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001-es BibID:	BIBFORM107634
035-os BibID:	(Wos)000724573400005 (Scopus)85104557504
Első szerző:	Chaves, Sílvia
Cím:	Recent Multi-target Approaches on the Development of Anti- Alzheimer's Agents Integrating Metal Chelation Activity / Sílvia Chaves, Katalin Várnagy, M. Amélia Santos
Dátum:	2021
ISSN:	0929-8673
Megjegyzések:	Alzheimer's disease (AD) is the most common and severe age-dependent neurodegenerative disorder, worldwide. Notwithstanding the large amount of research dedicated to both the elucidation of this pathology and the development of an effective drug, the multifaceted nature and complexity of the disease are certainly a rationale for the absence of cure so far. Current available drugs are used, mainly, to compensate the decline of the neurotransmitter acetylcholine by acetylcholinesterase (AChE) inhibition, though they only provide temporary symptomatic benefits and cannot stop AD progression. Although the multiple factors that contribute to trigger AD onset and progression are not yet fully understood, several pathological features and underneath pathways have been recognized to contribute to its pathology, such as metal dyshomeostasis, protein misfolding, oxidative stress and neurotransmitter deficiencies, some of them being interconnected. Thus, there is a widespread recent interest in the development of multitarget-directed ligands (MTDLs) for simultaneous interaction with several pathological targets of AD. In this review, a selection of the most recent reports (2016-up to present) on metal chelators of MTDLs with multifunctionalities is presented. These compounds enable the hitting of several AD targets or pathways, such as modulation of specific biometal ions (e.g. Cu, Fe, Zn) and of protein misfolding (?-amyloid and tau protein), anti-oxidant activity and AChE inhibition. The properties found for these hybrids are discussed in comparison with the original reference compounds, some MTDLs being outlined as leading compounds for pursuing future studies in view of efficient potential applications in AD therapy.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Alzheimer's disease multitarget drugs biometals metal chelators AChE inhibitors antioxidant properties drug repositioning
Megjelenés:	Current Medicinal Chemistry. - 28 : 35 (2021), p. 7247-7277. -
További szerzők:	Várnagy Katalin (1961-) (vegyész) Santos, M. Amélia
Pályázati támogatás:	OTKA-115480 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM107637
035-os BibID:	(Scopus)85161610965 (WoS)001028904000001
Első szerző:	Sóvágó Imre (vegyész)
Cím:	Interactions of copper(II) and zinc(II) ions with the peptide fragments of proteins related to neurodegenerative disorders: similarities and differences / Imre Sóvágó, Katalin Várnagy, Csilla Kállay, Ágnes Grenács
Dátum:	2023
ISSN:	0929-8673
Megjegyzések:	Metal binding ability and coordination modes of the copper(II) and zinc(II) complexes of various peptide fragments of prion, amyloid-beta and tau proteins are summarized in this review. Imidazole-N donors are the primary metal binding sites of all three proteins but the difference in the location of these residues and the presence or absence of other coordinating side chains results in significant differences in the complex formation processes. The presence of macrochelates and the possibility of the formation of multi-copper complexes is the most characteristic for prion fragments. Amyloid-? can form high stability complexes with both copper(II) and zinc(II) ions but the preferred binding sites are different for the two metal ions. Similar observations have been obtained for the tau fragments but the metal ion selectivity of the various fragments is even more pronounced. In addition to the complex formation, copper(II) ions can play an important role in the various oxidative reactions of peptides. Results of the metal ion catalyzed oxidation of peptide fragments of prion, amyloid-? and tau proteins are also summarized. Amino acid side chain oxidation (mostly methionine, histidine and aspartic acid) and protein fragmentations are the most common consequences of this process.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Current Medicinal Chemistry. - 30 : 36 (2023), p. 4050-4071. -
További szerzők:	Várnagy Katalin (1961-) (vegyész) Kállay Csilla (1978-) (vegyész) Grenács Ágnes (1988-) (vegyész, analitikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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