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001-es BibID:BIBFORM106885
035-os BibID:(Wos)000745038000002 (Scopus)85107736138
Első szerző:Bodnár Nikolett (vegyész)
Cím:Ambivalent role of ascorbic acid in the metal-catalyzed oxidation of oligopeptides / Nikolett Bodnár, Katalin Várnagy, Lajos Nagy, Gizella Csire, Csilla Kállay
Dátum:2021
ISSN:0162-0134 1873-3344
Megjegyzések:The effect of ascorbic acid on the metal-catalyzed oxidation of a human prion protein model peptide has been studied. The complex formation of the peptide was clarified first. The studied model peptide contains a methionine and a histidine amino acids which are important both as binding sites for metal ions and sensitive parts of the protein for oxidation. pH-potentiometric, UV?Vis and circular dichroism spectroscopic techniques were applied to study the stoichiometry, stability and structure of the copper(II) complexes, while HPLC-MS and MS/MS were used for identifying the products of metal-catalyzed oxidation. 3N and 4N complexes with (Nim,N?,N?,S) and (Nim,N?,N?,N?) coordination modes are formed at pH?7.4, where the oxidation was studied. Singly, doubly and triply oxidized products are formed in which the methionine and/or the histidine side chain is oxidized. The oxidation was carried out with hydrogen peroxide solution by the addition of metal ions, namely copper(II) and iron(III) and/or ascorbic acid.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Ascorbic acid
Metal-catalyzed oxidation
Copper(II)
Histidine
Methionine
Complex
Megjelenés:Journal of Inorganic Biochemistry. - 222 (2021), p. 111510-111519. -
További szerzők:Várnagy Katalin (1961-) (vegyész) Nagy Lajos (1979-) (vegyész) Csire Gizella (1990-) (vegyész) Kállay Csilla (1978-) (vegyész)
Pályázati támogatás:NKFI-115480
Egyéb
NKFI-128783
Egyéb
ÚNKP-20-5
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM107635
035-os BibID:(WOS)000750182100001 (Scopus)85125446140
Első szerző:Grenács Ágnes (vegyész, analitikus)
Cím:The effect of side chains on the complex formation processes of N-terminally free hexapeptides containing C-terminal cysteinyl functions / Ágnes Grenács, Nikolett Bodnár, Dóra Csilla Pálinkás, Norbert Lihi, Katalin Várnagy
Dátum:2022
ISSN:1144-0546 1369-9261
Megjegyzések:Cysteine containing ligands with free amino- and amidated C-termini were studied and their nickel(II), zinc(II) and cadmium(II) complexes were described in the aspect of their thermodynamic stability and structure, including the preference of the metal ions toward the two anchoring groups. Comparing the investigated ligands, AAASSC-NH2 and AAEAAC-NH2, with the previously studied ones, AAHAAC-NH2 and AADAAC-NH2, it can be stated that the ratio of coordination isomers of nickel(II) complexes can be altered by inserting strongly, weakly or non-coordinating internal amino acid residues. Priority of the C-terminal binding site enhances in an order of AAASSC-NH2 > AAEAAC-NH2 > AADAAC-NH2 > AAHAAC-NH2 forming an (N?,N?,N?,S?) fused chelate system at high pH. Under neutral conditions, in contrast with the former investigated ligands, a machrochelate structure is present in the NiL species without the involvement of amide nitrogen atoms, and in the case of AAEAAC-NH2 the ?-carboxylate function of glutamic acid residue contributes to the stability of this complex. Formation of zinc(II) complexes occurred with the stoichiometry of ZnHL and ZnL, latter containing the amino function in the coordination sphere, too, besides the thiolate (and carboxylate) groups. This finding is in a good agreement with the ligand containing aspartic acid, however, is in contrast with the strongly coordinating histidine peptide, where bis-ligand zinc(II) species were also formed. Bis(ligand) complex formation was more facilitated in case of cadmium(II) ions, except of AAASSC-NH2. All the other three ligands were able to form CdL2H2, CdL2H and CdL2 species meaning that an internal, even only weakly coordinating side chain enables the coordination of two ligands to a metal ion due to the tridentate binding of the peptide.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:New Journal Of Chemistry. - 46 : 8 (2022), p. 3754-3765. -
További szerzők:Bodnár Nikolett (1994-) (vegyész) Pálinkás Dóra Csilla (1997-) (vegyész) Lihi Norbert (1990-) (vegyész) Várnagy Katalin (1961-) (vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00008
GINOP
ÚNKP-21-4-II
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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