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Surface modification of titanium mat...
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Avaltroni, Michael Joseph.
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Surface modification of titanium materials to facilitate cell attachment, biomineralization, and interfacial adhesion.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Surface modification of titanium materials to facilitate cell attachment, biomineralization, and interfacial adhesion./
作者:
Avaltroni, Michael Joseph.
面頁冊數:
134 p.
附註:
Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3816.
Contained By:
Dissertation Abstracts International64-08B.
標題:
Chemistry, Inorganic. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3101031
ISBN:
0496486195
Surface modification of titanium materials to facilitate cell attachment, biomineralization, and interfacial adhesion.
Avaltroni, Michael Joseph.
Surface modification of titanium materials to facilitate cell attachment, biomineralization, and interfacial adhesion.
- 134 p.
Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3816.
Thesis (Ph.D.)--Princeton University, 2003.
Titanium and its alloys, most notably Ti-6Al-4V, are widely used as surgical implants which are in contact with bone. Bonding the fibronectin cell attachment peptide, arginine-glycine-aspartic acid (RGD) to the native oxide surface of titanium might enhance its osteoconductivity by providing sites for the promotion of cell adhesion and spreading. Two surface modification procedures are described herein to immobilize RGD onto Ti-6Al-4V. The first method uses an ca-terminated self-assembled monolayer (SAM) and an organic tether to provide a site for peptide attachment. The second method uses an organometallic, ( tert-butoxy) zirconium surface complex for direct immobilization of the peptide via ligand metathesis with the tert-butoxy groups. Both methods are shown to produce a surface that is cell attractive; mouse fibroblast and human osteoblast cell culture studies indicate a significant increase over controls in the adhesion and spreading of cells, and in the laying down of focal points of adhesion by cells. The SAM based system is stable to hydrolysis, but the zirconium complex is cleaved from the surface over several days. Long-term studies show that cells begin the process of mineralization on the metal surface, which is necessary for the process of bone growth. In addition to its biocompatibility, this surface film also shows a high degree of interfacial strength against both shear and tensile stress.
ISBN: 0496486195Subjects--Topical Terms:
517253
Chemistry, Inorganic.
Surface modification of titanium materials to facilitate cell attachment, biomineralization, and interfacial adhesion.
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Titanium and its alloys, most notably Ti-6Al-4V, are widely used as surgical implants which are in contact with bone. Bonding the fibronectin cell attachment peptide, arginine-glycine-aspartic acid (RGD) to the native oxide surface of titanium might enhance its osteoconductivity by providing sites for the promotion of cell adhesion and spreading. Two surface modification procedures are described herein to immobilize RGD onto Ti-6Al-4V. The first method uses an ca-terminated self-assembled monolayer (SAM) and an organic tether to provide a site for peptide attachment. The second method uses an organometallic, ( tert-butoxy) zirconium surface complex for direct immobilization of the peptide via ligand metathesis with the tert-butoxy groups. Both methods are shown to produce a surface that is cell attractive; mouse fibroblast and human osteoblast cell culture studies indicate a significant increase over controls in the adhesion and spreading of cells, and in the laying down of focal points of adhesion by cells. The SAM based system is stable to hydrolysis, but the zirconium complex is cleaved from the surface over several days. Long-term studies show that cells begin the process of mineralization on the metal surface, which is necessary for the process of bone growth. In addition to its biocompatibility, this surface film also shows a high degree of interfacial strength against both shear and tensile stress.
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