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By Rosario Pignatello

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Existence of locally unfolded states in collagen molecule has been also suggested (Escat, 2010), according to which, folded structure of collagen cannot fit into the catalytic site, since collagen triple-helix has a diameter of approximately 15 Å, whiles catalytic domain of MMPs has a catalytic site of only 5 Å wide. Beside, scissile bond, cleaved by collagenases is buried in collagen structure when collagen is exposed to solvent, which make it inaccessible for scission. Local unfolding is collagen triple-helix property, which occur without presence of collagenases, but necessary for collagen degradation in collagenase presence.

2011). However, the amino acid compositions are slightly different among all types of gelatine from different sources. , 2010). With the exception of gelatine from pigskin origin, all other gelatines do not contain aspartic acid (Asp) and glutamic acid (Glu). During the denaturation-hydrolysis process (Fig. , 2008). As the collagen matures, the cross-links become stabilised, because ε-amino groups of lysine (Lys) become linked to arginine (Arg) by glucose molecules (Mailard reaction), forming extremely stable pentosidine type cross-links.

5. Conclusion This review presents the characteristic properties of both fibrous proteins including biocompatibility, non-immunogenicity, their capacities for modification at the molecular level, thus rendering or tuning their functional (surface/interfacial, mechanical, topological and morphological) properties, characteristic gelation (sol-gel transition) and gel-forming abilities and, finally, their bio-absorbability and biodegradability. In addition, their expanding applications for biomaterials are compared, with emphasis on the importance of understanding their suitability, as defined biomaterials with specific properties, for certain cell types.

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