Acidic amino acid-rich sequences as binding sites of osteonectin to hydroxyapatite crystals

Fujisawa, Ryuichi; Wada, Yasuhiko; Nodasaka, Yoshinobu; Kuboki, Yoshinori

doi:10.1016/0167-4838(95)00190-5

Cited by 163 publications

(132 citation statements)

References 33 publications

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“…HAP-binding proteins have definitive HAP-binding sites based on acid side chains on amino acids. Proteins containing aspartic acid-rich sequences interact with crystals of calcium salt in a specific manner [50,51], and poly-glutamic acid sequences or poly-aspartic acid sequences are present in HAP-binding proteins [49]. From a comparison of Fig.…”

Section: Discussionmentioning

confidence: 99%

Bone tissue engineering with premineralized silk scaffolds

Kim

et al. 2008

Bone

269

244

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Silks fibroin biomaterials are being explored as novel protein-based systems for cell and tissue culture. In the present study, biomimetic growth of calcium phosphate on porous silk fibroin polymeric scaffolds was explored to generate organic/inorganic composites as scaffolds for bone tissue engineering. Aqueous-derived silk fibroin scaffolds were prepared with the addition of polyaspartic acid during processing, followed by the controlled deposition of calcium phosphate by exposure to CaCl 2 and Na 2 HPO 4 . These mineralized protein-composite scaffolds were subsequently seeded with human bone marrow stem cells (hMSC) and cultured in vitro for 6 weeks under osteogenic conditions with or without BMP-2. The extent of osteoconductivity was assessed by cell numbers, alkaline phosphatase and calcium deposition, along with immunohistochemistry for bone related outcomes. The results suggest increased osteoconductive outcomes with an increase in initial content of apatite and BMP-2 in the silk fibroin porous scaffolds. The premineralization of these highly porous silk fibroin protein scaffolds provided enhanced outcomes for the bone tissue engineering.

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Section: Discussionmentioning

confidence: 99%

Bone tissue engineering with premineralized silk scaffolds

Kim

et al. 2008

Bone

269

244

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“…Among them, hydroxyapatite (HAP, Ca 10 (PO 4 ) 6 (OH) 2 ) is the most thermodynamically stable [15,16]. Unlike other inorganic compounds, HAP is also an important biomineral with specific affinity for amino acids, peptides and proteins [17][18][19][20][21][22]. Therefore, it is reasonable to suggest that HAP may accumulate biomolecules to promote their chemical evolution.…”

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confidence: 99%

Mechanism of promoted dipeptide formation on hydroxyapatite crystal surfaces

Zhang

et al. 2011

Chin. Sci. Bull.

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The formation of dipeptides from amino acids can be driven by hydroxyapatite at a relatively low temperature in air. For example, the formation of (Ala) 2 from Ala is induced on hydroxyapatite at 110C with considerable yield. Typically, condensing agents, high temperatures (>250C) or high pressures (>25 MPa) are required to drive the condensation of amino acids. Similar effects are observed in the condensation of Gly, Glu and Asp. Experiments demonstrate that hydroxyapatite is an effective inorganic catalytic agent, reducing the activation barrier for the formation of dipeptides by more than 50%. HAP promotes condensation by adsorbing amino acid monomers in an organized manner, which decreases the distance between amino and carboxyl groups on neighboring molecules and extends the contact time of the reaction groups. This work provides a chemical understanding of the primitive condensation of amino acids and reveals a mechanism for enhancement of mineral catalysts. It is important that the conditions used for hydroxyapatite-assisted dipeptide formation are not harsh and can be readily achieved, revealing a possible mechanism for the chemical evolution of biomolecules over geologic ages.

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“…This result suggested that the porous chitosan/nHAC scaffold may be a promising carrier for BMP-7 mimetic peptide. Although the exact mechanism is not completely clear, the HA has high affinity to drugs and proteins 27) . The chitosan/nHAC scaffold contains a great quantity of HA.…”

Section: Discussionmentioning

confidence: 99%

Accelerated Bone Regeneration by Chitosan/Nanometer Hydroxyapatite/Collagen Composite Incorporating BMP-7 Mimetic Peptide

Feng

Hu²,

Yang-de³

2012

J. Hard Tissue Biology.

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The purpose of the present study was to examine whether the chitosan/ nanometer hydroxyapatite / collagen composite (chitosan/nHAC) incorporating BMP-7 mimetic peptide could accelerate bone regeneration. The chitosan/nHAC composite was prepared and the BMP-7 mimetic peptide introduced into the composite by vacuum adsorption. The released peptide content from the composite was detected using high performance liquid chromatography at different set times. 5 mm diameter cranial bone defects were created on both sides of the parietal bone in 24 adult Sprague-Dawley rats, which were randomized into two treatment groups; one receiving the chitosan/nHAC composite loaded with 1 mg BMP-7 mimetic peptide and the other one receiving the unload composite. Bone healing was evaluated with radiographic and histological analysis. The results showed that significantly improved and effective bone regeneration was achieved with the composite loaded with 1 mg BMP-7 mimetic peptide compared to the unloaded composite. In conclusion, the BMP-7 mimetic peptide in combination with the chitosan/nHAC composite could successfully accelerate the healing of rat's cranial bone defects. The chitosan/nHAC/BMP-7 mimetic peptide composite is an ideal bone substitute material.

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Acidic amino acid-rich sequences as binding sites of osteonectin to hydroxyapatite crystals

Cited by 163 publications

References 33 publications

Bone tissue engineering with premineralized silk scaffolds

Bone tissue engineering with premineralized silk scaffolds

Mechanism of promoted dipeptide formation on hydroxyapatite crystal surfaces

Accelerated Bone Regeneration by Chitosan/Nanometer Hydroxyapatite/Collagen Composite Incorporating BMP-7 Mimetic Peptide

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