@misc{oai:repo.qst.go.jp:00069864,
 author = {Jin, Zhao-Hui and Furukawa, Takako and Waki, Atsuo and Akaji, Kenichi and Coll, Jean-Luc and Saga, Tsuneo and Fujibayashi, Yasuhisa and 金 朝暉 and 古川 高子 and 佐賀 恒夫},
 month = {Sep},
 note = {Multivalent interactions are frequently used to enhance ligand-receptor binding affinity. In this study a mono-, di- and trimeric AVTGRGDSY peptide derived from fibronectin were compared concerning the integrin receptor binding affinity and/or specificity. Methods: AVTGRGDSY monomer, dimer and trimer were synthesized, labeled with 125I or Cy5.5. Using human embryonic kidney cells HEK293 (naturally alphaV-positive and beta3-negative), HEK293(beta1) (beta1-transfected and alphaVbeta3-negative), HEK293(beta3)( beta3-transfected and strongly alphaVbeta3
-positive), and human glioblastoma cells U87MG (naturally alphaVbeta3-positive),
cell-binding assay, competitive inhibition assay, cell adhesion assay and confocal laser scanning microscopic study were performed to determine the bioactivities of these peptides. Results: The monomeric AVTGRGDSY showed specific binding to both HEK293(beta1) and HEK293(beta3) cells. Multimerization resulted in no change with HEK293 cells, diminished binding for HEK293(beta1) cells, but substantially enhanced binding for alphaVbeta3-positive HEK293(beta3) and U87MG cells in the presence of Mn2+. Moreover, the multimeric AVTGRGDSY peptides were found to be nearly comparable with th alphaVbeta3-specific cyclo(RGDfV) peptide in specificity and affinity for targeting alphaVbeta3 integrin. Conclusion: The multimeric AVTGRGDSY peptide might be an efficient alphaVbeta3-targeting molecule. The present study would be useful for better understanding of the molecular basis of the interaction between RGD ligands and integrin receptors., World Molecular Imaging Congress},
 title = {Comparison of in vitro characteristics of a monomeric, dimeric and trimeric fibronectin-derived linear},
 year = {2009}
}