The role exercised by the central residue of the chemotactic N-formyltripeptide HCO-Met-Leu-Phe-OMe (fMLP-OMe) in controlling both the backbone conformation and the biochemical activity is the subject of recent interest. Here, two new centrally constrained fMLP-OMe analogues, namely HCO-Met-azaPro-Phe-OMe (4) and HCO-Met-(γ-lactam)-Phe-OMe (6) have been synthesized and their CDCl3 solution conformation and activity have been studied. The azapeptide 4 adopts β-folded conformation with the azaPro residue at the i+2 position and an intramolecular H-bond involving the formylic oxygen and the Phe NH. The γ-lactam tripeptide 6 prefers a semi-extended backbone conformation. When tested on human neutrophils both the new models were found practically devoid of biological activity. The role exerted by the NH groups as well as by the conformational preferences is discussed.

Pagani Zecchini, G., Paglialunga Paradisi, M., Torrini, I., Lucente, G., Mastropietro, G., Paci, M., et al. (1996). Centrally constrained chemotactic N-formyltripeptides: Synthesis, conformation, and activity of two new analogues. ARCHIV DER PHARMAZIE, 329(12).

Centrally constrained chemotactic N-formyltripeptides: Synthesis, conformation, and activity of two new analogues

PACI, MAURIZIO;
1996

Abstract

The role exercised by the central residue of the chemotactic N-formyltripeptide HCO-Met-Leu-Phe-OMe (fMLP-OMe) in controlling both the backbone conformation and the biochemical activity is the subject of recent interest. Here, two new centrally constrained fMLP-OMe analogues, namely HCO-Met-azaPro-Phe-OMe (4) and HCO-Met-(γ-lactam)-Phe-OMe (6) have been synthesized and their CDCl3 solution conformation and activity have been studied. The azapeptide 4 adopts β-folded conformation with the azaPro residue at the i+2 position and an intramolecular H-bond involving the formylic oxygen and the Phe NH. The γ-lactam tripeptide 6 prefers a semi-extended backbone conformation. When tested on human neutrophils both the new models were found practically devoid of biological activity. The role exerted by the NH groups as well as by the conformational preferences is discussed.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
English
Con Impact Factor ISI
γ-lactam; Azaproline-containing peptides; Chemotaxis; Formylpeptides
http://onlinelibrary.wiley.com/doi/10.1002/ardp.19963291202/pdf
Pagani Zecchini, G., Paglialunga Paradisi, M., Torrini, I., Lucente, G., Mastropietro, G., Paci, M., et al. (1996). Centrally constrained chemotactic N-formyltripeptides: Synthesis, conformation, and activity of two new analogues. ARCHIV DER PHARMAZIE, 329(12).
Pagani Zecchini, G; Paglialunga Paradisi, M; Torrini, I; Lucente, G; Mastropietro, G; Paci, M; Spisani, S
Articolo su rivista
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/44160
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact