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The extracellular matrix (ECM) is composed of a mixture of glue-like macromolecules in the extracellular spaces which give a tissue its characteristic form and maintains its integrity [Exposito, 2002; Gelse, 2003]. The ECM also regulates a variety of cellular behaviors such as proliferation, differentiation, motion and communication [Kadler, et al., 2007; Tsuchiya, et al., 2007]. Collagens are the most abundant proteins in the animal kingdom and have been highly conserved in evolution [Exposito, 2002; Kadler, et al., 2007]. These proteins constitute one third of the human proteome and contribute threequarters of dry weight of human skin [Kotch & Raines, 2006]. Increasingly, this family of proteins is gaining attention from scientists in different fields, ranging from biochemistry to tissue engineering. In the last century, collagen has been studied extensively by researchers from different disciplines including chemistry, physics, medicine and biology. Despite of this intensity, the understanding of many collagen properties is still limited and the number of collagen types or collagen-like proteins (CLP) discovered are increasing continuously. Type I collagen is the most abundant protein in the animal body and located in all ECM of connective tissues like bone, skin, tendon and blood vessels. The primary function of Type I collagen is to give mechanical support for the structural organization of the ECM of connective tissues, therefore giving the tissues their characteristic form and maintaining the cellular integrity in the ECM. Possibly there are still many unknown functions to be found. Type I collagen represents the characteristic structure very well and has the characteristic large domains comprised of peptides with varied length of [Gly-X-Y], where X and Y are generally proline (Pro), repeats with a length about 300 nm and folded into unique triple helix structure as its native form [Prockop, & Kivirikko, 1995]. Every chain from the three polypeptide-chains (α1)2(α2) form a left-handed helix then fold together to form a righthanded triple helix.

Preparation and Characterization Urea-Solubilized Sol-Gel Type I Collagen and Its Possible Use in Applications