Metal Loading Capacity of Aβ N-Terminus: a Combined Potentiometric and Spectroscopic Study of Zinc(II) Complexes with Aβ(1−16), Its Short or Mutated Peptide Fragments and Its Polyethylene Glycol−ylated Analogue

Autor: Giuseppe Impellizzeri, Imre Sóvágó, Katalin Osz, Chiara A. Damante, Zoltán Nagy, Giuseppe Pappalardo, Enrico Rizzarelli, Giulia Grasso

Publikováno v: Inorganic chemistry 48 (2009): 10405–10415. doi:10.1021/ic8006052
info:cnr-pdr/source/autori:Chiara A. Damante; Kataline Osz; Zoltan Nagy; Giuseppe Pappalardo; Giulia Grasso; Giuseppe Impellizzeri; Enrico Rizzarelli; Imre Sóvágó/titolo:Metal loading capacity of Abeta N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with Abeta(1-16), its short or mutated peptide fragments and its polyethylene glycol-ylated analogue./doi:10.1021%2Fic8006052/rivista:Inorganic chemistry/anno:2009/pagina_da:10405/pagina_a:10415/intervallo_pagine:10405–10415/volume:48

Aggregation of the amyloid beta-peptide (Abeta) into insoluble fibrils is a key pathological event in Alzheimer's Disease (AD). There is now compelling evidence that metal binding to Abeta is involved in AD pathogenesis. The amino acid region 1-16 is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4999025a3507c217960a2a8656c04908
https://doi.org/10.1021/ic9012334

Copper(II) Interaction with Unstructured Prion Domain Outside the Octarepeat Region: Speciation, Stability, and Binding Details of Copper(II) Complexes with PrP106−126 Peptides

Autor: Giovanni Micera, Zoltán Nagy, Katalin Osz, Giuseppe Pappalardo, Giuseppe Di Natale, Imre Sóvágó, Diego La Mendola, Viktória Rigó, Giuseppe Impellizzeri, Nikolett Mihala, Daniele Sanna, Enrico Rizzarelli, Giulia Grasso

Publikováno v: Inorganic chemistry 44 (2005): 7214–7225. doi:10.1021/ic050754k
info:cnr-pdr/source/autori:Giuseppe Di Natale; Giulia Grasso; Giuseppe Impellizzeri; Diego La Mendola; Giovanni Micera; Nikolett Mihala; Zoltan Nagy; Katalin Osz; Giuseppe Pappalardo; Viktoria Rigò; Enrico Rizzarelli; Daniele Sanna; Imre Sòvàgò/titolo:Copper(II) Interaction with Unstructured Prion Domain Outside the Octarepeat Region: Speciation, Stability, and Binding Details of Copper(II) Complexes with PrP106-126 Peptides./doi:10.1021%2Fic050754k/rivista:Inorganic chemistry/anno:2005/pagina_da:7214/pagina_a:7225/intervallo_pagine:7214–7225/volume:44

Copper(II) complexes of the neurotoxic peptide fragments of human and chicken prion proteins were studied by potentiometric, UV-vis, CD, and EPR spectroscopic and ESI-MS methods. The peptides included the terminally blocked native and scrambled seque

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e22690d4fe7a5fd0770bfb9f656c0054
https://doi.org/10.1021/ic050754k

Copper(ii) and nickel(ii) binding modes in a histidine-containing model dodecapeptide

Autor: Maria Grazia Saita, Raffaele P. Bonomo, Giulia Grasso, Tiziana Campagna, Giuseppe Impellizzeri, Giuseppe Pappalardo

Publikováno v: New Journal of Chemistry. 26:593-600

The formation of complexes of HGGGHGHGGGHG (HG12) with copper(II) and nickel(II) have been studied in aqueous solution under various experimental conditions, including different pH and metal to ligand ratios. The study has been carried out using visi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dfeeb882fcd513b0fdc66409edb22168
https://doi.org/10.1039/b110655d

Chiral recognition by the copper(II) complex of 6-deoxy-6-N-(2-methylaminopyridine)-?-cyclodextrin

Autor: Giuseppe Maccarrone, Raffaele P. Bonomo, Graziella Vecchio, Lorenza Carima, Franca D'Alessandro, Giuseppe Impellizzeri, Enrico Rizzarelli, Giorgio Sartor, Vincenzo Cucinotta, Roberto Corradini, Rosangela Marchelli

Publikováno v: Chirality. 9:341-349

A modified β-cyclodextrin bearing a 2-aminomethylpyridine binding site for copper(II) (6-deoxy-6-[N-(2-methylamino)pyridine)]-β-cyclodextrin, CDampy was synthesized by C6-monofunctionalization. The acid-base properties of the new ligand in aqueous

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a523a1fdeeb103e04708271045e43283
https://doi.org/10.1002/(sici)1520-636x(1997)9:4<341::aid-chir5>3.0.co

Copper(II) coordination properties of the integrin ligand sequence PHSRN and its new β-cyclodextrin conjugates

Autor: Diego La Mendola, Donatella A. Distefano, Antonio Magrì, Giuseppe Impellizzeri, Franca D'Alessandro, Giuseppe Pappalardo, Tiziana Campagna

Publikováno v: Journal of inorganic biochemistry 113 (2012): 15–24. doi:10.1016/j.jinorgbio.2012.04.002
info:cnr-pdr/source/autori:Magri, Antonio; D'Alessandro, Franca; Distefano, Donatella A.; Campagna, Tiziana; Pappalardo, Giuseppe; Impellizzeri, Giuseppe; La Mendola, Diego/titolo:Copper(II) coordination properties of the integrin ligand sequence PHSRN and its new beta-cyclodextrin conjugates/doi:10.1016%2Fj.jinorgbio.2012.04.002/rivista:Journal of inorganic biochemistry/anno:2012/pagina_da:15/pagina_a:24/intervallo_pagine:15–24/volume:113

The peptide sequence PHSRN is the second cell binding site of the human fibronectin protein, a glycoprotein which plays a critical adhesive role during development, tissue repair and angiogenesis. The copper(II) complexes with the peptide fragment PH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8dd169bd0fa41dfb74723fc7e059139
https://pubmed.ncbi.nlm.nih.gov/22687490