Novel synthetic peptides from the C-terminal heparin binding domain of fibronectin with heparin binding activity.
To identify a minimal peptide ligand that participates in recognition of heparin, we synthesized peptides extending a 29-kDa fragment in the C-terminal heparin binding domain of fibronectin. We obtained evidence that two peptides (designated D5 and D1) exhibit inhibitory activity on binding of the 29-kDa fragment to heparin-Sepharose CL 6B. It dose inhibitory studies, peptide D5 showed the potent inhibitory activity with IC50 of 210 +/- 37 microM. A new heparin binding site in the C-terminal heparin binding domain of fibronectin is demonstrated and provides a rationale for understanding the mechanism of cell adhesion and spreading.
First Department of Internal Medicine, Yokohama City University School of Medicine, Japan.
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H
Mohri
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K
Katoh
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S
Motomura
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T
Okubo
D001665:Binding Sites; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
D005353:Fibronectins; D010446:Peptide Fragments; D006493:Heparin