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High-affinity self-reactive human-antibodies by design and selection - targeting the integrin ligand-binding site

Academic Article
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Overview

authors

  • Barbas III, Carlos
  • Languino, L. R.
  • Smith, J. W.

publication date

  • November 1993

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • A strategy for the design and selection of human antibodies that bind receptors is described. We have demonstrated the validity of the approach by producing semi-synthetic human antibodies that bind integrins alpha v beta 3 and alpha IIb beta 3 with high affinity (10(-10) M). The selected antibodies mimic the integrins' natural ligands as demonstrated by their ability to compete with these ligands and Arg-Gly-Asp (RGD)-containing peptides for binding to the integrins. Furthermore, the antibodies bind in a cation-dependent fashion and are functional in cell adhesion assays. Antibodies that are high-affinity inhibitors of cell adhesion receptors should be of use in assessing receptor function and dissecting mechanisms of adhesion. Semisynthetic human antibodies that target integrins are potential therapeutic agents for the treatment of a number of diseases including thrombosis and metastasis. Furthermore, antibodies that are optimized to bind by a single complementarity determining region may be important lead compounds for the design of small molecule pharmaceuticals.

subject areas

  • Amino Acid Sequence
  • Antibodies
  • Base Sequence
  • Binding Sites
  • DNA Primers
  • Humans
  • Immunoglobulin Fab Fragments
  • Integrins
  • Kinetics
  • Ligands
  • Molecular Sequence Data
  • Mutagenesis
  • Oligopeptides
  • Platelet Glycoprotein GPIIb-IIIa Complex
  • Polymerase Chain Reaction
  • Receptors, Cytoadhesin
  • Receptors, Vitronectin
  • Recombinant Proteins
  • Structure-Activity Relationship
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Research

keywords

  • CELL ADHESION
  • COMBINATORIAL LIBRARIES
  • DRUG DESIGN
  • METASTASIS
  • PHAGE DISPLAY
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Identity

PubMed Central ID

  • PMC47701

International Standard Serial Number (ISSN)

  • 0027-8424

PubMed ID

  • 7694276
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Additional Document Info

start page

  • 10003

end page

  • 10007

volume

  • 90

issue

  • 21

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