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Modifications of the amide bond at position 3 in fMLP analogs select neutrophil functions.
- S. Spisani, A. Breveglieri, E. Fabbri, G. Vertuani, O. Rizzuti, G. Cavicchioni
- Chemistry, BiologyPeptide research
- 1 November 1996
The results indicate that this amide bond is required for optimal chemotactic activity, but not for superoxide anion production.
The Importance of the Peptide Bond at Position 2 in HCO‐Met‐Leu‐Phe‐OMe Analogues as shown by Studies on Human Neutrophils
- G. Cavicchioni, A. Breveglieri, M. Boggian, G. Vertuani, E. Reali, S. Spisani
- Chemistry, BiologyJournal of peptide science : an official…
- 1 May 1996
The formylpeptides formyl‐methionyl‐Nmethylleucyl‐ phenylaline methyl ester and analogue 2 were synthesized in order to investigate the role of the amide bond at position 2 on biological activities on human neutrophils.
Design and Synthesis of 1-Aminocycloalkane-1-carboxylic Acid-Substituted Deltorphin Analogues: Unique δ and μ Opioid Activity in Modified Peptides
Deltorphin analogues were substituted by a series of achiral Cα,α-dialkyl cyclic α-amino acids (1-aminocycloalkane-1-carboxylic acids, Acxc) in position 2, 3, 4, or 2 and 3 in deltorphin C, and both peptides yielded peptides with decreased Kiδ, such that the latter peptide was essentially inactive.
Design and synthesis of 1-aminocycloalkane-1-carboxylic acid-substituted deltorphin analogues: unique delta and mu opioid activity in modified peptides.
The data confirmed that delta selectivity occurs in the absence of D-chirality at position 2, (i) the aromaticity of Phe3 is replaceable by an achiral residue with a hydrophobic ring-saturated side chain, and (ii) the acquisition of dual high-affinity analogues occurs through the elimination of the anionic function at position 4 and replacement by an amino acid with a Hydrophobic side chain.
Conformational studies of chemotactic HCO-Met-Leu-Phe-OMe analogues
- G. Vertuani, M. Boggian, A. Breveglieri, G. Cavicchioni, S. Spisani, A. Scatturin
- Chemistry, BiologyAmino Acids
- 11 June 1995
The results obtained comparing biological and conformational data evidence the critical presence of the NH group at position 2, a rather flexible backbone, and the chemical structure of the central residue which can affect the stability of a possible active conformer.
Biological Properties of the fMLP Analog Containing an Iodomethylated Methionine Residue
- S. Spisani, A. Breveglieri, E. Reali, A. Scatturin, G. Vertuani, G. Cavicchioni
- Biology, ChemistryProtein & Peptide Letters
- 1 December 1995
The formylpeptide HCO-Met-Leu-Phe-OMe methylsulphonium iodide (fMLP-OMe•MSl) was synthesized in order to clarify the role of the charge on Met sulphur atom in biological activities of human…
Synthesis and biological activity of a conformationally constrained chemotactic gamma-lactam formyl tetrapeptide.
The tetrapeptide evidences chemotactic activity as well as superoxide anion production and lysozyme release, although with lower efficacy when compared with the parent tripeptide.