| Abstract | A new anti-inflammatory peptide X (Ingramon)--a fragment of C-terminal sequence (65-76) of MCP-1, was elaborated. In Boyden chamber assay, Ingramon inhibited migration of human monocytic cells THP-1 and peripheral blood monocytes. In vitro in blood plasma, Ingramon was stable for at least 24 hours. Ingramon was accumulated in sites of inflammation in rats, and impaired monocyte and granulocyte accumulation occurred in different models of inflammation in rodents and primates. Ingramon exerted no effect on the MCP-1-dependent externalisation of p2 integrins CD lib CD18 (Mac-1). We propose that Ingramon might interfere with MCP-1-heparin/heparan sulphate binding on cell surface. Ingramon reception by volunteers showed its safety. The clinical trials of Ingramon in patients with acute coronary syndromes and percutaneous coronary interventions, have been launched. |
