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Synthesis and biological characterization of human monocyte chemoattractant protein 1 (MCP-1) and its analogs

✍ Scribed by Marian Kruszynski; Nicole Stowell; Anuk Das; Jonathan Seideman; Ping Tsui; Michael Brigham-Burke; Jennifer F. Nemeth; Raymond Sweet; George A. Heavner

Publisher
John Wiley and Sons
Year
2005
Tongue
English
Weight
147 KB
Volume
12
Category
Article
ISSN
1075-2617

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✦ Synopsis

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.

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