title: Insights into the mechanisms of amyloid formation of Zn(II)-Ab11-28: pH-dependent zinc coordination and overall charge as key parameters for kinetics and the structure of Zn(II)-Ab11-28 aggregates.
abstract: Self-assembly of amyloidogenic peptides and their metal complexes are of multiple interest including their association with several neurological diseases. Therefore, a better understanding of the role of metal ions in the aggregation process is of broad interest. We report pH-dependent structural and aggregation studies on Zn(II) binding to the amyloidogenic peptide Ab11-28. The results suggest that coordination of the N-terminal amine to Zn(II) is responsible for the inhibition of amyloid formation and the overall charge for amorphous aggregates.
authors: Laboratoire de Chimie de Coordination, CNRS, 205 route de Narbonne, BP 44099, F-31077 Toulouse Cedex 4, France.
authors: Bruno
authors: B
authors: Alies
authors: Giovanni
authors: G
authors: LaPenna
authors: Stéphanie
authors: S
authors: Sayen
authors: Emmanuel
authors: E
authors: Guillon
authors: Christelle
authors: C
authors: Hureau
authors: Peter
authors: P
authors: Faller
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D056928:X-Ray Absorption Spectroscopy; D015032:Zinc / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D009942:Organometallic Compounds; D010446:Peptide Fragments; C419470:amyloid beta-protein (11-28); D015032:Zinc