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

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 inve...

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Bibliographic Details
Published in:European Journal of Organic Chemistry 2005-04, Vol.2005 (8), p.1644-1651
Main Authors: Spezzacatena, Caterina, Pepe, Antonietta, Green, Lora M., Sandberg, Lawrence B., Bochicchio, Brigida, Tamburro, Antonio M.
Format: Article
Language:English
Subjects:
Biological activity
Elastin
Peptides
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Summary: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)
ISSN:1434-193X
1099-0690
DOI:10.1002/ejoc.200400510