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1. Synthesis and biological evaluation of a novel pyroglutamyl-modified TRH analogue

Author

Grazia Luisi, A. Giorgi, Luigi Brunetti, Francesco Pinnen, Alessandra Spirito, Lucia Recinella, Silvestro Duprè, Ivana Cacciatore, P. Sozio, A. Di Stefano, Giustino Orlando, and Barbara Michelotto

Subjects
Male, Stereochemistry, Dopamine, Pyroglutamyl-Peptidase I, Pharmaceutical Science, Peptide, Residue (chemistry), chemistry.chemical_compound, Pituitary Gland, Anterior, Drug Discovery, Peptide synthesis, Animals, Moiety, Pyroglutamyl-peptidase I, Rats, Wistar, Nuclear Magnetic Resonance, Biomolecular, Thyrotropin-Releasing Hormone, Cells, Cultured, chemistry.chemical_classification, Dipeptide, Dose-Response Relationship, Drug, Biological activity, Prolactin, Pyrrolidonecarboxylic Acid, Rats, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Cattle, Pyroglutamic acid
Abstract

The TRH analogue 3, incorporating the (S)-isothiazolidine-1,1-dioxide-3-carboxylic acid (1) moiety in place of the native L-pyroglutamic acid (pGlu) residue, has been synthesized and fully characterized by 1H and 13C NMR. The effects of replacing pGlu with its sulphonamido counterpart on biological activity have been investigated. This peptide, which is significantly stabilized towards hydrolysis by pyroglutamyl peptidase type I (PP I, EC 3.4.19.3), has shown to maintain in vitro prolactin-releasing activity.

Published
2002
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2. Ψ(SO2NH) transition state isosteres of peptides. Synthesis and bioactivity of sulfonamido pseudopeptides related to carnosine

Author

Grazia Luisi, Silvestro Duprè, A. Calcagni, Antonio Di Stefano, D. Rossi, Alessandra Spirito, Francesco Pinnen, and Pier Giuseppe Ciattini

Subjects
chemistry.chemical_classification, Dipeptidase, Dipeptidases, Dipeptide, biology, Stereochemistry, Carnosine, Pharmaceutical Science, Biological activity, Dipeptides, Chemical synthesis, Combinatorial chemistry, In vitro, chemistry.chemical_compound, Enzyme, chemistry, Enzyme inhibitor, Drug Discovery, biology.protein, Enzyme Inhibitors
Abstract

This paper reports the synthesis of tauryl dipeptides related to carnosine. In particular H-Tau-His-OH (5), H-Tau-His(π-Me)-OH (6) and H-Tau-His(τ-Me)-OH (9) are described. The enzyme carnosinase has been isolated from pig kidney and after purification has been used to test the stability and the inhibitory activity of the three new analogues. H-Tau-His-OH (5) and H-Tau-His(τ-Me)-OH (9) were found to possess weak inhibitory properties towards carnosinase, while H-Tau-His(π-Me)-OH (6) proved to be devoid of any significant activity. All the three sulfonamido pseudopeptides 5, 6 and 9 show stability to carnosinase activity.

Published
1999
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