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Titolo:
Peptides containing the sulfonamide junction. 2. Structure and conformation of Z-Tau-Pro-D-Phe-NHiPr
Autore:
Calcagni, A; Gavuzzo, E; Lucente, G; Mazza, F; Morera, E; Paradisi, MP; Rossi, D;
Indirizzi:
Univ La Sapienza, Ctr Studio Chim Farmaco, CNR, Dipartimento Studi Farmaceut, I-00185 Rome, Italy Univ La Sapienza Rome Italy I-00185 Studi Farmaceut, I-00185 Rome, Italy CNR, Ist Strutturist Chim, I-00016 Monterotondo, Roma, Italy CNR Monterotondo Roma Italy I-00016 im, I-00016 Monterotondo, Roma, Italy Univ Aquila, Dipartimento Chim Ingn Chim & Mat, I-67010 Laquila, Italy Univ Aquila Laquila Italy I-67010 ngn Chim & Mat, I-67010 Laquila, Italy
Titolo Testata:
BIOPOLYMERS
fascicolo: 6, volume: 54, anno: 2000,
pagine: 379 - 387
SICI:
0006-3525(200011)54:6<379:PCTSJ2>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE ISOSTERE; SOLID-PHASE SYNTHESIS; ROTATING-FRAME; PEPTIDOMIMETICS; SULFINAMIDE; INHIBITORS; PEPTIDOSULFONAMIDES; PSEUDOPEPTIDES; RECEPTORS; CRYSTAL;
Keywords:
conformation; crystal structure; nitrogen pyramidalization; pseudopeptides; sulfonamides; sulfonamido-peptides; taurine;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Lucente, G Univ La Sapienza, Ctr Studio Chim Farmaco, CNR, Dipartimento Studi Farmaceut, I-00185 Rome, Italy Univ La Sapienza Rome Italy I-00185 ceut, I-00185 Rome, Italy
Citazione:
A. Calcagni et al., "Peptides containing the sulfonamide junction. 2. Structure and conformation of Z-Tau-Pro-D-Phe-NHiPr", BIOPOLYMERS, 54(6), 2000, pp. 379-387

Abstract

The taurine (Tau) containing N-protected pseudotripeptide isopropylamide Z-Tau-Pro-D-Phe-NHiPr (1) has been specifically designed and synthesized as suitable model to test the ability of the sulfonamido group to participate as II-bond acceptor to a type II beta -turn and to get information on the preferred rotameric conformation around the S-N bond and the hybridization stale of the nitrogen atom. The present structural investigation reveals that, although the sulfonamide junction is invariably folded in a gauche mode,the beta -turn structure, stabilized by the 4 --> 1 hydrogen bond, is not found in the crystal and the sulfonamido oxygen atoms are not involved in any intra- or intermolecular hydrogen-bond interaction. More than one conformer populates the CDCl3 solution with only a minor contribution by the expected beta -turn. The Pro nitrogen is significantly pyramidalized and the nitrogen lone pair points in opposite direction to that of the Pro (CH)-H-alpha bond thus adopting R chirality, in an arrangement practically identical to that found in the previously studied homochiral analogue Z-Tau-Pro-Phe-NHiPr. (C) 2000 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 16:13:05