Amyloidogenic peptides at hydrophobic-hydrophilic interfaces: coordination affinities and the chelate effect dictate the competitive binding of Cu2+ and Zn2+

Chemphyschem. 2011 Aug 22;12(12):2225-9. doi: 10.1002/cphc.201100215. Epub 2011 Jul 12.
No abstract available

MeSH terms

  • Alzheimer Disease / drug therapy
  • Alzheimer Disease / metabolism
  • Alzheimer Disease / physiopathology
  • Alzheimer Disease / prevention & control
  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Binding, Competitive
  • Chelating Agents / metabolism
  • Chelating Agents / pharmacology
  • Chelating Agents / therapeutic use
  • Copper / metabolism*
  • Histidine / chemistry
  • Histidine / metabolism*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Mimicry
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism*
  • Protein Folding
  • Protein Structure, Secondary
  • Spectrometry, X-Ray Emission
  • Surface Properties
  • Zinc / metabolism*

Substances

  • Amyloid
  • Chelating Agents
  • Peptides
  • Histidine
  • Copper
  • Zinc