Inhibitor of inflammation, peptide fragment (65–76) of monocyte chemotactic protein-1 (MCP-1), inhibits binding of MCP-1 to heparin

Autor: Maria Sidorova, T. L. Bushueva, Petr I. Nikitin, Tatiana I. Arefieva, A. A. Az’muko, Zh. D. Bespalova, T. L. Krasnikova, S. G. Gorshkov, N. Yu. Ruleva, T. I. Ksenevich
Rok vydání: 2011
Předmět:
Zdroj: Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 5:29-36
ISSN: 1990-7494
1990-7478
DOI: 10.1134/s1990747811010089
Popis: Monocyte chemotactic protein-1 (MCP-1, CCL2) is one of the most important chemokines involved in inflammation. MCP-1 stimulates migration of monocytes and certain lymphocyte populations to the affected area, in particular to the sites of atherosclerotic plaque formation. Development of drugs inhibiting MCP-1 is now a topical task. We earlier designed and synthesized a dodecapeptide from C-terminal domain of MCP-1 (65–76, peptide X) that possessed an anti-inflammatory activity. The mechanism of action of chemokines (in particular, of MCP-1) in vivo is based on activation of CCR2 receptor on target cells and binding to glycosaminoglycans (GAGs) on the cell surface of and extracellular matrix. Peptide X did not affect the MCP-1-CCR2 interaction. Thus, we hypothesized that peptide X could impair MCP-1 binding to GAGs. Here we studied the effect of peptide X on the MCP-1 binding to heparin using the label-free biosensing device Picoscope®, enzyme-linked immunoassay (ELISA), and the intrinsic fluorescence method. According to the data obtained, peptide X interfered with the MCP-1-heparin binding, which may be due to the competition of peptide X with MCP-1 for heparin binding sites. Probably, this effect determines the anti-inflammatory activity of peptide X in vivo.
Databáze: OpenAIRE
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