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Colloidal ß-Tricalcium Phosphate Prepared by Discharge in a Modified Body Fluid Facilitates Synthesis of Collagen Composites

Y. Shibata*, H. Yamamoto, and Takashi Miyazaki

Department of Oral Biomaterials and Technology, Showa University School of Dentistry, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan;



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Figure 1. Chemical structure of colloidal calcium phosphates. Pure ß-TCP (1) and hydroxyapatite (2) powder were used as standard reference materials. FTIR analysis demonstrated PO43– adsorption peaks around 1000, 600, and 580 cm–1 attributable to ß-TCP on the precipitate synthesized in m•SBF (3). Peaks around 1000, 600, and 3570 cm–1, attributed to OH groups, were observed with precipitation of HBSS (4); thus, the precipitate of HBSS was determined as hydroxyapatite. All data were confirmed with 6 different samples, respectively, for each colloidal calcium phosphate.

 


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Figure 2. Conformational changes in ß-TCP/collagen (A) and hydroxyapatite/collagen (B) composites 30 sec, and 10, 20, and 30 min after being mixed. N-H stretching at 3310 cm–1 for amide A, C-H stretching at 3063 cm–1 for amide B, C=O stretching at 1600–1700 cm–1 for the amide I, N-H deformation at 1500–1550 cm–1 for the amide II, and N-H deformation at 1200–1300 cm–1 for the amide III band were detected in the ß-TCP/collagen composite. An isolated OH group around 3600 cm–1was detected only in the ß-TCP/collagen, while amides A and I increased at the beginning of analysis. All data were confirmed with 6 different samples, respectively, for each composite.

 


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Figure 3. Narrow-scan FTIR spectra. (A) Narrow-scan FTIR for amide A: The amide A peak of ß-TCP/collagen (1) was clearly detected compared with that of hydroxyapatite/collagen (2). (B) Narrow-scan FTIR for amide I: The amide I peak of ß-TCP/collagen (1) was much higher than that of hydroxyapatite/collagen (2). (C) Phosphate vibration mode of colloidal ß-TCP (1). The phosphate vibration mode of ß-TCP shifted to 1025 cm–1 (2), clearly indicating that a -P-O-P- polymerization chain was produced in the ß-TCP/collagen composite after being mixed. All data were confirmed with 6 different samples, respectively, for each composite.

 


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Figure 4. XPS high-resolution spectra of each composite. (A) High-resolution spectra of P2p in the ß-TCP/collagen composite; the secondary peak indicates NH+-phosphate binding. High-resolution spectra of Ca2p (B) and N1s (C) in both composites. The energy positions of N1s and Ca2p in the ß-TCP/collagen composite (1) were significantly higher (p < 0.01) than those in the hydroxyapatite/collagen composite (2). Average binding energies are expressed as the mean ± standard deviation (SD) of 6 specimens (n = 6), and significant differences in each spectrum between composites were analyzed statistically by Student’s t test (p < 0.01).

 





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