Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor
Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor
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DOI:
10.1002/smll.200700855
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发表时间:
2008-01-01
期刊:
影响因子:
13.3
通讯作者:
Watanabe, Yoshihito
中科院分区:
文献类型:
--
作者:
Koshiyama, Tomomi;Yokoi, Norihiko;Watanabe, Yoshihito
Bioarchitectures containing synthetic molecules are very attractive candidates for the construction of catalysts, sensors, and materials with novel properties.[1–11] Protein self-assemblies are especially suitable for these purposes because they can lead to various different nanoscale cage architectures. For example, protein assemblies such as viruses (eg, Cowpea chlorotic mottle virus and Tobacco mosaic virus), chaperonin, and ferritin are known to be able to accommodate metal nanoparticles in their protein cages.[6, 8, 12, 13] Additionally, the covalent conjugation of fluorescence probes, metal complexes, and drugs on protein surfaces has been examined.[7, 9, 14–17] While these assemblies are very useful for the organization of various functions, it is difficult to control the number and stability of the molecules attached on the protein surfaces.We have investigated the use of a unique cage as a catalytic reaction space. This cage consists of a heteroprotein assembly that is a trimer of gene product 27 and gene product 5,(gp27-gp5) 3, isolated from bacteriophage T4 (Figure 1).[18] This protein assembly of bacteriophageT4