Structural studies and anticancer activity of a novel class of β-peptides

Chem Asian J. 2015 Feb;10(2):383-9. doi: 10.1002/asia.201403171. Epub 2014 Nov 18.

Abstract

Functionalized oligomeric organic compounds with well-defined β-proline scaffold have been synthesized by a cycloadditive oligomerization approach in racemic and enantiopure forms. The structure of the novel β-peptides was investigated by NMR spectroscopic and X-ray methods determining the conformational shapes of the β-proline oligomers in solution and solid states. The main structural elements subject to conformational switches are β-peptide bonds between 5-arylpyrrolidine-2-carboxylic acid units existing in Z/E configurations. The whole library of short β-peptides and intermediate acrylamides has been tested on antiproliferative activity towards the hormone-refractory prostate cancer cell line PC-3 revealing several oligomeric compounds with low micromolar and submicromolar activities. Bromine-substituted dimeric and trimeric acrylamides induced caspase-dependent apoptosis of PC-3 cells through cell-cycle arrest and mitochondrial damage.

Keywords: antiproliferative agents; cycloaddition; mTOR pathway; oligomers; prostate cancer; β-proline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / chemical synthesis
  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / toxicity
  • Apoptosis / drug effects
  • Caspases / metabolism
  • Cell Cycle Checkpoints / drug effects
  • Cell Line, Tumor
  • Cycloaddition Reaction
  • Humans
  • Membrane Potential, Mitochondrial / drug effects
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Peptides / toxicity
  • Proline / analogs & derivatives
  • Proline / chemistry
  • Protein Conformation
  • Stereoisomerism

Substances

  • Antineoplastic Agents
  • Peptides
  • Proline
  • Caspases
  • beta-proline