Recombinant hBMP4 incorporated with non-canonical amino acid for binding to hydroxyapatite
作者： Makoto Sakuragi , Takashi Kitajima , Teruyuki Nagamune , Yoshihiro Ito , None
DOI: 10.1007/S10529-011-0637-1
关键词:
摘要: A novel growth factor containing non-canonical amino acids was designed and synthesized to enhance the binding hydroxyapatite (HA). The protein human bone morphogenetic 4 (hBMP4) incorporating diphosporylated serines (pSpS) that found in salivary statherin reported be responsible for HA. Recombinant hBMP4 a short peptide sequences pSpS were ligated by enzymatice reaction of sortase A, which exchanges terminal two polypeptides. Resulting (hBMP4-pSpS) bound HA more efficiently than hBMP-4 tagged with canonical (hBMP4-SS). HA-bound hBMP-4-pSpS exhibited osteogenesis inducing activity multipotential mesenchyme cells (C3H10T1/2) as evidenced increased expression osteogenic markers, not seen hBMP4-SS. This will applicable regeneration materials combination
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