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Peptide mimics of monocyte chemoattractant protein-1 (MCP-1) with an antagonistic activity.
- Source :
-
Journal of biochemistry [J Biochem] 2001 Apr; Vol. 129 (4), pp. 577-83. - Publication Year :
- 2001
-
Abstract
- In this study, we attempted to analyze the peptide motifs recognized by 24822.111 and F9, monoclonal antibodies (mAbs) that inhibit the chemotactic activity of monocyte chemoattractant protein-1 (MCP-1), a member of the CC subfamily of chemokines. We isolated phage clones from a phage display library and identified six peptide motifs. One of these clones, C27, was strongly and specifically recognized by 24822.111 mAb, while another, G25, was similarly recognized by F9 mAb. Both the C27 motif and the G25 motif contain two cysteines in their sequences and have little homology to the primary amino acid sequence of MCP-1. These clones, however, bound to THP-1 cells, and the binding was competitively inhibited by MCP-1. The clones strongly inhibited the MCP-1-induced chemotaxis of human monocytes. The synthetic and intramolecularly disulfide-linked peptides of C27 and G25 (sC27 and sG25) also inhibited the chemotaxis induced by MCP-1, while their derivatives with serine in place of cysteine did not, suggesting the importance of the loop structure for the inhibition. These results suggest that sC27 and sG25 may mimic the MCP-1-binding domain to the MCP-1 receptor.
- Subjects :
- Amino Acid Sequence
Antibodies, Monoclonal immunology
Bacteriophages genetics
Bacteriophages metabolism
Binding Sites
Blotting, Western
Cell Line
Chemokine CCL2 immunology
Chemokine CCL2 pharmacology
Chemotaxis drug effects
Drug Design
Epitopes chemistry
Epitopes immunology
Flow Cytometry
Humans
Peptide Library
Peptides immunology
Peptides metabolism
Protein Binding
Protein Structure, Tertiary
Receptors, CCR2
Receptors, Chemokine metabolism
Chemokine CCL2 antagonists & inhibitors
Chemokine CCL2 chemistry
Molecular Mimicry
Peptides chemistry
Peptides pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-924X
- Volume :
- 129
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 11275557
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a002893