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001-es BibID:	BIBFORM119588
035-os BibID:	(cikkazonosító)795 (Scopus)85186265754 (WoS)001172372500001
Első szerző:	Székely Enikő (vegyész)
Cím:	Characterization of Copper(II) and Zinc(II) Complexes of Peptides Mimicking the CuZnSOD Enzyme / Enikő Székely, Mariann Molnár, Norbert Lihi, Katalin Várnagy
Dátum:	2024
ISSN:	1420-3049
Megjegyzések:	Antimicrobial peptides are short cationic peptides that are present on biological surfaces susceptible to infection, and they play an important role in innate immunity. These peptides, like other compounds with antimicrobial activity, often have significant superoxide dismutase (SOD) activity. One direction of our research is the characterization of peptides modeling the CuZnSOD enzyme and the determination of their biological activity, and these results may contribute to the development of novel antimicrobial peptides. In the framework of this research, we have synthesized 10, 15, and 16-membered model peptides containing the amino acid sequence corresponding to the Cu(II) and Zn(II) binding sites of the CuZnSOD enzyme, namely the Zn(II)-binding HVGD sequence (80?83. fragments), the Cu(II)-binding sequence HVH (fragments 46?48), and the histidine (His63), which links the two metal ions as an imidazolate bridge: Ac-FHVHEGPHFN-NH2 (L1(10)), Ac-FHVHAGPHFNGGHVG-NH2 (L2(15)), and Ac-FHVHEGPHFNGGHVGD-NH2 (L3(16)). pH-potentiometric, UV-Vis-, and CD-spectroscopy studies of the Cu(II), Zn(II), and Cu(II)-Zn(II) mixed complexes of these peptides were performed, and the SOD activity of the complexes was determined. The binding sites preferred by Cu(II) and Zn(II) were identified by means of CD-spectroscopy. From the results obtained for these systems, it can be concluded that in equimolar solution, the ?(NGG)HVGD- sequence of the peptides is the preferred binding site for copper(II) ion. However, in the presence of both metal ions, according to the native enzyme, the -HVGD- sequence offers the main binding site for Zn(II), while the majority of Cu(II) binds to the -FHVH- sequence. Based on the SOD activity assays, complexes of the 15- and 16-membered peptide have a significant SOD activity. Although this activity is smaller than that of the native CuZnSOD enzyme, the complexes showed better performance in the degradation of superoxide anion than other SOD mimics. Thus, the incorporation of specific amino acid sequences mimicking the CuZnSOD enzyme increases the efficiency of model systems in the catalytic decomposition of superoxide anion.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk multihistidine peptide Cu(II)-complex Zn(II)-complex SOD activity CuZnSOD
Megjelenés:	Molecules. - 29 : 4 (2024), p. 1-27. -
További szerzők:	Molnár Marianna Lihi Norbert (1990-) (vegyész) Várnagy Katalin (1961-) (vegyész)
Pályázati támogatás:	ÚNKP-22-5 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM102109
035-os BibID:	(cikkazonosító)3435 (WoS)000808816800001 (Scopus)85131653251
Első szerző:	Székely Enikő (vegyész)
Cím:	The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides / Enikő Székely, Gizella Csire, Bettina Diána Balogh, Judit Zsuzsa Erdei, Judit Mária Király, Judit Kocsi, Júlia Pinkóczy, Katalin Várnagy
Dátum:	2022
ISSN:	1420-3049
Megjegyzések:	The systematic studies of copper(II), nickel(II) and zinc(II) ion complexes of protected multihistidine peptides containing amino acids with different side chains (Ac-SarHAH-NH2, Ac-HADH-NH2, Ac-HDAH-NH2, Ac-HXHYH-NH2 X, Y = A, F, D or K, Ac-HXHAHXH-NH2, X = F or D) have provided information about the metal ion and protein interaction and have made it possible to draw conclusions regarding general trends in the coordination of metal complexes of multihistidine peptides. The stability of the metal complexes significantly depends on the position of the histidines and amino acids, which are present in the neighbourhood of the histidine amino acids as well. The most significant effect was observed on peptides containing aspartic acid or phenylalanine. The redox parameters of complexes, however, depend on the number and position of histidines, and the other side chain donor atoms have practically no effect on the electrochemical properties of imidazole-coordinated species. However, the presence of aspartic acid side chains results in a more distorted geometry of amide-coordinated species and increases the reducibility of these complexes.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk multihisztidin peptidek réz(II) nikkel(II) cink(II) komplex stabilitási állandók electrokémiai paraméterek
Megjelenés:	Molecules. - 27 (2022), p. 1-29. -
További szerzők:	Csire Gizella (1990-) (vegyész) Balogh Bettina Diána (1994-) (vegyész) Erdei Judit Zsuzsa (1992-) (vegyész) Király Judit Mária Kocsi Judit Pinkóczy Júlia Várnagy Katalin (1961-) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: