Bone sialoprotein (BSP), an acidic non-collagenous protein, is proposed previously to modulate hydroxyapatite (HAP) nanocrystal growth.  Two highly conserved phosphorylated acidic amino-acid sequences are hypothesized as the functional motifs.  We choose one of them, (Sp)2E8 (Sp represents a phosphoserine), as a model to study interactions between BSP and HAP (001) face.  A bioinformatics method predicts the likely peptide conformations adsorbed on the HAP, which, subsequently, is subject to further examinations using molecular dynamics simulations with the explicit solvent model.  The bioinformatics method demonstrates a Sp residue binds strongly to the surface, and Glu residues show propensity to form a helical conformation.  Long-time molecular dynamic simulations observe some variations of the sidechain orientations with the backbone structure and the major binding features preserved.  No apparent geometrical templating between peptide residues and the studied HAP surface sites is noticed, implying adsorption and subsequent crystal growth modulation by BSP may be structurally non-specific.

Adsorption of bone sialoprotein on hydroxyapatite: A combination study with bioinformatics and molecular dynamics simulations

245th National Meeting (2013)

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