2010
DOI: 10.1016/j.ijbiomac.2010.08.004
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Chemical and thermal cross-linking of collagen and elastin hydrolysates

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Cited by 97 publications
(77 citation statements)
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“…Many attempts have been made to overcome this problem through the means of mixing collagen with either natural (e.g. elastin [11,12], chitosan [10,12], glycoaminoglycans -GAGs [13,14]) or synthetic polymers (e.g. poly(vinyl alcohol) -PVA [15], polycaprolactone -PCL [6,16], polylactic acid -PLLA [6], polyglycolic acid -PGA [6,17]) or by adding mineral crystals [18,19].…”
Section: Introductionmentioning
confidence: 99%
“…Many attempts have been made to overcome this problem through the means of mixing collagen with either natural (e.g. elastin [11,12], chitosan [10,12], glycoaminoglycans -GAGs [13,14]) or synthetic polymers (e.g. poly(vinyl alcohol) -PVA [15], polycaprolactone -PCL [6,16], polylactic acid -PLLA [6], polyglycolic acid -PGA [6,17]) or by adding mineral crystals [18,19].…”
Section: Introductionmentioning
confidence: 99%
“…4b, the positions of peaks before and after cross-linked collagen are located in the completely same points, but the area of the IR bands for cross-linked collagen is much smaller compared to uncross-linked collagen. According to Sinokowska et al [26], the position of IR spectra for the collagen cross-liked with EDC could be same with the uncross-linked collagen because the secondary structure of collagen is not destroyed. Also, the coupled area of amide A and OH band (3,700-3,100 cm -1 ) is much smaller for cross-linked collagen because crosslinked collagen loses water bonded to the collagen [26].…”
Section: Characterization Of Collagen Scaffoldmentioning
confidence: 98%
“…According to Sinokowska et al [26], the position of IR spectra for the collagen cross-liked with EDC could be same with the uncross-linked collagen because the secondary structure of collagen is not destroyed. Also, the coupled area of amide A and OH band (3,700-3,100 cm -1 ) is much smaller for cross-linked collagen because crosslinked collagen loses water bonded to the collagen [26]. From these IR spectra, the collagen was sufficiently crosslinked in the EDC solution.…”
Section: Characterization Of Collagen Scaffoldmentioning
confidence: 98%
“…In fact, it is used as suture material in surgery [304], as depot delivery device in the local extended release of antibiotics [305], DNA [306], siRNA [307], and proteins [308] and as haemostatic sealant [309]. In tissue engineering, collagen sponges are widely diffused due to their ability to withstand high tensile loads (92.5 MPa ultimate tensile strength) [310]. Other applications of collagen relate to reconstructive skin surgery and tissue engineering scaffold for cartilage, tendon, and ligament [311].…”
Section: Proteins and Poly(amino Acids)mentioning
confidence: 99%