American Chemical Society
Browse
jm5b00841_si_001.pdf (1.52 MB)

Synthesis and Characterization in Vitro and in Vivo of (l)‑(Trimethylsilyl)alanine Containing Neurotensin Analogues

Download (1.52 MB)
journal contribution
posted on 2015-10-08, 00:00 authored by Roberto Fanelli, Élie Besserer-Offroy, Adeline René, Jérôme Côté, Pascal Tétreault, Jasmin Collerette-Tremblay, Jean-Michel Longpré, Richard Leduc, Jean Martinez, Philippe Sarret, Florine Cavelier
The silylated amino acid (l)-(trimethylsilyl)­alanine (TMSAla) was incorporated at the C-terminal end of the minimal biologically active neurotensin (NT) fragment, leading to the synthesis of new hexapeptide NT[8–13] analogues. Here, we assessed the ability of these new silylated NT compounds to bind to NTS1 and NTS2 receptors, promote regulation of multiple signaling pathways, induce inhibition of the ileal smooth muscle contractions, and affect distinct physiological variables, including blood pressure and pain sensation. Among the C-terminal modified analogues, compound 6 (JMV2007) carrying a TMSAla residue in position 13 exhibits a higher affinity toward NT receptors than the NT native peptide. We also found that compound 6 is effective in reversing carbachol-induced contraction in the isolated strip preparation assay and at inducing a drop in blood pressure. Finally, compound 6 produces potent analgesia in experimental models of acute and persistent pain.

History