skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Study and Characterization of Tobacco Mosaic Virus Head-to-tail Assembly Assisted by Aniline Polymerization

Abstract

One-dimensional composite nanofibres with narrow dispersity, high aspect ratio and high processibility have been fabricated by head-to-tail self-assembly of rod-like tobacco mosaic virus assisted by aniline polymerization, which can promote many potential applications including electronics, optics, sensing and biomedical engineering.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914408
Report Number(s):
BNL-78976-2007-JA
TRN: US200809%%60
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Chem. Commun.; Journal Volume: 2006; Journal Issue: 28
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; ANILINE; POLYMERIZATION; TOBACCO MOSAIC VIRUS; NANOSTRUCTURES; FIBERS; FABRICATION; USES; national synchrotron light source

Citation Formats

Niu,Z., Bruckman, M., Kotakadi, V., He, J., Emrick, T., Russell, T., Yang, L., and Wang, Q. Study and Characterization of Tobacco Mosaic Virus Head-to-tail Assembly Assisted by Aniline Polymerization. United States: N. p., 2006. Web. doi:10.1039/b603780a.
Niu,Z., Bruckman, M., Kotakadi, V., He, J., Emrick, T., Russell, T., Yang, L., & Wang, Q. Study and Characterization of Tobacco Mosaic Virus Head-to-tail Assembly Assisted by Aniline Polymerization. United States. doi:10.1039/b603780a.
Niu,Z., Bruckman, M., Kotakadi, V., He, J., Emrick, T., Russell, T., Yang, L., and Wang, Q. Sun . "Study and Characterization of Tobacco Mosaic Virus Head-to-tail Assembly Assisted by Aniline Polymerization". United States. doi:10.1039/b603780a.
@article{osti_914408,
title = {Study and Characterization of Tobacco Mosaic Virus Head-to-tail Assembly Assisted by Aniline Polymerization},
author = {Niu,Z. and Bruckman, M. and Kotakadi, V. and He, J. and Emrick, T. and Russell, T. and Yang, L. and Wang, Q.},
abstractNote = {One-dimensional composite nanofibres with narrow dispersity, high aspect ratio and high processibility have been fabricated by head-to-tail self-assembly of rod-like tobacco mosaic virus assisted by aniline polymerization, which can promote many potential applications including electronics, optics, sensing and biomedical engineering.},
doi = {10.1039/b603780a},
journal = {Chem. Commun.},
number = 28,
volume = 2006,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}
  • One-dimensional (1D) polyaniline/tobacco mosaic virus (TMV) composite nanofibers and macroscopic bundles of such fibers were generated via a self-assembly process of TMV assisted by in-situ polymerization of polyaniline on the surface of TMV. At near-neutral reaction pH, branched polyaniline formed on the surface of TMV preventing lateral association. Therefore, long 1D nanofibers were observed with high aspect ratios and excellent processibility. At a lower pH, transmission electron microscopy (TEM) analysis revealed that initially long nanofibers were formed which resulted in bundled structures upon long-time reaction, presumably mediated by the hydrophobic interaction because of the polyaniline on the surface of TMV.more » In-situ time-resolved small-angle X-ray scattering study of TMV at different reaction conditions supported this mechanism. This novel strategy to assemble TMV into 1D and 3D supramolecular composites could be utilized in the fabrication of advanced materials for potential applications including electronics, optics, sensing, and biomedical engineering.« less
  • The initial stage in the self-assembly of tobacco mosaic virus (TMV) RNA and coat protein into virions involves insertion of a loop of TMV RNA between layers of a double-layered disk of TMV protein (containing 17 coat protein subunits per layer) via the central channel of the disk, followed by conversion of the disk-RNA complex into a two-turn protohelix and addition of more protein (elongation). This mechanism leads to assembling particles in which one of the uncoated RNA tails, that containing the 5'-terminus, runs back along the central channel of the growing rod.
  • Sedimentation and proton binding studies of the endothermic self-association of tobacco mosaic virus (TMV) protein indicate that the so-called 20S sedimenting protein is an interaction system involving at least the 34-subunit two-turn cylindrical disk aggregate and the 49-subunit three-turn helical rod. The pH dependence of this overall equilibrium suggests that disk formation is proton-linked through the binding of protons to the two-turn helix which is not present at significant concentrations near pH 7. There is a temperature-induced intramolecular conformation change in the protein leading to a difference spectrum which is complete in 5 x 10/sup -6/s at pH 7 andmore » 20/sup 0/C and is dominated at 300 nm by tryptophan residues. The probable binding frame at the internal assembly nucleation site of TMV-RNA has been determined by measuring the association constants for the binding of various trinucleoside diphosphates to helical TMV protein rods. The -CAG-AAG-AAG-sequence at the nucleation site is capable of providing at least 10 to 14 kcal/mol of sites of binding free energy for the nucleation event in TMV self-assembly.« less
  • Assembly of tobacco mosaic virus is initiated by the binding of a specific loop of the RNA into the central hole of the disk aggregate of protein subunits. Since the nucleation loop is located about five-sixths along the RNA molecule, subsequent elongation must be bidirectional. We have now measured the rates of elongation in the two directions by determining the lengths of RNA protected from nuclease digestion at different times and using either intact TMV RNA, or RNA with most of the longer tail removed. Comparison of the rates with the protein supplied as either a mixture of disks withmore » A-protein (a mixture of less aggregated states) or just A-protein, shows that different mechanisms and protein aggregates are used for the most rapid growth. When the disks are present, they add more rapidly along the longer RNA tail but do not appear to add directly on the shorter tail. In contrast, smaller aggregates (A-protein) can add at both ends of the rod, but do so more slowly. Mechanisms for these processes are discussed. Preliminary results on the binding of the specific hexanucleotide AAGAAG to the disk are given and compared with the known changes on binding nonspecific hexanucleotides or the trinucleotide AAG.« less