Nuclear magnetic resonance studies of the interaction of FN-C/H II, a pentadecapeptide from fibronectin, with heparin
- Univ. of California, Riverside, CA (United States)
Arrest of circulating tumor cells by adhesion to components of the extracellular matrix (ECM) is a critical step in metastasis. Tumor cell adhesion involves the binding of cell surface receptors, including heparan sulfate proteoglycan (HSPG) receptors, to fibronectin and other proteins of the ECM. Interruption of tumor cell adhesion has therapeutic potential in metastasis prevention. The peptide FN-C/H II, a pentadecapeptide (KNNQKSEPLIGRKKT) from module III{sub 14} of fibronectin binds to the heparan sulfate part of HSPG on the surface of highly metastatic mouse melanoma cells, and inhibits experimental metastasis of the melanoma cells, presumably by inhibition of their arrest by competitive binding to cell surface receptor sites. In this poster, results of one and two dimensional NMR studies to characterize FN-C/H II and related peptides and their binding by heparin will be reported. Structural information obtained from NOESY spectra for FN-C/H II indicates that the peptide free in solution has little structure, but that the heparin-complexed peptide is highly structured. NOESY data for the bound peptide are consistent with a helical structure. In the helical structure, 3 of the 5 arginine and lysine residues are located together on one side, thus presenting a region of high positive charge density for binding to the highly negatively charged heparin.
- OSTI ID:
- 126081
- Report Number(s):
- CONF-950402--
- Country of Publication:
- United States
- Language:
- English
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