Role of hexahistidine in directed nanoassemblies of tobacco mosaic virus coat protein

ACS Nano. 2011 Mar 22;5(3):1606-16. doi: 10.1021/nn1025719. Epub 2011 Feb 25.

Abstract

A common challenge in nanotechnology is the fabrication of materials with well-defined nanoscale structure and properties. Here we report that a genetically engineered tobacco mosaic virus (TMV) coat protein (CP), to which a hexahistidine (His) tag was incorporated, can self-assemble into disks, hexagonally packed arrays of disks, stacked disks, helical rods, fibers, and elongated rafts. The insertion of a His tag to the C-terminus of TMV-CP was shown to significantly affect the self-assembly in comparison to the wild type, WT-TMV-CP. Furthermore, the His tag interactions attributed to the alternative self-assembly of His-TMV-CP can be controlled through ethanol and nickel-nitrilotriacetic acid (Ni-NTA) additions as monitored with atomic force microscopy.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Capsid Proteins / chemistry*
  • Capsid Proteins / genetics
  • Capsid Proteins / ultrastructure*
  • Crystallization / methods*
  • Histidine / chemistry*
  • Macromolecular Substances / chemistry
  • Materials Testing
  • Molecular Conformation
  • Nanostructures / chemistry*
  • Nanostructures / ultrastructure*
  • Oligopeptides / chemistry*
  • Particle Size
  • Protein Engineering / methods*
  • Surface Properties

Substances

  • Capsid Proteins
  • His-His-His-His-His-His
  • Macromolecular Substances
  • Oligopeptides
  • coat protein, Tobacco necrosis virus (Nebraska)
  • Histidine