Molecular properties of poly(RGD) and its binding capacities to metastatic melanoma cells
| Autor: | Seiichi Tokura, Norio Nishi, Ikuo Saiki, Jun Murata, Ryu Ogawa, Ichiro Azuma |
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| Rok vydání: | 2009 |
| Předmět: |
Protein Conformation
Cell Antineoplastic Agents Peptide Tripeptide Biochemistry Mice medicine Animals Neoplasm Metastasis Receptor Cell adhesion Melanoma Peptide sequence Cell Line Transformed chemistry.chemical_classification biology Cell Membrane Adhesion Molecular biology Fibronectins Fibronectin medicine.anatomical_structure chemistry biology.protein Peptides Oligopeptides |
| Zdroj: | International Journal of Peptide and Protein Research. 38:212-217 |
| ISSN: | 0367-8377 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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