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Encapsidated atom-transfer radical polymerization in Qbeta virus-like nanoparticles

Academic Article
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Overview

related to degree

  • Higginson, Cody, Ph.D. in Chemistry, Scripps Research 2010 - 2015
  • Hovlid, Marisa L, Ph.D. in Chemistry, Scripps Research 2008 - 2014
  • Lau, Jolene Lim, Ph.D. in Chemistry, Scripps Research 2004 - 2010

authors

  • Hovlid, Marisa L
  • Lau, Jolene Lim
  • Breitenkamp, K.
  • Higginson, Cody
  • Laufer, B.
  • Manchester, Marianne
  • Finn, M.G.

publication date

  • August 2014

journal

  • ACS Nano  Journal

abstract

  • Virus-like particles (VLPs) are unique macromolecular structures that hold great promise in biomedical and biomaterial applications. The interior of the 30 nm-diameter Qβ VLP was functionalized by a three-step process: (1) hydrolytic removal of endogenously packaged RNA, (2) covalent attachment of initiator molecules to unnatural amino acid residues located on the interior capsid surface, and (3) atom-transfer radical polymerization of tertiary amine-bearing methacrylate monomers. The resulting polymer-containing particles were moderately expanded in size; however, biotin-derivatized polymer strands were only very weakly accessible to avidin, suggesting that most of the polymer was confined within the protein shell. The polymer-containing particles were also found to exhibit physical and chemical properties characteristic of positively charged nanostructures, including the ability to easily enter mammalian cells and deliver functional small interfering RNA.

subject areas

  • Acrylic Resins
  • Amines
  • Binding Sites
  • Biological Transport
  • Capsid
  • HeLa Cells
  • Humans
  • Hydrolysis
  • Intracellular Space
  • Models, Molecular
  • Molecular Conformation
  • Nanoparticles
  • Particle Size
  • Polymerization
  • RNA, Viral
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Research

keywords

  • ATRP
  • encapsulation
  • polymerization
  • unnatural amino acid
  • virus-like particle
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Identity

PubMed Central ID

  • PMC4148144

International Standard Serial Number (ISSN)

  • 1936-0851

Digital Object Identifier (DOI)

  • 10.1021/nn502043d

PubMed ID

  • 25073013
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Additional Document Info

start page

  • 8003

end page

  • 8014

volume

  • 8

issue

  • 8

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