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Evolution and protein packaging of small-molecule rna aptamers

Academic Article
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Overview

related to degree

  • Fiedler, Jason, Ph.D. in Biology, Scripps Research 2007 - 2012
  • Brown, Steven David, Ph.D. in Chemical Biology, Scripps Research 2004 - 2010
  • Lau, Jolene Lim, Ph.D. in Chemistry, Scripps Research 2004 - 2010

authors

  • Lau, Jolene Lim
  • Baksh, M. M.
  • Fiedler, Jason
  • Brown, Steven David
  • Kussrow, A.
  • Bornhop, Darryl
  • Ordoukhanian, Phillip
  • Finn, M.G.

publication date

  • October 2011

journal

  • ACS Nano  Journal

abstract

  • A high-affinity RNA aptamer (K(d) = 50 nM) was efficiently identified by SELEX against a heteroaryldihydropyrimidine structure, chosen as a representative drug-like molecule with no cross reactivity with mammalian or bacterial cells. This aptamer, its weaker-binding variants, and a known aptamer against theophylline were each embedded in a longer RNA sequence that was encapsidated inside a virus-like particle by a convenient expression technique. These nucleoprotein particles were shown by backscattering interferometry to bind to the small-molecule ligands with affinities similar to those of the free (nonencapsidated) aptamers. The system therefore comprises a general approach to the production and sequestration of functional RNA molecules, characterized by a convenient label-free analytical technique.

subject areas

  • Allolevivirus
  • Aptamers, Nucleotide
  • Base Sequence
  • Capsid Proteins
  • Inverted Repeat Sequences
  • Ligands
  • Molecular Sequence Data
  • Pyrimidines
  • SELEX Aptamer Technique
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Research

keywords

  • RNA packaging
  • aptamers
  • backscattering interferometry
  • virus-like particles
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Identity

PubMed Central ID

  • PMC3209476

International Standard Serial Number (ISSN)

  • 1936-0851

Digital Object Identifier (DOI)

  • 10.1021/nn2006927

PubMed ID

  • 21899290
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Additional Document Info

start page

  • 7722

end page

  • 7729

volume

  • 5

issue

  • 10

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