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Titolo:
Peptide T revisited: Conformational mimicry of epitopes of anti-HIV proteins
Autore:
Picone, D; Rivieccio, A; Crescenzi, O; Caliendo, G; Santagada, V; Perissutti, E; Spisani, S; Traniello, S; Temussi, PA;
Indirizzi:
Univ Naples Federico II, Dipartimento Chim, I-80126 Naples, Italy Univ Naples Federico II Naples Italy I-80126 Chim, I-80126 Naples, Italy Univ Naples Federico II, Dipartimento Chim Organ & Biochim, I-80126 Naples, Italy Univ Naples Federico II Naples Italy I-80126 chim, I-80126 Naples, Italy Univ Naples Federico II, Dipartimento Chim Farmaceut & Tossicol, I-80126 Naples, Italy Univ Naples Federico II Naples Italy I-80126 icol, I-80126 Naples, Italy Univ Ferrara, Dipartimento Biochim & Biol Mol, I-44100 Ferrara, Italy UnivFerrara Ferrara Italy I-44100 im & Biol Mol, I-44100 Ferrara, Italy
Titolo Testata:
JOURNAL OF PEPTIDE SCIENCE
fascicolo: 4, volume: 7, anno: 2001,
pagine: 197 - 207
SICI:
1075-2617(200104)7:4<197:PTRCMO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; RECEPTOR-BINDING; LINEAR PEPTIDES; CD4 RECEPTOR; PENTAPEPTIDE; INFECTIVITY; ENVELOPE; SPECTROSCOPY; CHEMOKINES; CHEMOTAXIS;
Keywords:
chemotactic activity; conformation; HIV; NMR; peptide T;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Picone, D Univ Naples Federico II, Dipartimento Chim, Via Cintia,ComplessoUniv Monte S Angelo, I-80126 Naples, Italy Univ Naples Federico II Via Cintia,Complesso Univ Monte S Angelo Naples Italy I-80126
Citazione:
D. Picone et al., "Peptide T revisited: Conformational mimicry of epitopes of anti-HIV proteins", J PEPT SCI, 7(4), 2001, pp. 197-207

Abstract

Peptide T (ASTITNYT), a fragment corresponding to residues 185- 192 of gp120, the coat protein of HIV, is endowed with several biological properties In vitro, notably inhibition of the binding of both isolated gp120 and HI-1to the CD4 receptor, and chemotactic activity. Based on previous nuclear magnetic resonance (NMR) studies performed in our laboratory, which were consistent with a regular conformation of the C-terminal pentapeptide, and SARstudies showing that the C-terminal pentapeptide retains most of the biological properties, we designed eight hexapeptides containing in the central part either the TNYT or the TTNY sequence, and charged residues (D/E/R) at the two ends. Conformational analysis based on NMR and torsion angle dynamics showed that all peptides assume folded conformations, albeit with different geometries and stabilities. In particular, peptides carrying an acidic residue at the N-terminus and a basic residue at the C-terminus are characterized by stable helical structures and retain full chemotactic activity. The solution conformation of peptide ETNYTR displays strong structural similarity to the region 19-26 of both bovine pancreatic and bovine seminal ribonuclease, which are endowed with anti-HIV activity. Moreover, the frequent occurrence, in many viral proteins, of TNYT and TTNY, the two core sequences employed in the design of the hexapeptides studied in the present work, hints that the sequence of the C-terminal pentapeptide TTNYT is probably representative of a widespread viral recognition motif. Copyright (C) 2001 European Peptide Society and John Wiley Br Sons, Ltd.

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Documento generato il 22/01/20 alle ore 21:38:33