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- W2548903987 abstract "Dentin phosphoprotein (DPP) is the most acidic protein in vertebrates and structurally is classified as an intrinsically disordered protein. Functionally, DPP is related to dentin and bone formation, however the specifics of such association remain unknown. Here, we used atomistic molecular dynamics simulations to screen selected binding domains of DPP onto hydroxyapatite (HA), which is one of its important interacting partners. From these results, we selected a functionally relevant peptide, Ace-SSDSSDSSDSSDSSD-NH2 (named P5) and its phosphorylated form (named P5P), for experimental characterization. SAXS experiments indicated that in solution P5 was disordered, possibly in an extended conformation while P5P displayed more compact globular conformations. Circular dichroism and FTIR confirmed that, either in the presence or absence of Ca2 +/HA, P5 adopts a random coil structure, whereas its phosphorylated counterpart, P5P, has a more compact arrangement associated with conformations that display β-sheet and α-helix motifs when bound to HA. In solution, P5 inhibited HA crystal growth, whereas at similar concentrations, P5P stimulated it. These findings suggest that phosphorylation controls the transient formation of secondary and tertiary structure of DPP peptides, and, most likely of DPP itself, which in turn controls HA growth in solution and possibly HA growth in mineralized tissues." @default.
- W2548903987 created "2016-11-11" @default.
- W2548903987 creator A5012845912 @default.
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- W2548903987 creator A5058486200 @default.
- W2548903987 creator A5074544353 @default.
- W2548903987 date "2017-02-01" @default.
- W2548903987 modified "2023-10-18" @default.
- W2548903987 title "Phosphorylation regulates the secondary structure and function of dentin phosphoprotein peptides" @default.
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- W2548903987 doi "https://doi.org/10.1016/j.bone.2016.10.028" @default.
- W2548903987 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5234040" @default.
- W2548903987 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27810285" @default.
- W2548903987 hasPublicationYear "2017" @default.
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