Cell attachment peptide of C-reactive protein: critical amino acids and minimum length

✍ Scribed by Michael C. Mullenix; Pravin T. P. Kaumaya; Richard F. Mortensen

• Book ID: 102876583
• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 913 KB
• Volume: 54
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240540310

✦ Synopsis

Human C-reactive protein (CRP) is an acute phase blood component that accumulates at sites of tissue damage and necrosis and is degraded by neutrophils to biologically active peptides. A dodecapeptide composed of amino acids 27-38 of CRP mediates cell attachment in vitro. This peptide was designated the cell-binding peptide (CB-Pep) of CRP. Characterization of the interaction between fibroblasts and modified synthetic peptides with sequential deletions from either the N-terminus or C-terminus revealed that the minimal sequence for cell attachment or inhibition of cell attachment to the CB-Pep was Phe-Thr-Val-Cys-Leu, which corresponds to residues 33-37 within each of the five 206 amino acid subunits of CRP. The pentapeptide by itself mediated cell attachment. Substitutions for each residue within the CB-Pep indicated that the critical residues for activity were Phe-33 and Thr-34. This cell-binding pentapeptide represents a recognition motif for cell adhesion not found in other proteins.