Copper(II) interaction with peptide fragments of histidine-proline-rich glycoprotein: Speciation, stability and binding details(125 visite) La Mendola D, Magrì A, Santoro AM, Nicoletti VG, Rizzarelli E
Parole chiave: Angiogenesis, Copper, Hprg, Peptide, Protein, Zinc, Amide, Copper Complex, Glycoprotein, Histidine, Histidine Proline Rich Glycoprotein, Imidazole, Mutant Protein, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Article, Binding Site, Chemical Interaction, Circular Dichroism, Controlled Study, Electron Spin Resonance, Metal Binding, Point Mutation, Potentiometric Titration, Protein Binding, Protein Stability, Proton Transport, Ultraviolet Spectroscopy, Coordination Complexes, Hydrogen-Ion Concentration, Molecular Structure, Peptide Fragments, Spectrophotometry,
*** IBB - CNR *** Istituto di Biostrutture e Bioimmagini-CNR-Catania, Viale A. Doria 6, Catania, Italy. email@example.com Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria 6, 95125 Catania, Italy
Poo, J.L., Rosas-Romero, R., Montemayor, A.C., Isoard, F., Uribe, M., (2003) J. Gastroenterol., 38, pp. 45-51
GHHPH is the peptide repeat present in histidine-proline rich glycoprotein (HPRG), a plasma glycoprotein involved in angiogenesis process. The copper(II) ions interaction with mono (Ac-GHHPHG-NH(2)) and its bis-repeat (Ac-GHHPHGHHPHG-NH(2)) was investigated by means of potentiometric and spectroscopic techniques. To single out the copper(II) coordination environments of different species formed with Ac-GHHPHG-NH(2), three single point mutated peptides were also synthesized and their ability to coordinate Cu(2+) investigated. Ac-GHHPHG-NH(2) binds Cu(2+) by the imidazole side chain and the amide nitrogen deprotonation that takes place towards the N-terminus. The bis-repeat is able to bind Cu(2+) more efficiently than Ac-GHHPHG-NH(2). This difference is not only due to the number of His residues in the sequence but also to the different binding sites. In fact, the comparison of the potentiometric and spectroscopic data of the copper(II) complexes with a bis-repeatPeg construct Ac-(GHHPHG)-Peg-(GHHPHG)-NH(2) and those of the metal complexes with Ac-HGHH-NH(2), indicates that the central HGHH amino acid sequence is the main copper(II) binding site. Copyright 2012 Elsevier Inc. All rights reserved.
Ntziachristos V, Cuénod CA, Fournier L, Balvay D, Pradel C, Siauve N, Clement O, Jouannot E, Lucidarme O, Vecchio SD, Salvatore M, Law B, Tung C-H, Jain RK, Fukumura D, Munn LL, Brown EB, Schellenberger E, Montet X, Weissleder R, Clerck ND, Postnov A * Tumor Imaging(124 visite) Textbook Of In Vivo Imaging In Vertebrates (ISSN: 9780-4700), 2007 Jul 16; 1: 277-309. Impact Factor:1.148 DettagliEsporta in BibTeXEsporta in EndNote
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