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Titolo:
Structure-activity investigation of the inhibition of 3-hydroxypyridin-4-ones on mammalian tyrosine hydroxylase
Autore:
Liu, ZD; Lockwood, M; Rose, S; Theobald, AE; Hider, RC;
Indirizzi:
Univ London Kings Coll, Dept Pharm, London SE1 8WA, England Univ London Kings Coll London England SE1 8WA m, London SE1 8WA, England Univ London Kings Coll, GKT Sch Biomed Sci, Neurodegenerat Disorders Res Ctr, London SE1 1UL, England Univ London Kings Coll London England SE1 1ULr, London SE1 1UL, England
Titolo Testata:
BIOCHEMICAL PHARMACOLOGY
fascicolo: 3, volume: 61, anno: 2001,
pagine: 285 - 290
SICI:
0006-2952(20010201)61:3<285:SIOTIO>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
IRON CHELATORS; PHYSICOCHEMICAL PROPERTIES; BIOLOGICAL EVALUATION; BINDING; SITE;
Keywords:
iron chelators; hydroxypyridinone; tyrosine hydroxylase; lipophilicity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Hider, RC Univ London Kings Coll, Dept Pharm, London SE1 8WA, England UnivLondon Kings Coll London England SE1 8WA SE1 8WA, England
Citazione:
Z.D. Liu et al., "Structure-activity investigation of the inhibition of 3-hydroxypyridin-4-ones on mammalian tyrosine hydroxylase", BIOCH PHARM, 61(3), 2001, pp. 285-290

Abstract

3-Hydroxypyridin-4-ones are currently one of the main candidates for the development of orally active iron chelators. Small bidentate ligands lend toinhibit iron-containing metalloenzymes and therefore can cause undesirableside effects. A range of 3-hydroxypyridin-4-ones with different R-2 substitutents was selected for the investigation of the structure-activity relationship between the chemical nature of the ligand and the inhibition of mammalian tyrosine: hydroxylase. Results indicated that lipophilicity was the dominant factor in controlling the ability of this class of chelator to inhibit mammalian tyrosine hydroxylase. Ligands with hydrophilic R-2 substitutents tended to be weak inhibitors. No significant correlation was found in this study between iron-binding affinity, extended R-2 chain length, and enzyme inhibitory activity. In contrast, both the LogP values of the entire molecule and of the R-2 segment correlated well with inhibitory activity. (C)2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:06:16