Synthesis, Solution Structure and Biological Activity of Val-Val-Pro-Gln,a Bioactive Elastin Peptide

• Published in: European Journal of Organic Chemistry Vol. 2005; no. 8; pp. 1644 - 1651
• Main Authors: Spezzacatena, Caterina, Pepe, Antonietta, Green, Lora M., Sandberg, Lawrence B., Bochicchio, Brigida, Tamburro, Antonio M.
• Format: Book Review Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01-04-2005; WILEY‐VCH Verlag
• Subjects: Biological activity; Elastin; Peptides
• ISSN: 1434-193X; 1099-0690
• DOI: 10.1002/ejoc.200400510

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. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)