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Titolo:
Peptoid-peptide hybrids that bind Syk SH2 domains involved in signal transduction
Autore:
Ruijtenbeek, R; Kruijtzer, JAW; van de Wiel, W; Fischer, MJE; Fluck, M; Redegeld, FAM; Liskamp, RMJ; Nijkamp, FP;
Indirizzi:
Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Med Chem, NL-3508 TB Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3508 TB 3508 TB Utrecht, Netherlands Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Pharmacol & Pathophysiol, NL-3508 TB Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3508 TB 3508 TB Utrecht, Netherlands Univ Bern, ME Muller Inst Biomech, CH-3010 Bern, Switzerland Univ Bern Bern Switzerland CH-3010 st Biomech, CH-3010 Bern, Switzerland
Titolo Testata:
CHEMBIOCHEM
fascicolo: 3, volume: 2, anno: 2001,
pagine: 171 - 179
SICI:
1439-4227(20010302)2:3<171:PHTBSS>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; AFFINITY IGE RECEPTOR; SOLID-PHASE SYNTHESIS; FC-EPSILON-RI; MASS-SPECTROMETRIC CHARACTERISTICS; SRC HOMOLOGY-2 DOMAINS; N-SUBSTITUTED GLYCINES; CHEMICAL PHOSPHORYLATION; PHOSPHOTYROSYL PEPTIDE; DRUG DISCOVERY;
Keywords:
peptides; peptidomimetics; peptoids; SH2; domains; signal transduction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Fischer, MJE Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Med Chem, POB80-082, NL-3508 TB Utrecht, Netherlands Univ Utrecht POB 80-082 Utrecht Netherlands NL-3508 TB lands
Citazione:
R. Ruijtenbeek et al., "Peptoid-peptide hybrids that bind Syk SH2 domains involved in signal transduction", CHEMBIOCHEM, 2(3), 2001, pp. 171-179

Abstract

Peptoid-peptide hybrids are oligomeric peptidomimetics that contain one ormore N-substituted glycine residues. In these hybrids, the side chains of one or several amino acids are "shifted" from the alpha -carbon atom to theamide nitrogen atom. A library of phosphorylated peptoid-peptide hybrids derived from the sequence pTyr-Glu-Thr-Leu was synthesized and tested for binding to the tandem SH2 domain of the protein tyrosine kinase Syk. A considerable influence of the side chain position was observed. Compounds 19-21, 24, and 25 comprising a peptoid NpTyr and/or NGlu residue did not show any binding. Compounds 22, 23, and 26 containing an NhThr (hThr = homothreonine) and/or NLeu peptoid residue showed binding with IC50 values that were only five to eight times higher than that of the tetrapeptide lead compound 18. These data show that side chain shifting is possible with retention of binding capacity, but only at the two C-terminal residues of the tetramer. This method of a peptoid scan using peptoid-peptide hybrids appears to be very useful to explore to what extent a peptide sequence can be transformed into a peptoid while retaining its affinity.

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Documento generato il 04/12/20 alle ore 09:48:09