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Titolo:
Conformationally constrained analogues of endogenous tripeptide inhibitorsof zinc metalloproteinases
Autore:
DAlessio, S; Gallina, C; Gavuzzo, E; Giorhano, C; Gorini, B; Mazza, F; Paradisi, MP; Panini, G; Pochettic, G;
Indirizzi:
Univ G DAnnunzio, Ist Sci Farmaco, Dipartimento Sci Farmaco, I-66100 Chieti, Italy Univ G DAnnunzio Chieti Italy I-66100 Sci Farmaco, I-66100 Chieti, Italy Polifarma Res Ctr, I-00185 Rome, Italy Polifarma Res Ctr Rome Italy I-00185 ifarma Res Ctr, I-00185 Rome, Italy CNR, Ist Strutturist Chim, I-00016 Monterotondo, Rome, Italy CNR Monterotondo Rome Italy I-00016 im, I-00016 Monterotondo, Rome, Italy Univ Rome La Sapienza, CNR, Ctr Studio Chim Farmaco, I-00185 Rome, Italy Univ Rome La Sapienza Rome Italy I-00185 im Farmaco, I-00185 Rome, Italy Univ Aquila, Dipartimento Chim Ingn Chim & Mat, I-67010 Coppito, Italy Univ Aquila Coppito Italy I-67010 ngn Chim & Mat, I-67010 Coppito, Italy
Titolo Testata:
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
fascicolo: 1, volume: 36, anno: 2001,
pagine: 43 - 53
SICI:
0223-5234(200101)36:1<43:CCAOET>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PICTET-SPENGLER REACTION; MATRIX METALLOPROTEINASES; ADAMALYSIN-II; VENOM METALLOPROTEINASE; DRUG DESIGN; COLLAGENASE; PEPTIDES;
Keywords:
2-acylamino-3-oxohexahydroindolizino[8,7-b]indole carboxylates; crystal structure; adamalysin II; matrix metalloproteinases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Gallina, C Univ G DAnnunzio, Ist Sci Farmaco, Dipartimento Sci Farmaco, Via Vestini, I-66100 Chieti, Italy Univ G DAnnunzio Via Vestini Chieti ItalyI-66100 hieti, Italy
Citazione:
S. D'Alessio et al., "Conformationally constrained analogues of endogenous tripeptide inhibitorsof zinc metalloproteinases", EUR J MED C, 36(1), 2001, pp. 43-53

Abstract

Two diastereomeric furan-2-carbonylamino-3-oxohexahydroindolizino[8,7-b]indole carboxylates, highly constrained analogues of endogenous pyroglutamyl tripeptide inhibitors of snake venom endopeptidases, have been prepared as potential inhibitors of adamalysin II and matrix metalloproteinases. They proved to be inactive against adamalysin II and weak inhibitors of gelatinase A, gelatinase B, stromelysin 1 and human neutrophyl collagenase. Evaluation of the mode of binding of the (2R,5S,11bR) isomer in the active site of adamalysin II suggests that the decrease of potency may be due to the reorientation of the acylamino chain in three of the heterocyclic nucleus, to a short contact at the entrance of the S-1' hydrophobic cleft and to the lossof flexibility of the tetracyclic nucleus in the P-1', P-2' region of the inhibitor, which prevents optimal arrangement in the S-1' specificity subsite. (C) 2001 Editions scientifiques et medicales Elsevier SAS.

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Documento generato il 23/09/20 alle ore 09:37:16