作者: K.J. Cross , N.L. Huq , D.P. Stanton , M. Sum , E.C. Reynolds
DOI: 10.1016/J.BIOMATERIALS.2004.01.045
关键词:
摘要: The repair of early tooth enamel lesions has been recently demonstrated by tryptic phosphopeptides derived from milk caseins that associate with amorphous calcium phosphate (ACP) forming stable complexes. These casein (CPP), containing the cluster sequence-Ser(P)-Ser(P)-Ser(P)-Glu-Glu-, form delivery vehicles retard demineralization and promote remineralization. Recently, we have shown these peptides also stabilize fluoride as soluble complexes designated CPP-ACFP, potential to provide superior clinical efficacy in preventing dental caries treating repairing stages disease. In an approach determine ultrastructure phosphopeptide-amorphous complexes, studied structure predominant peptide alpha(S1)-CN(59-79) bound ACFP using nuclear magnetic resonance (NMR) spectroscopy X-ray diffraction. stabilized nanocomplexes a hydrodynamic radius 2.12+/-0.26 nm. exhibited stoichiometry one 15 calcium, nine three ions. Sequence-specific assignments were determined for complexed ACFP. secondary was characterized sequential (i, i+1), medium-range i+2) nOes H alpha chemical shifts. spectral data compared ions, revealing structurally significant NH alpha-chemical shifts similar.