Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization.

@article{Gu2011ImmobilizationOA,
  title={Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization.},
  author={Li-sha Gu and Young Kyung Kim and Yan Liu and Kei Takahashi and S. N. Arun and Courtney E Wimmer and Raquel Osorio and Jun-qi Ling and Stephen W. Looney and David Henry Pashley and Franklin R Tay},
  journal={Acta biomaterialia},
  year={2011},
  volume={7 1},
  pages={268-77}
}
Immobilization of phosphoproteins on a collagen matrix is important for the induction of intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no reactive sites for covalent binding to collagen amine groups. Binding of poly(vinyl phosphonic acid) (PVPA), a biomimetic templating analog of matrix phosphoproteins, to collagen was found to be electrostatic in nature. Thus, an alternative retention mechanism was designed for immobilization of PVPA on collagen by… CONTINUE READING

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