Kumara Mudalige Thilak, Srividya Narayanan, Muralidharan Subra, Tripp Brian C
Department of Chemistry and Nanotechnology Research and Computation Center, Western Michigan University, Kalamazoo, Michigan 49008-5410, USA.
Nano Lett. 2006 Sep;6(9):2121-9. doi: 10.1021/nl060598u.
An E. coli flagellin protein, termed FliTrx, was investigated for use as a novel form of self-assembling protein nanotube. This protein was genetically engineered to display constrained peptide loops with a series of different thiol, cationic, anionic, and imidazole functional groups. "Cys-loop" thiol variants consisting of 6 and 12 cysteine residues were isolated in the form of disulfide-linked nanotube bundles, a novel nanomaterial. Bundles were characterized by fluorescence microscopy, transmission electron microscopy, and optical trapping.
一种名为FliTrx的大肠杆菌鞭毛蛋白被研究用作一种新型的自组装蛋白质纳米管。这种蛋白质经过基因工程改造,以展示带有一系列不同硫醇、阳离子、阴离子和咪唑官能团的受限肽环。由6个和12个半胱氨酸残基组成的“半胱氨酸环”硫醇变体以二硫键连接的纳米管束形式分离出来,这是一种新型纳米材料。通过荧光显微镜、透射电子显微镜和光镊对纳米管束进行了表征。