Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Unnatural amino acid incorporation into virus-like particles

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

related to degree

  • Brown, Steven David, Ph.D. in Chemical Biology, Scripps Research 2004 - 2010
  • Lander, Gabriel, Ph.D. in Biophysics, Scripps Research 2004 - 2009
  • Prasuhn Jr., Duane E, Ph.D. in Chemistry, Scripps Research 2001 - 2007
  • Strable, Erica, Ph.D. in Biochemistry, Scripps Research 2000 - 2006

authors

  • Strable, Erica
  • Prasuhn Jr., Duane E
  • Udit, A. K.
  • Brown, Steven David
  • Link, A. J.
  • Ngo, J. T.
  • Lander, Gabriel
  • Quispe, J.
  • Potter, Clinton
  • Carragher, Bridget
  • Tirrell, D. A.
  • Finn, M.G.

publication date

  • April 2008

journal

  • Bioconjugate Chemistry  Journal

abstract

  • Virus-like particles composed of hepatitis B virus (HBV) or bacteriophage Qbeta capsid proteins have been labeled with azide- or alkyne-containing unnatural amino acids by expression in a methionine auxotrophic strain of E. coli. The substitution does not affect the ability of the particles to self-assemble into icosahedral structures indistinguishable from native forms. The azide and alkyne groups were addressed by Cu(I)-catalyzed [3 + 2] cycloaddition: HBV particles were decomposed by the formation of more than 120 triazole linkages per capsid in a location-dependent manner, whereas Qbeta suffered no such instability. The marriage of these well-known techniques of sense-codon reassignment and bioorthogonal chemical coupling provides the capability to construct polyvalent particles displaying a wide variety of functional groups with near-perfect control of spacing.

subject areas

  • Allolevivirus
  • Amino Acid Sequence
  • Amino Acids
  • Capsid Proteins
  • Dimerization
  • Hepatitis B virus
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Trypsin
scroll to property group menus

Identity

PubMed Central ID

  • PMC2713011

International Standard Serial Number (ISSN)

  • 1043-1802

Digital Object Identifier (DOI)

  • 10.1021/bc700390r

PubMed ID

  • 18318461
scroll to property group menus

Additional Document Info

start page

  • 866

end page

  • 875

volume

  • 19

issue

  • 4

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support