Design of Inhibitors for S100B

Curr Top Med Chem. 2005;5(12):1093-108. doi: 10.2174/156802605774370865.

Abstract

S100B interacts with the p53 protein in a calcium-dependent manner and down-regulates its function as a tumor suppressor. Therefore, inhibiting the S100B-p53 interaction represents a new approach for restoring functional wild-type p53 in cancers with elevated S100B such as found in malignant melanoma. A discussion of the biological rational for targeting S100B and a description of methodologies relevant to the discovery of compounds that inhibit S100B-p53 binding, including computational techniques, structural biology techniques, and cellular assays, is presented.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Biomarkers, Tumor
  • Calcium / metabolism
  • Computer-Aided Design
  • Drug Design
  • Female
  • Humans
  • Magnetic Resonance Spectroscopy
  • Male
  • Molecular Structure
  • Nerve Growth Factors / antagonists & inhibitors*
  • Nerve Growth Factors / metabolism
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins / antagonists & inhibitors*
  • S100 Proteins / metabolism
  • Solubility
  • Spectrometry, Fluorescence
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Biomarkers, Tumor
  • Nerve Growth Factors
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins
  • S100B protein, human
  • Tumor Suppressor Protein p53
  • Calcium