Study of Inhibitors of Neu and Related Tyrosine-Specific Protein Kinases: Implications for the Treatment of Breast Cancer

Abstract

The vast majority of potent tyrosine kinase-specific inhibitors described to date are competitive with ATP. Although these species tend to exhibit impressive Ki values, their effectiveness under physiological conditions is markedly impaired due to high intracellular concentrations of ATP. Peptide based inhibitors that are competitive with protein/peptide substrate have been described for various tyrosine kinases, however these nonphosphorylatable phenylalanine containing inhibitors typically display poor inhibitory profiles. We have found that L-Dopa serves as a powerful nonphosphorylatable tyrosine mimetic. In addition, we have identified several promising leads in the creation of nonpeptidic inhibitors of tyrosine kinases. Since these species are not directed to the ATP binding region, they do not suffer from the disadvantages associated with ATP analogs.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 1997
Accession Number
ADA338938

Entities

People

  • Arthur Edelman

Organizations

  • University at Buffalo

Tags

DTIC Thesaurus Topics

  • Amines
  • Amino Acids
  • Breast Cancer
  • Cells
  • Chemical Compounds
  • Chemistry
  • Diseases And Disorders
  • Enzyme Inhibitors
  • Enzymes
  • Materials
  • Neoplasms
  • New York
  • Parkinson'S Disease
  • Phenylalanine
  • Resins
  • Substrate Specificity
  • Substrates

Fields of Study

  • Biology

Readers

  • Breast cancer cell signaling and growth regulation.
  • Molecular and Cellular Biochemistry
  • Systems Analysis and Design