Copper(II) Complexes with Carnosine Conjugates of Hyaluronic Acids at Different Dipeptide Loading Percentages Behave as Multiple SOD Mimics and Stimulate Nrf2 Translocation and Antioxidant Response in In Vitro Inflammatory Model

Autor: Francesco Bellia, Valeria Lanza, Irina Naletova, Barbara Tomasello, Valeria Ciaffaglione, Valentina Greco, Sebastiano Sciuto, Pietro Amico, Rosanna Inturri, Susanna Vaccaro, Tiziana Campagna, Francesco Attanasio, Giovanni Tabbì, Enrico Rizzarelli

Publikováno v: Antioxidants, Vol 12, Iss 8, p 1632 (2023)

A series of copper(II) complexes with the formula [Cu2+Hy(x)Car%] varying the molecular weight (MW) of Hyaluronic acid (Hy, x = 200 or 700 kDa) conjugated with carnosine (Car) present at different loading were synthesized and characterized via differ

Externí odkaz: https://doaj.org/article/1a23f477b93147f688413a27bf50edfb

Copper(II) Coordination Abilities of the Tau Protein's N-Terminus Peptide Fragments: A Combined Potentiometric, Spectroscopic and Mass Spectrometric Study

Autor: Márton, Lukács, Györgyi, Szunyog, Ágnes, Grenács, Norbert, Lihi, Csilla, Kállay, Giuseppe, Di Natale, Tiziana, Campagna, Valeria, Lanza, Giovanni, Tabbi, Giuseppe, Pappalardo, Imre, Sóvágó, Katalin, Várnagy

Publikováno v: ChemPlusChem. 84(11)

Copper(II) complexes of the N-terminal peptide fragments of tau protein have been studied by potentiometric and various spectroscopic techniques (UV-vis, CD, ESR and ESI-MS). The octapeptide Tau(9-16) (Ac-EVMEDHAG-NH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a28c58459ff290e61bca7415a0933243
https://pubmed.ncbi.nlm.nih.gov/31943878

Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end

Autor: Armando Zarrelli, Giovanni Di Fabio, Jan Balzarini, Carmelo La Rosa, Emanuela Crisafi, Tiziana Campagna, Maria Gaglione, Alessandro D'Urso, Anna Messere, Danilo Milardi, Valeria Romanucci

Publikováno v: Bioorganic & medicinal chemistry
22 (2014): 960–966. doi:10.1016/j.bmc.2013.12.051
info:cnr-pdr/source/autori:Romanucci, Valeria; Milardi, Danilo; Campagna, Tiziana; Gaglione, Maria; Messere, Anna; D'Urso, Alessandro; Crisafi, Emanuela; La Rosa, Carmelo; Zarrelli, Armando; Balzarini, Jan; Di Fabio, Giovanni/titolo:Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end/doi:10.1016%2Fj.bmc.2013.12.051/rivista:Bioorganic & medicinal chemistry (Print)/anno:2014/pagina_da:960/pagina_a:966/intervallo_pagine:960–966/volume:22

Novel conjugated G-quadruplex-forming d(TG(3)AG) oligonucleotides, linked to hydrophobic groups through phosphodiester bonds at 5'-end, have been synthesized as potential anti-HIV aptamers, via a fully automated, online phosphoramidite-based solid-ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43245831b806ef7262e1feaf950548c1
http://hdl.handle.net/11591/235602

A doppel α-helix peptide fragment mimics the copper(II) interactions with the whole protein

Autor: Carla Isernia, Tiziana Campagna, Antonio Magrì, Diego La Mendola, Enrico Rizzarelli, Luca Raiola, Örjan Hansson, Maria Anna Campitiello, Raffaele P. Bonomo

Publikováno v: Chemistry-A European Journal 16 (2010): 6212–6223. doi:10.1002/chem.200902405
info:cnr-pdr/source/autori:D. La Mendola; A. Magrì; T. Campagna; M.A. Campitiello; L. Raiola; C. Isernia; Ö. Hansonn; R. P. Bonomo; E. Rizzarelli/titolo:A doppel halfa-helix peptide fragment mimics the copper(II) interactions with the whole protein/doi:10.1002%2Fchem.200902405/rivista:Chemistry-A European Journal/anno:2010/pagina_da:6212/pagina_a:6223/intervallo_pagine:6212–6223/volume:16

The doppel protein (Dpi) is the first homologue of the prion protein (PrP C) to be discovered; it is overexpressed in transgenic mice that lack the prion gene, resulting in neurotoxicity. The whole prion protein is able to inhibit Dpi neurotoxicity,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85f4882023fe2e8077c8e31c82292463
http://hdl.handle.net/11591/197076

Copper(II) binding of prion protein's octarepeat model peptides

Autor: Giuseppe Pappalardo, Giuseppe Impellizzeri, Tiziana Campagna

Publikováno v: Inorganica Chimica Acta (Testo stamp.) 357 (2004): 185–194. doi:10.1016/S0020-1693(03)00492-4
info:cnr-pdr/source/autori:Giuseppe Pappalardo1; Giuseppe Impellizzeri2; Tiziana Campagna1/titolo:Copper(II) binding of prion protein's octarepeat model peptides/doi:10.1016%2FS0020-1693(03)00492-4/rivista:Inorganica Chimica Acta (Testo stamp.)/anno:2004/pagina_da:185/pagina_a:194/intervallo_pagine:185–194/volume:357

The complexes between copper(II) and the synthetic octapeptide fragments of the prion protein Ac-GWGQPHGG-NH 2 ( 1 ), Ac-PHGGGWGQ-NH 2 ( 3 ) and the cyclic analogue c-(GWGQPHGG) ( 2 ) have been comparatively investigated by circular dichroism (CD), a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c36bb5b7a500f76e2dd87170f038f6a8
https://publications.cnr.it/doc/179385