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Water induced β-turn modification in a chemotactic tetrapeptide. Synthesis, crystal conformation, and activity of HCO-Met-Leu-ΔZPhe-Phe-OMe

1993; Elsevier BV; Volume: 49; Issue: 2 Linguagem: Inglês

10.1016/s0040-4020(01)80316-1

1464-5416

Ines Torrini, Giampiero Pagani Zecchini, Mario Paglialunga Paradisi, Gino Lucente, E. Gavuzzo, Fernando Mazza, G. Pochetti, Susanna Spisani,

Neuropeptides and Animal Physiology

In order to study the influence of the conformation on the activity and bioselectivity, the new tetrapeptide ligand of the chemotactic formylpeptide receptors HCO-Met-Leu-ΔZPhe-Phe-OMe (2) has been studied. Compound 2 has been designed so as to induce a preferential β-turn conformation with the N-formyl group located outside the backbone loop. The crystallographic analysis reveals that 2 adopts only in part the expected conformation due to the presence of a water molecule isnide the turn. Details on the H-bonding network stabilizing the “open-turn” are given. The tetrapeptide 2 is active towards human neutrophils, stimulating directed migration, superoxide anion generation and lysozyme release. The influence of the backbone conformation on the bioselectivity is discussed.