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Titolo:
Protease inhibitors: Synthesis of a series of bacterial collagenase inhibitors of the sulfonyl amino acyl hydroxamate type
Autore:
Clare, BW; Scozzafava, A; Supuran, CT;
Indirizzi:
Univ Western Australia, Dept Chem, Crawley, WA 6009, Australia Univ Western Australia Crawley WA Australia 6009 wley, WA 6009, Australia Univ Florence, Lab Chim Inorgan & Bioinorgan, I-50121 Florence, Italy UnivFlorence Florence Italy I-50121 Bioinorgan, I-50121 Florence, Italy
Titolo Testata:
JOURNAL OF MEDICINAL CHEMISTRY
fascicolo: 13, volume: 44, anno: 2001,
pagine: 2253 - 2258
SICI:
0022-2623(20010621)44:13<2253:PISOAS>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBONIC-ANHYDRASE INHIBITORS; CLOSTRIDIUM-HISTOLYTICUM COLLAGENASE; MATRIX-METALLOPROTEINASE INHIBITORS; HUMAN NEUTROPHIL COLLAGENASE; LOWERING AROMATIC/HETEROCYCLIC SULFONAMIDES; INDIVIDUAL COLLAGENASES; OCULAR PHARMACOLOGY; POTENT INHIBITORS; DRUG DESIGN; MOIETIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Clare, BW Univ Western Australia, Dept Chem, 35 Stirling Highway, Crawley,WA 6009, Australia Univ Western Australia 35 Stirling Highway Crawley WA Australia 6009
Citazione:
B.W. Clare et al., "Protease inhibitors: Synthesis of a series of bacterial collagenase inhibitors of the sulfonyl amino acyl hydroxamate type", J MED CHEM, 44(13), 2001, pp. 2253-2258

Abstract

A series of sulfonyl amino acyl hydroxamates incorporating alkyl/arylsulfonyl-N-2-nitrobenzyl-L-alanine was prepared. Related compounds were obtainedby reaction of N-2-nitrobenzyl-L-Ala with aryl isocyanates, arylsulfonyl isocyanates, or benzoyl isothiocyanate, followed by the conversion of the COOH into the CONHOH moiety. The new compounds were assayed as inhibitors of the Clostridium histolyticum collagenase (ChC), a bacterial protease involved in the degradation of extracellular matrix. Many of the obtained hydroxamates proved to be effective bacterial collagenase inhibitors, the main contributor to activity being the substitution pattern at the sulfonamido moiety. The best ChC inhibitors were those containing pentafluorophenylsulfonyland 3- and 4-protected-aminophenylsulfonyl P-1 groups among others, with affinities in the low nanomolar range. This study also proves that the 2-nitrobenzyl- moiety, similarly to the 4-nitrobenyl one previously investigated(Scozzafava, A.; Supuran, C. T. J. Med. Chem. 2000, 43, 1858-1865) is an efficient P-2 anchoring moiety for obtaining potent bacterial collagenase inhibitors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:28:32