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Collagens tissue engineering

Berglund JD, Nerem RM and Sambanis A. Incorporation of intact elastin scaffolds in tissue-engineered collagen-based vascular grafts. Tissue Eng. 10 1526-1535,2004. [Pg.803]

PLGA Bone tissue engineering Collagen mineralization process induced the formation of nanosize carbonated hydroxyapatite, while nanosize hydroxyapatite is formed during PLGA mineralization Liao et al. (2008)... [Pg.202]

Ito, H., Steplewski, A., Alabyeva, T., and Fertala, A., Testing the utility of rationally engineered recombinant collagen-hke proteins for appheations in tissue engineering, J. Biomed. Mater. Res. A., 76 (3), 551-560, 2006. [Pg.273]

The ability of these peptidomimetic collagen-structures to adopt triple helices portends the development of highly stable biocompatible materials with collagenlike properties. For instance, it has been found that surface-immobilized (Gly-Pro-Meu)io-Gly-Pro-NH2 in its triple-helix conformation stimulated attachment and growth of epithelial cells and fibroblasts in vitro [77]. As a result, one can easily foresee future implementations of biostable collagen mimics such as these, in tissue engineering and for the fabrication of biomedical devices. [Pg.24]

Abstract Synthetic polymers and biopolymers are extensively used within the field of tissue engineering. Some common examples of these materials include polylactic acid, polyglycolic acid, collagen, elastin, and various forms of polysaccharides. In terms of application, these materials are primarily used in the construction of scaffolds that aid in the local delivery of cells and growth factors, and in many cases fulfill a mechanical role in supporting physiologic loads that would otherwise be supported by a healthy tissue. In this review we will examine the development of scaffolds derived from biopolymers and their use with various cell types in the context of tissue engineering the nucleus pulposus of the intervertebral disc. [Pg.201]

Li CQ et al (2009) Construction of collagen II/hyaluronate/chondroitin-6-sulfate tri-copoly-mer scaffold for nucleus pulposus tissue engineering and preliminary analysis of its physicochemical properties and biocompatibility. J Mater Sci Mater Med 21 741-751... [Pg.229]

Calderon L et al (2010) Type II collagen-hyaluronan hydrogel-a step towards a scaffold for intervertebral disc tissue engineering. Eur Cell Mater 20 134—148... [Pg.229]

Tedder ME et al (2009) Stabilized collagen scaffolds for heart valve tissue engineering. Tissue Eng Part A 15(6) 1257-1268... [Pg.230]

Daamen WF et al (2003) Preparation and evaluation of molecularly-defined collagen-elastin-glycosaminoglycan scaffolds for tissue engineering. Biomaterials 24(22) 4001-4009... [Pg.230]

R. A. MacDonald, B.F. Laurenzi G. Viswanathan P. M. Ajayan J. P. Stegemann, Collagen-carbon nanotube composite materials as scaffolds in tissue engineering, Journal of Biomedical Materials Research Part A, vol. 74A, pp. 489-496, 2005. [Pg.120]

In biomedical applications, transglutaminases have been used for tissue engineering materials such as enzymatically crosslinked collagen [60-63] or gelatin scaffolds [64-69]. Even melt-extruded guides based on enzymatically crosslinked macromolecules for peripheral nerve repair have been reported [70]. [Pg.28]

Lyons, F. G., Al-Munajjed, A. A., Kieran, S. M., Toner, M. E., Murphy, . M., Duffy, G. P., and O Brien, F. J. (2010). The healing of bony defects by cell-free collagen-based scaffolds compared to stem cell-seeded tissue engineered constructs. Biomaterials 31, 9232-9245. [Pg.118]

In Nature, there are many examples of protein and peptide molecular self-assembly. Of the genetically engineered fibrous proteins, collagen, spider silks, and elastin have received attention due to their mechanical and biological properties which can be used for biomaterials and tissue engineering. [Pg.97]

Hu, K., Lv, Q., Cui, F.Z., Feng, Q.L., Kong, X.D., Wang, H.L., Huang, L.Y., and Li, T. "Biocompatible fibroin blended films with recombinant human-like collagen for hepatic tissue engineering". J. Bioact. Compat. Polym. 21(1), 23-37 (2006a). [Pg.152]


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See also in sourсe #XX -- [ Pg.352 ]

See also in sourсe #XX -- [ Pg.37 , Pg.38 ]




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