Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide

Brain Res Bull. 2014 Sep:108:113-7. doi: 10.1016/j.brainresbull.2014.08.009. Epub 2014 Sep 26.

Abstract

Aggregated β-amyloid peptides play key roles in the development of Alzheimer's disease, and recent evidence suggests that microbial particles, among others, can facilitate their polymerization. Bacterial enzymes, however, have been proved to be beneficial in degrading pathological fibrillar structures in clinical settings, such as strepto-kinases in resolving blood-clots. The purpose of this study was to investigate the ability of bacterial substances to effectively hydrolyze β-amyloid peptides. Degrading products of several proteinases from Bacillus pumilus were evaluated using MALDI-TOF mass-spectrometry, and their toxicity was assessed in vitro using cell-culture assays and morphological studies. These enzymes have proved to be non-toxic and were demonstrated to cleave through the functional domains of β-amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate anti-amyloid agents.

Keywords: Aggregation; Alzheimer's disease; Bacillus pumilus; Bacterium; Proteinase; β-Amyloid-peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism*
  • Amyloid beta-Peptides / metabolism*
  • Bacillus / enzymology*
  • Humans
  • Neuroblastoma
  • Peptide Fragments / metabolism*
  • Peptide Hydrolases / isolation & purification
  • Peptide Hydrolases / metabolism*
  • Proteolysis
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Tumor Cells, Cultured

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-42)
  • Peptide Hydrolases