Val-Val-Pro-Gln (valyl-valyl-prolyl-glutamine) is a small but highly conserved sequence present in all elastins. We describe its synthesis by mixed anhydride solution chemistry as an alternative to solid-phase peptide synthesis (SPPS). The molecular structure of the tetrapeptide in solution was investigated by classical spectroscopy, such as circular dichroism (CD), nuclear magnetic resonance (NMR) and Fourier Transform Infrared Spectroscopy (FTIR). The biological activity of Val-Val-Pro-Gln was evaluated by a bromodeoxyuridine (BrdU) incorporation assay with normal human dermal fibroblasts. This small peptide may play a critical role in control of matrix metabolism through its release from the elastin polypeptide chain during periods of tissue breakdown and remodelling.
Synthesis, Solution Structure and Biological Activity of Val-Val-Pro-Gln,a Bioactive Elastin Peptide
PEPE, Antonietta;BOCHICCHIO, Brigida;TAMBURRO, Antonio Mario
2005-01-01
Abstract
Val-Val-Pro-Gln (valyl-valyl-prolyl-glutamine) is a small but highly conserved sequence present in all elastins. We describe its synthesis by mixed anhydride solution chemistry as an alternative to solid-phase peptide synthesis (SPPS). The molecular structure of the tetrapeptide in solution was investigated by classical spectroscopy, such as circular dichroism (CD), nuclear magnetic resonance (NMR) and Fourier Transform Infrared Spectroscopy (FTIR). The biological activity of Val-Val-Pro-Gln was evaluated by a bromodeoxyuridine (BrdU) incorporation assay with normal human dermal fibroblasts. This small peptide may play a critical role in control of matrix metabolism through its release from the elastin polypeptide chain during periods of tissue breakdown and remodelling.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
