Autori: Murariu, M., Dragan, E. S., Manea, M., Drochioiu, G
Editorial: Ph. Collery, I. Maymard, T. Theophanides, L. Khassanova, T. Collery, John Libbey Eurotext, Paris, Metal Ions in Biology and Medicine: XIII Neurology, 10, p.701-707, 2008.
Some new synthesized metal-affinity peptides and their metal complexes have been investigated by mass spectrometry, circular dichroism and atomic force microscopy to reveal their conformational changes. These peptides have been prepared by Fmoc strategy using TGR resin and Abeta1-40 peptide and its fragments by Boc/Bzl strategy on MBHA resin as solid support. A model decapeptide is proposed as a simple system which can be used for a systematic study of the impact of different metal ions on peptide secondary structure on the molecular level; histidine residues were incorporated into this peptide in a sequence similar to beta-amyloid peptide (Abeta 1-40) to generate possible complexation sites for metal ions. The secondary structure of the decapeptide was investigated by circular dichroism (CD) compared to Abeta 1-40 peptide and its fragments. The self-assembled nanostructures are dependent on the presence of metal ions and sodium dodecyl sulfate (SDS). Atomic force microscopy (AFM) revealed also that metal ions and SDS affect differently the Abeta 1-40 nanostructures and the decapeptide ones.
Cuvinte cheie: Metal-affinity peptide, mass spectrometry, CD spectropolarimetry, atomic force microscopy