Matrices of acidic β-sheet peptides as templates for calcium phosphate mineralization

Shlomit Segman-Magidovich; Haviv Grisaru; Tamar Gitli; Yael Levi-Kalisman; Hanna Rapaport

doi:10.1002/adma.200702125

Matrices of acidic β-sheet peptides as templates for calcium phosphate mineralization

Shlomit Segman-Magidovich^*, Haviv Grisaru, Tamar Gitli, Yael Levi-Kalisman, Hanna Rapaport

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

Early stage of calcium phosphate mineralization on designed β-sheet peptides was monitored that may serve as nucleating templates for hydroxyapatite. A solution composed of the various ions present in the blood serum, in 1.5× their physiological concentration, was selected to monitor the mineralization under conditions that may be of biological relevancy. A film of the peptide that is spread on SBF_1.5 and held 18 hrs in the expanded state prior to compression, becomes less compressible. The TEM images showed structural features that are nanomeric in scale, and found that the flat calcium phosphate sheets could be a form of unchanged amorphous calcium phosphate aggregates. The 20 days mineralized peptide film shows the most prominent differences between the 20 days and 10 days spectra with an enhanced absorption at 1037 cm^-1.

Original language	American English
Pages (from-to)	2156-2161
Number of pages	6
Journal	Advanced Materials
Volume	20
Issue number	11
DOIs	https://doi.org/10.1002/adma.200702125
State	Published - 4 Jun 2008
Externally published	Yes

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abstract = "Early stage of calcium phosphate mineralization on designed β-sheet peptides was monitored that may serve as nucleating templates for hydroxyapatite. A solution composed of the various ions present in the blood serum, in 1.5× their physiological concentration, was selected to monitor the mineralization under conditions that may be of biological relevancy. A film of the peptide that is spread on SBF1.5 and held 18 hrs in the expanded state prior to compression, becomes less compressible. The TEM images showed structural features that are nanomeric in scale, and found that the flat calcium phosphate sheets could be a form of unchanged amorphous calcium phosphate aggregates. The 20 days mineralized peptide film shows the most prominent differences between the 20 days and 10 days spectra with an enhanced absorption at 1037 cm-1.",

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AU - Rapaport, Hanna

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N2 - Early stage of calcium phosphate mineralization on designed β-sheet peptides was monitored that may serve as nucleating templates for hydroxyapatite. A solution composed of the various ions present in the blood serum, in 1.5× their physiological concentration, was selected to monitor the mineralization under conditions that may be of biological relevancy. A film of the peptide that is spread on SBF1.5 and held 18 hrs in the expanded state prior to compression, becomes less compressible. The TEM images showed structural features that are nanomeric in scale, and found that the flat calcium phosphate sheets could be a form of unchanged amorphous calcium phosphate aggregates. The 20 days mineralized peptide film shows the most prominent differences between the 20 days and 10 days spectra with an enhanced absorption at 1037 cm-1.

AB - Early stage of calcium phosphate mineralization on designed β-sheet peptides was monitored that may serve as nucleating templates for hydroxyapatite. A solution composed of the various ions present in the blood serum, in 1.5× their physiological concentration, was selected to monitor the mineralization under conditions that may be of biological relevancy. A film of the peptide that is spread on SBF1.5 and held 18 hrs in the expanded state prior to compression, becomes less compressible. The TEM images showed structural features that are nanomeric in scale, and found that the flat calcium phosphate sheets could be a form of unchanged amorphous calcium phosphate aggregates. The 20 days mineralized peptide film shows the most prominent differences between the 20 days and 10 days spectra with an enhanced absorption at 1037 cm-1.

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Matrices of acidic β-sheet peptides as templates for calcium phosphate mineralization

Abstract

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