Interaction of Aβ peptide with tubulin causes an inhibition of tubulin polymerization and the apoptotic death of cancer cells

Chem Commun (Camb). 2015 Feb 11;51(12):2249-52. doi: 10.1039/c4cc09390a.

Abstract

We report in this work that the Aβ peptide directly interacts with tubulin close to the vinblastine and GTP/GDP binding site, inhibits the tubulin polymerization rate, induces tubulin aggregation, causes cell shrinking, enhances Mad2, BubR1, p53, and p21 activation in MCF7 cells and induces the apoptotic death of A549, HeLa and MCF7 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism*
  • Apoptosis
  • Binding Sites
  • Cell Line, Tumor
  • Cyclin-Dependent Kinase Inhibitor p21 / metabolism
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism
  • HeLa Cells
  • Humans
  • MCF-7 Cells
  • Mad2 Proteins / metabolism
  • Peptides
  • Polymerization
  • Protein Binding
  • Protein Serine-Threonine Kinases / metabolism
  • Tubulin / chemistry
  • Tubulin / metabolism*
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Amyloid beta-Peptides
  • Cyclin-Dependent Kinase Inhibitor p21
  • Mad2 Proteins
  • Peptides
  • Tubulin
  • Tumor Suppressor Protein p53
  • Guanosine Triphosphate
  • BUB1 protein, human
  • Protein Serine-Threonine Kinases