Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1-40)

Chem Commun (Camb). 2018 May 24;54(43):5430-5433. doi: 10.1039/c8cc01733f.

Abstract

We investigated the influence of the chemical structure of the phenylalanine side chain in position 19 of the 40 residue amyloid β peptide. Side chain modifications in this position yielded fibrils of essentially unaltered morphology, structure, and dynamics, but significantly increased fibrillation kinetics and diminished the toxicity of the peptides.

MeSH terms

  • Amyloid beta-Peptides / antagonists & inhibitors*
  • Amyloid beta-Peptides / toxicity
  • Animals
  • Cell Line
  • Cell Survival / drug effects
  • Kinetics
  • Molecular Structure
  • Peptide Fragments / antagonists & inhibitors*
  • Peptide Fragments / toxicity
  • Phenylalanine / chemistry
  • Phenylalanine / pharmacology*
  • Rats

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • Phenylalanine