Semax, an ACTH4-10 peptide analog with high affinity for copper(II) ion and protective ability against metal induced cell toxicity(462 views) Tabbì G, Magrì A, Giuffrida A, Lanza V, Pappalardo G, Naletova I, Nicoletti VG, Attanasio F, Rizzarelli E
Keywords: Cell Viability, Copper, Semax, Speciation, Spectroscopy, Voltammetry, Copper Ion, Corticotropin[4-10], Heptapeptide, Histidine, Methionine, Neuroprotective Agent, Nitrogen, Unclassified Drug, Article, Cell Protection, Complex Formation, Conformational Transition, Drug Cytotoxicity, Electrospray Mass Spectrometry, Endothelium Cell, Metal Binding, Mtt Assay, Neuroblastoma Cell, Oxidation Reduction Potential, Potentiometric Titration, Proton Transport, Species Differentiation, Species Distribution, Stereochemistry, Acth (4-7), Pro-Gly-Pro-, Peptide Fragment, Analogs And Derivatives, Cell Line, Electron Spin Resonance, Procedures, Adrenocorticotropic Hormone, Electron Spin Resonance Spectroscopy, Pharmacology, Methods,
Affiliations: *** IBB - CNR ***
CNR-Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126 Catania, Italy.
Dipartimento di Scienze Biomediche, Universita Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Consorzio Interuniversitario C.I.R.C.S.M.B., Via C. Ulpiani 27, 70125 Bari, Italy.
Consiglio Nazionale delle Ricerche (CNR
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Semax, an ACTH4-10 peptide analog with high affinity for copper(II) ion and protective ability against metal induced cell toxicity
Heptapeptide Semax, encompassing the sequence 4-7 of N-terminal domain of the adrenocorticotropic hormone (ACTH) and a C-terminal Pro-Gly-Pro tripeptide, belongs to a short regulatory peptides family. This compound has been found to affect learning processes and to exert marked neuroprotective activities on cognitive brain functions. Dys-homeostasis of metal ions is involved in several neurodegenerative disorders and growing evidences have showed that brain is a specialized organ able to concentrate metal ions. In this work, the metal binding ability and protective activity of Semax and its metal complexes were studied. The equilibrium study clearly demonstrated the presence of three complex species. Two minor species [CuL] and [CuLH_(1)](-) co-exist together with the [CuLH_(2)](2-) in the pH range from 3.6 to 5. From pH 5 the [CuLH_(2)](2-) species becomes predominant with the donor atoms around copper arranged in a 4 N planar coordination mode. Noteworthy, a reduced copper induced cytotoxicity was observed in the presence of Semax by MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] assay on a SHSY5Y neuroblastoma and RBE4 endothelial cell lines. (C) 2014 Elsevier Inc. All rights reserved.
Semax, an ACTH4-10 peptide analog with high affinity for copper(II) ion and protective ability against metal induced cell toxicity
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Hesse B, Tagil K, Cuocolo A, Anagnostopoulos C, Bardies M, Bax J, Bengel F, Busemann Sokole E, Davies G, Dondi M, Edenbrandt L, Franken P, Kjaer A, Knuuti J, Lassmann M, Ljungberg M, Marcassa C, Marie PY, Mckiddie F, O'connor M, Prvuolovich E, Underwood R * 3. 0 T perfusion MR imaging(726 views) Rivista Di Neuroradiologia (ISSN: 1120-9976), 2004; 17(6): 807-812. Impact Factor:0.023 ViewExport to BibTeXExport to EndNote