Proteins immobilization on the surface of modified plant viral particles coated with hydrophobic polycations

J Biomater Sci Polym Ed. 2014;25(16):1743-54. doi: 10.1080/09205063.2014.946877. Epub 2014 Aug 14.

Abstract

Two hydrophobic cations based on poly-N-ethyl-vinylpyridine were used to produce biologically active complexes. The complexes obtained from tobacco mosaic virus (TMV) spherical particles (SPs), hydrophobic polycation, and a model protein were stable and did not aggregate in solution, particularly at high ionic strengths. The nucleic acid-free SPs were generated by thermal remodeling of the TMV (helical rod-shaped plant virus). The model protein preserved its antigenic activity in the ternary complex (SP-polycation-protein). Immobilization of proteins on the surface of SPs coated with hydrophobic cation is a promising approach to designing biologically active complexes used in bionanotechnologies.

Keywords: biologically active complexes; hydrophobic polycations; spherical particles; tobacco mosaic virus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Hydrophobic and Hydrophilic Interactions
  • Immobilized Proteins / chemistry*
  • Ions / chemistry
  • Microscopy, Fluorescence
  • Molecular Structure
  • Nanoparticles / chemistry
  • Plant Lectins
  • Polyamines / chemistry*
  • Polyelectrolytes
  • Polyvinyls / chemistry
  • Potexvirus
  • Protein Stability
  • Pyridinium Compounds / chemistry
  • Serum Albumin, Bovine / chemistry
  • Solutions
  • Spectrum Analysis
  • Tobacco Mosaic Virus
  • Virion / chemistry*

Substances

  • Datura stramonium lectin
  • Immobilized Proteins
  • Ions
  • Plant Lectins
  • Polyamines
  • Polyelectrolytes
  • Polyvinyls
  • Pyridinium Compounds
  • Solutions
  • poly(N-ethyl-4-vinylpyridine bromide)
  • polycations
  • Serum Albumin, Bovine