Molecular properties of poly(RGD) and its binding capacities to metastatic melanoma cells.

Abstract

We examined the binding capacity of anti-metastatic polypeptide containing repetitive Arg-Gly-Asp(RGD) sequence derived from cell binding site of fibronectin, poly(RGD), to the surface of tumor cells. Poly(RGD) competitively inhibited the binding of radiolabeled fibronectin to the cell surface more potently than oligo(RGD) or RGD tripeptide on a molar basis. Compared on a weight basis to oligo(RGD) or RGD peptide, poly(RGD) was more active than the oligo- and monomeric peptide at inhibiting tumor cell adhesion to immobilized fibronectin. The secondary structure of poly(RGD) was predicted to be a beta-turn from the data of CD spectra and its amino acid sequence. These findings suggest that poly(RGD)-mediated inhibition of cell adhesion is due to its potent binding capacity to fibronectin receptors on cell surface probably through its conformational properties.

• Authors: J Murata, I Saiki, R Ogawa, N Nishi, S Tokura, I Azuma
• Journal: International journal of peptide and protein research (Int J Pept Protein Res) Vol. 38 Issue 3 Pg. 212-7 (Sep 1991) ISSN: 0367-8377 [Print] Denmark
• PMID: 1761368 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antineoplastic Agents
• Fibronectins
• Oligopeptides
• Peptides
• poly (arginyl-glycyl-aspartic acid)
• arginyl-glycyl-aspartic acid

Topics

• Animals
• Antineoplastic Agents (pharmacology)
• Cell Line, Transformed (drug effects)
• Cell Membrane (metabolism)
• Fibronectins (metabolism)
• Melanoma (metabolism)
• Mice
• Neoplasm Metastasis
• Oligopeptides (metabolism, pharmacology)
• Peptides (metabolism, pharmacology)
• Protein Conformation