Construction of Robust Bio-nanotubes using the Controlled Self-Assembly of Component Proteins of Bacteriophage T4
Construction of Robust Bio-nanotubes using the Controlled Self-Assembly of Component Proteins of Bacteriophage T4
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DOI：
10.1002/smll.201000772
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发表时间：
2010-09-06
期刊：
影响因子：
13.3
通讯作者：
Ueno, Takafumi
中科院分区：
文献类型：
--
作者：
Yokoi, Norihiko;Inaba, Hiroshi;Ueno, Takafumi
横井纪彦、稻叶浩、寺内诚、Adam Z. Stieg、Nusrat JM Sanghamitra、Tomomi Koshiyama、Katsuhide Yutani、Shuji Kanamaru、Fumio Arisaka、Tatsuo Hikage、Atsuo Suzuki、Takashi Yamane、James K. Gimzewski、 Yoshihito Watanabe、Susumu Kitakawa 和 Takafumi Ueno* 在适当位点的功能分子。因此，获得具有高稳定性和明确的纳米级长度的管结构以在纳米管表面上正确排列合成分子仍然具有挑战性。 β-螺旋蛋白基序有望成为克服这些问题的候选者。该基序主要出现在天然管状结构蛋白中，例如抗冻蛋白、朊病毒和病毒。[24-26]β-螺旋结构已被使用短肽或聚合物缀合肽人工模拟，因为该基序通常由易于操作的短周期的高度重复片段组成。[27, 28]该基序也存在于 噬菌体T4，最常见的生物超分子之一，由40多种成分蛋白组成（方案1）。 [29]三链β-螺旋组装体由基因产物5 ((gp5) 3) 的三个亚基组成。该组件位于噬菌体 T4 的基板上，起到穿透大肠杆菌宿主生物体表面膜的针的作用。 [29, 30] 鉴于其超分子
Norihiko Yokoi, Hiroshi Inaba, Makoto Terauchi, Adam Z. Stieg, Nusrat JM Sanghamitra, Tomomi Koshiyama, Katsuhide Yutani, Shuji Kanamaru, Fumio Arisaka, Tatsuo Hikage, Atsuo Suzuki, Takashi Yamane, James K. Gimzewski, Yoshihito Watanabe, Susumu Kitagawa, and Takafumi Ueno* of functional molecules at appropriate sites. Thus, it has remained challenging to obtain tube structures with high stability and well-defined nanoscale lengths for properly aligning synthetic molecules on the surfaces of the nanotubes. The β-helical protein motif holds promise as a candidate to overcome these problems. This motif occurs predominantly in native tubular structural proteins such as antifreeze proteins, prions, and viruses.[24–26] β-helical structures have been artificially mimicked using short or polymer-conjugated peptides because the motif typically consists of highly repeated fragments with a short period that can be easily manipulated.[27, 28] This motif is also found in a component protein of bacteriophage T4, one of the most common bio-supramolecules, which consists of more than 40 component proteins (Scheme 1).[29] The triple-stranded β-helical assembly is composed of three subunits of gene product 5 ((gp5) 3). This assembly is located on the base plate of bacteriophage T4, and functions as a needle for penetrating the surface membrane of the E. coli host organism.[29, 30] In view of its supramolecular