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Synthesis and biological characterization of human monocyte chemoattractant protein 1 (MCP‐1) and its analogs
Author(s) -
Kruszynski Marian,
Stowell Nicole,
Das Anuk,
Seideman Jonathan,
Tsui Ping,
BrighamBurke Michael,
Nemeth Jennifer F.,
Sweet Raymond,
Heavner George A.
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.680
Subject(s) - monoclonal antibody , chemistry , chemotaxis , recombinant dna , monocyte , ccr2 , surface plasmon resonance , peptide , receptor , ligand (biochemistry) , biological activity , affinity chromatography , biochemistry , antibody , microbiology and biotechnology , in vitro , chemokine , chemokine receptor , biology , enzyme , nanoparticle , immunology , materials science , gene , nanotechnology
Abstract Novel analogs of human monocyte chemoattractant protein 1 (MCP‐1) were designed, synthesized and characterized to be used as tools to generate monoclonal antibodies as potential human therapeutics. MCP‐1 and three analogs were synthesized by step‐wise Fmoc solid phase synthesis. After oxidation to form the two‐disulfide bonds, affinity chromatography using an immobilized mouse anti‐human MCP‐1 monoclonal antibody (mAb) was utilized for a simple and highly effective purification procedure for the proteins. The final products were extensively characterized and compared with recombinant human MCP‐1 (rhMCP‐1). All proteins showed identical binding with mouse anti‐human MCP‐1 mAbs as measured by surface plasmon resonance. Synthetic MCP‐1 and the analogs were comparable to recombinant MCP‐1 in competition radio‐ligand binding to CCR2 receptors on THP‐1 cells, and MCP‐1‐induced, calcium mobilization and chemotaxis assays. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.