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By Rosario Pignatello
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Additional resources for Biomaterials applications for nanomedicine
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. During the alkaline processing, the alkali breaks one of the initial (pyridinoline) cross-links and as a result, on heating the collagen releases, mainly, denatured α-chains into solution. Once the pentosidine cross-links of the mature animal have formed in the collagen, the main process of denaturation has to be thermal hydrolysis of peptide bonds, resulting in protein fragments being from below 100 kDa to more than 700 kDa, and with IEP between 4,6 and 9.
Apart from collagenases, gelatinases play an important role in collagen degradation. Besides, with any further degradation of initially-cleaved collagen, gelatinases can degrade native collagen type I, IV, V and VII (Overall, 1991). , 1999). 3 Immunological response of collagen-based biomaterials As already mentioned, the implantation of biomaterials often initiates acute inflammatory responses, which sometimes can cause chronic inflammatory response. Measuring the intensities and duration of the immune responses against implanted biomaterials is important for biocompatibility evaluation.
2) collagen, the predominant genetic type in the collagen family being the major component of tendons, bones and ligaments, is a heterotrimeric copolymer composed of two α1 (I) and one α2 (I) chains, containing approximately 1050 amino acids each. , 2004). Its molecule consist of three domains: aminoterminal nontriple helical (N-telopeptide), central triple helical consisting of more than 300 repeat units and represent more than 95% of polypeptide, and carboxy-terminal nontriple helical (C-telopeptide) (Yamauchi & Shiiba, 2008).