Author(s): Kumara MT, Srividya N, Muralidharan S, Tripp BC
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Abstract 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.
This article was published in Nano Lett
and referenced in Journal of Analytical & Bioanalytical Techniques