title: Amyloidogenic peptides at hydrophobic-hydrophilic interfaces: coordination affinities and the chelate effect dictate the competitive binding of Cu2+ and Zn2+.
authors.affiliation: Department of Interfaces, Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam, Germany. hoernke@mpikg.mpg.de
authors.forename: Maria
authors.initials: M
authors.lastname: Hoernke
authors.forename: Beate
authors.initials: B
authors.lastname: Koksch
authors.forename: Gerald
authors.initials: G
authors.lastname: Brezesinski
mesh_terms: D000544:Alzheimer Disease / Q000188:drug therapy / Q000378:metabolism / Q000503:physiopathology / Q000517:prevention & control; D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D001667:Binding, Competitive; D002614:Chelating Agents / Q000378:metabolism / Q000494:pharmacology / Q000627:therapeutic use; D003300:Copper / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013052:Spectrometry, X-Ray Emission; D013499:Surface Properties; D015032:Zinc / Q000378:metabolism*
chemical_list: D000682:Amyloid; D002614:Chelating Agents; D010455:Peptides; D006639:Histidine; D003300:Copper; D015032:Zinc