title: Alternative origin for "gain-of-function" by mutant SOD enzyme and for conformational change of normal prion protein.
abstract: Capillary electrophoresis and ESI-Mass spectrometry methods have revealed that a hydroperoxo-copper(II) complex with (tpa) (=tris(2-pyridylmethyl)amine) reacts with carbonic anhydrase or amyloid beta-peptide (1-40) as a nucleophile to induce the conformational change of the protein structure, while the Cu(bdpg)-complex ((bdpg)=N,N-bis(2-pyridylmethy)-beta-alanineamide) acts as an electrophile toward the proteins to degrade them under the same experimental conditions. This will lead to suggest that enhanced nucleophilic attack by a copper(II)-peroxide adduct to peptide bonding may be one of the serious origins for the "gain-of-function" by mutant superoxide dismutase and for conformational change of normal prion protein.
authors.affiliation: Chemical Institute for Neurodegeneration (CIN), Department of Chemistry, Faculty of Science, Yamagata University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Nishino
authors.forename: A
authors.initials: A
authors.lastname: Kishita
authors.forename: Y
authors.initials: Y
authors.lastname: Nishida
mesh_terms: D019075:Electrophoresis, Capillary; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D021241:Spectrometry, Mass, Electrospray Ionization; D013482:Superoxide Dismutase / Q000737:chemistry / Q000235:genetics*
chemical_list: D011328:Prions; D013482:Superoxide Dismutase