the rational cysteine mutants, the precise disulfide bonds formed within the protein crystal. The cross-linked crystals were then dissolved to obtain the designed assembly such as the protein cage from polyhedra crystals synthesised in insect cell [1] or tubular protein from RubisCO crystals from in vitro [2]. In this study, we utilised the crystals of Trypanosoma brucei cysteine protease cathepsin B (TbCatB) synthesised in insect cells to build the fibril protein. Several sets of cysteine mutants were introduced to TbCatB protein. After collecting crystals of various TbCatB mutants and dissolving the crystals at low pH (lower than pH 4), the stable filament protein has obtained.
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