Interference of a new cyclometallated Pt compound with Cu binding to amyloid-β peptide.
Coordination of a cyclometallated Pt(II) complex (1) to an amyloid-β peptide was probed by NMR and ESI-MS. Furthermore, EPR showed that binding of 1 to the Cu(II)-amyloid-β species resulted in a reshuffling of the Cu(II) coordination sphere, which was absent or lower for the sister non cyclometallated Pt(II) complexes.
CNRS, LCC (Laboratoire de Chimie de Coordination), Toulouse, France. isabelle.sasaki@lcc-toulouse.fr
Isabelle
I
Sasaki
Christian
C
Bijani
Sonia
S
Ladeira
Valérie
V
Bourdon
Peter
P
Faller
Christelle
C
Hureau
D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D009944:Organoplatinum Compounds / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
D016229:Amyloid beta-Peptides; D009944:Organoplatinum Compounds; D010446:Peptide Fragments; C084358:amyloid beta-protein (1-28); D003300:Copper