Hydroxyapatite mineralization and demineralization in the presence of synthetic phosphorylated pentapeptides

Wikiel, Kazimierz; Burke, Eileen M.; Perich, John W.; Reynolds, Eric C.; Nancollas, G.H.

doi:10.1016/0003-9969(94)90099-x

Cited by 33 publications

(43 citation statements)

References 30 publications

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“…Constantcomposition kinetic methods comparing the growth rate of the HAP seed crystals in the presence and absence of preadsorbed N6 indicated that the peptide inhibits crystallization Ͼ99% relative to the uncoated control. These results are consistent with those reported for N-terminal penta-and hexapeptides of statherin (25,26).…”

Section: Resultssupporting

confidence: 83%

“…The existence of secondary structure in other acidic proteins has also been predicted and hypothesized to play a role in crystal recognition through lattice-matching mechanisms (22)(23)(24). As initially demonstrated by Hay, Nancollas, and coworkers, peptides from this N terminus of statherin bind effectively to HAP seed crystals and inhibit their further growth in metastable supersaturated solutions (25,26).…”

mentioning

confidence: 93%

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A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface

Long

Dindot

Zebroski

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Proteins play an important role in the biological mechanisms controlling hard tissue development, but the details of molecular recognition at inorganic crystal interfaces remain poorly characterized. We have applied a recently developed homonuclear dipolar recoupling solidstate NMR technique, dipolar recoupling with a windowless sequence (DRAWS), to directly probe the conformation of an acidic peptide adsorbed to hydroxyapatite (HAP) crystals. The phosphorylated hexapeptide, DpSpSEEK (N6, where pS denotes phosphorylated serine), was derived from the N terminus of the salivary protein statherin. Constantcomposition kinetic characterization demonstrated that, like the native statherin, this peptide inhibits the growth of HAP seed crystals when preadsorbed to the crystal surface. The DRAWS technique was used to measure the internuclear distance between two 13 C labels at the carbonyl positions of the adjacent phosphoserine residues. Dipolar dephasing measured at short mixing times yielded a mean separation distance of 3.2 ؎ 0.1 Å. Data obtained by using longer mixing times suggest a broad distribution of conformations about this average distance. Using a more complex model with discrete ␣-helical and extended conformations did not yield a better fit to the data and was not consistent with chemical shift analysis. These results suggest that the peptide is predominantly in an extended conformation rather than an ␣-helical state on the HAP surface. Solid-state NMR approaches can thus be used to determine directly the conformation of biologically relevant peptides on HAP surfaces. A better understanding of peptide and protein conformation on biomineral surfaces may provide design principles useful for the modification of orthopedic and dental implants with coatings and biological growth factors that are designed to enhance biocompatibility with surrounding tissue.

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Section: Resultssupporting

confidence: 83%

mentioning

confidence: 93%

A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface

Long

Dindot

Zebroski

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…Poly-Glu and poly-Asp are among the strongest inhibitors of HA growth when dissolved in solution, but they can act as HA nucleators when adsorbed on a surface Phosphorylated residues are responsible for the inhibitory effect of statherin-like pentapeptides dissolved in solution [45]. This can explain the role of statherin as an inhibitory protein in the saliva [25].…”

Section: Poly Amino Acids and Peptidesmentioning

confidence: 99%

The role of amino acids in hydroxyapatite mineralization

Tavafoghi¹,

Cerruti²

2016

J. R. Soc. Interface.

209

147

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Polar and charged amino acids (AAs) are heavily expressed in noncollagenous proteins (NCPs), and are involved in hydroxyapatite (HA) mineralization in bone. Here, we review what is known on the effect of single AAs on HA precipitation. Negatively charged AAs, such as aspartic acid, glutamic acid (Glu) and phosphoserine are largely expressed in NCPs and play a critical role in controlling HA nucleation and growth. Positively charged ones such as arginine (Arg) or lysine (Lys) are heavily involved in HA nucleation within extracellular matrix proteins such as collagen. Glu, Arg and Lys intake can also increase bone mineral density by stimulating growth hormone production. In vitro studies suggest that the role of AAs in controlling HA precipitation is affected by their mobility. While dissolved AAs are able to inhibit HA precipitation and growth by chelating Ca 2þ and PO 4 32 ions or binding to nuclei of calcium phosphate and preventing their further growth, AAs bound to surfaces can promote HA precipitation by attracting Ca 2þ and PO 4 32 ions and increasing the local supersaturation. Overall, the effect of AAs on HA precipitation is worth being investigated more, especially under conditions closer to the physiological ones, where the presence of other factors such as collagen, mineralization inhibitors, and cells heavily influences HA precipitation. A deeper understanding of the role of AAs in HA mineralization will increase our fundamental knowledge related to bone formation, and could lead to new therapies to improve bone regeneration in damaged tissues or cure pathological diseases caused by excessive mineralization in tissues such as cartilage, blood vessels and cardiac valves.

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“…Nancollas has demonstrated that N-terminal peptides from statherin also display functional activities in controlling HAP growth [76,77]. Secondary structure predictions suggest that the N-terminus has a propensity for α-helix formation.…”

Section: Statherin: a Protein That Regulates Crystallization Of Hydromentioning

confidence: 99%

Solid state NMR studies of molecular recognition at protein–mineral interfaces

Goobes

Stayton

Drobny

2007

Progress in Nuclear Magnetic Resonance Spectroscopy

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Hydroxyapatite mineralization and demineralization in the presence of synthetic phosphorylated pentapeptides

Cited by 33 publications

References 30 publications

A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface

A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface

The role of amino acids in hydroxyapatite mineralization

Solid state NMR studies of molecular recognition at protein–mineral interfaces

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