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001-es BibID:	BIBFORM018698
Első szerző:	Enyedy Éva Anna (vegyész)
Cím:	Interaction of folic acid and some matrix metalloproteinase (MMP) inhibitor folate-[gamma]-hydroxamate derivatives with Zn(II) and human serum albumin / Éva A. Enyedy, Etelka Farkas, Orsolya Dömötör, M. Amélia Santos
Dátum:	2011
ISSN:	0162-0134
Megjegyzések:	Human serum albumin binding of folic acid and its [gamma]-hydroxamate/carboxylate derivatives was studied byultrafiltration and spectrofluorimetry, and it was found that the ligands exhibit a moderate binding (KD ~2?50 ?M), and the folate-[gamma]-phenylalanine represents the highest conditional binding constant towards albumin.This feature may have importance in the serum transport processes of these ligands. Interaction of folic acidand its derivatives with Zn(II) was investigated in aqueous solution to obtain the composition and stabilitiesof the complexes by the means of pH-potentiometry, 1H NMR and electrospray ionization mass spectrometry,together with the characterization of the proton dissociation processes and the hydro-lipophilic properties ofthe ligands. The formation of mono-ligand complexes was demonstrated in all cases and the contribution ofthe glutamyl carboxylates to the coordination was excluded. Binding of folic acid and its [gamma]-carboxylatederivatives to Zn(II) via the pteridine moiety is suggested, while the (O,O) coordination fashion of the folate-[gamma]-hydroxamate ligands has importance in their inhibitory activity against Zn(II)-containing matrixmetalloproteinases. It was found that the enzyme inhibition of these folate-[gamma]-hydroxamate ligands is mainlytuned by other features, such as the lipophilic character rather than the Zn(II)-chelate stability.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Molekulatudomány Solution equilibrium Stability constants Folic acid Folate-[gamma]-hydroxamate conjugates Protein-[gamma]-ligand interaction Ultrafiltration
Megjelenés:	Journal Of Inorganic Biochemistry. - 105 : 3 (2011), p. 444-453. -
További szerzők:	Farkas Etelka (1948-) (vegyész) Dömötör Orsolya Santos, Amélia M.
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Fémionok és biológiailag aktív hidroxámsavak kölcsönhatása
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001-es BibID:	BIBFORM089447
035-os BibID:	(cikkazonosító)110963 (WoS)000528628200017 (Scopus)85076831661
Első szerző:	Kozsup Máté (Okleveles vegyész)
Cím:	Synthesis, characterization and albumin binding capabilities of quinizarin containing ternary cobalt(III) complexes / Kozsup Máté, Dömötör Orsolya, Nagy Sándor, Farkas Etelka, Enyedy Éva A., Buglyó Péter
Dátum:	2020
ISSN:	0162-0134 1873-3344
Megjegyzések:	Four Co(III) ternary complexes with the composition of [(Co(4 N))2(quin)](ClO4)4 or [(Co(4 N))2(quinS)](ClO4)3, where 4 N =tris(2aminoethyl)amine (tren) or tris(2-pyridylmethyl)amine (tpa), quinH2 = quinizarin (1,4-dihydroxy-9,10-anthraquinone), quinSH3 = quinizarin-2-sulfonic acid (1,4-dihydroxy-9,10-anthraquinone2-sulfonic acid), were synthesized, characterized and their human serum albumin (HSA) binding capabilities were also tested. The complexes can be considered as likely chaperons of quinizarins which are structural models for anthracycline-based anticancer drugs like doxorubicin. All the Co(III) complexes are dinuclear and were isolated as mixture of isomers. Comparison of the cyclic voltammograms of the free ligands and the appropriate Co(III) complexes revealed that the new signals belonging to reversible processes in the range ?400?0 mV (vs. Ag/AgCl) for the complexes can be attributed to the reversible reduction of the Co(III) centre. These potentials are in the range of typical (O,O) chelated Co(III) ternary complexes bearing 4 N donor ligands and follow the order being more positive for the tpa containing complexes. Presence of the sulfonate group in the quinizarin results in slightly more negative reduction potential of the Co(III) complexes. HSA binding capabilities of the quinH2 and quinSH3 ligands as well as the appropriate complexes showed that quinSH3 has higher affinity to the protein than quinH2 while none of the complexes seem to bind to HSA.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Inorganic Biochemistry. - 204 (2020), p. 1-9. -
További szerzők:	Dömötör Orsolya Nagy Sándor (1993-) (vegyész) Farkas Etelka (1948-) (vegyész) Enyedy Éva Anna (1975-) (vegyész) Buglyó Péter (1965-) (vegyész)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00008 GINOP OTKA-112317 OTKA Egyéb GINOP ÚNKP19-3-I-DE-45 Egyéb ÚNKP19-3-I-DE-56 Egyéb
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