Synthesis, NMR and function of an O-phosphorylated peptide, comprising the RGD-adhesion sequence of osteopontin.

@article{Pettersson1991SynthesisNA,
  title={Synthesis, NMR and function of an O-phosphorylated peptide, comprising the RGD-adhesion sequence of osteopontin.},
  author={Ethel Pettersson and Bjoern Luening and Henrik Mickos and Dick Heineg{\aa}rd},
  journal={Acta chemica Scandinavica},
  year={1991},
  volume={45 6},
  pages={
          604-8
        }
}
The bone phosphoprotein osteopontin owes its cell adhesion property to the RGD-sequence. In order to determine whether a phosphate substituent on the serine following the RGD-sequence interferes with cell binding, we have synthesized GRGDSL along with the corresponding peptide phosphorylated on serine. The latter peptide showed significantly lower cell binding as measured by inhibition of adhesion of R1 cells to surfaces coated with BSP. GRGDSL and phosphorylated GRGDSL show NMR spectra which… CONTINUE READING
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