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Titolo:
MODIFIED CHEMOTACTIC PEPTIDES - SYNTHESIS, CRYSTAL CONFORMATION, AND ACTIVITY OF FOR-HSE(ME)-LEU-PHE-OME
Autore:
TORRINI I; ZECCHINI GP; PARADISI MP; LUCENTE G; GAVUZZO E; MAZZA F; POCHETTI G; TRANIELLO S; SPISANI S;
Indirizzi:
UNIV ROMA LA SAPIENZA,DIPARTIMENTO STUDI FARMACEUT I-00185 ROME ITALY UNIV ROMA LA SAPIENZA,CNR,CTR STUDIO CHIM FARM I-00185 ROME ITALY CNR,IST STRUTTURIST CHIM G GIACOMELLO ROME ITALY UNIV FERRARA,IST CHIM BIOL I-44100 FERRARA ITALY
Titolo Testata:
Biopolymers
fascicolo: 1, volume: 34, anno: 1994,
pagine: 1 - 9
SICI:
0006-3525(1994)34:1<1:MCP-SC>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-STRUCTURE; PHE-OME; ANALOGS; MET; PHENYLALANINE; CHEMOATTRACTANTS; NEUTROPHILS; ACIDS; AMINO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
I. Torrini et al., "MODIFIED CHEMOTACTIC PEPTIDES - SYNTHESIS, CRYSTAL CONFORMATION, AND ACTIVITY OF FOR-HSE(ME)-LEU-PHE-OME", Biopolymers, 34(1), 1994, pp. 1-9

Abstract

The presence of the sulfur atom of the methionine side chain exerts significant effects at different levels on biochemical behavior of chemotactic N-formylpeptides. In order to acquire more information on thispoint, the synthesis, the conformation in the crystal, and the activity of For-Hse(Me)-Leu-Phe-OMe (2)-an oxygen analogue of For-Met-Leu-Phe-OMe (fMLP-OMe) containing the O-methyl-L-homoserine in place of the native methionine at position 1-is reported. The new analogue 2 adoptsa conformation that is extended at the first two residues and folded at the C-terminal phenylalanine. This conformation is different from that of the parent fMLP-OMe and strikingly similar to that adopted by fMLP-OBu(t). The side-chain spatial orientation of 2 corresponds to that adopted by fMLP-OH when cocrystallized with an immunoglobulin possessing binding properties similar to those of neutrophil receptors. Whentested on human neutrophils the formylpeptide 2 is more active than the parent in the stimulation of directed mobility and maintains both the granule enzyme release activity and the superoxide anion production. (C) 1994 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 09:36:37