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Chemical adaptor immunotherapy: design, synthesis, and evaluation of novel integrin-targeting devices

Academic Article
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Overview

authors

  • Li, L. S.
  • Rader, Christoph
  • Matsushita, M.
  • Das, S.
  • Barbas III, Carlos
  • Lerner, Richard
  • Sinha, Subhash

publication date

  • November 2004

journal

  • Journal of Medicinal Chemistry  Journal

abstract

  • A series of beta-diketone derivatives of RGD peptidomimetics that selectively bind to alphavbeta3 and alphavbeta5 integrins were synthesized and covalently docked to the reactive lysine residues of monoclonal aldolase antibody 38C2. The resulting targeting devices strongly and selectively bound to human cancer cells expressing integrins alphavbeta3 and alphavbeta5 as analyzed by flow cytometry. In vitro and in vivo studies revealed that these novel integrin-targeting devices efficiently inhibit tumor growth. Thus, the combination of beta-diketone derivatives of RGD peptidomimetics that target cell surface integrins alphavbeta3 and alphavbeta5 with monoclonal aldolase antibodies through formation of a covalent bond of defined stoichiometry holds promise as a new approach to cancer therapy.

subject areas

  • Antibodies, Monoclonal
  • Breast Neoplasms
  • Cell Line, Tumor
  • Drug Design
  • Female
  • Fructose-Bisphosphate Aldolase
  • Humans
  • Immunotherapy
  • Integrin alphaVbeta3
  • Integrins
  • Ketones
  • Lysine
  • Melanoma
  • Models, Molecular
  • Molecular Mimicry
  • Oligopeptides
  • Protein Binding
  • Receptors, Vitronectin
  • Structure-Activity Relationship
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Identity

International Standard Serial Number (ISSN)

  • 0022-2623

Digital Object Identifier (DOI)

  • 10.1021/jm049666k

PubMed ID

  • 15509162
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Additional Document Info

start page

  • 5630

end page

  • 5640

volume

  • 47

issue

  • 23

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