Abstract
ABSTRACTThe aim of this study was to demonstrate the effect of different treatments on collagen self-assembly, the morphological and the qualitative analysis of collagen assembly were measured by atomic force microscopy. Collagen samples were treated with 0.02%, 0.04%, 0.10% and 0.20% glutaraldehyde individually at the first steps. Meanwhile, the other experimental groups were treated with 0.05%, 0.10%, 0.20% riboflavin, respectively, the structural change of the collagen network with 15, 30, 45, 60 min UV365 exposure and the fluorescent irradiation as the control group in turn was investigated by atomic force microscopy. The width and height of collagen assembly increased with the concentration of glutaraldehyde, which were changed from 36.45 ± 4.45nm to 64.35 ± 2.58nm and 2.26 ± 0.19nm to 4.93 ± 0.29 nm, respectively. The effect of different UV365 irradiation time on the height of collagen was greater than the effect on the width, the width and height of collagen were varied from 41.36 ± 4.30nm to 55.47 ± 4.53nm and 3.10 ± 0.39nm to 6.20 ± 0.85nm, which were changed 25.44% and 50.00%, respectively. The concentration of riboflavin was more efficiently than irradiation time, and the maximum width and height of collagen reached 106.98 ± 3.37nm and 11.17 ± 1.33 nm, respectively, the control group without a significant change at the fluorescent irradiation by the time. This optimized cross-linking method with riboflavin/UV365 would have great potential for tissue engineering in clinic and food packaging science.
Highlights
Packaging and food industry are increasingly focusing on the development of biodegradable packaging materials, protein films play a very important role in this field
Heo and his colleagues suggested that the mechanical properties of collagen scaffold after photo crosslinking had been significantly improved, so it was better used in meniscus tissue engineering.[2]
atomic force microscopy (AFM) was used to explore the morphology of collagen treated with glutaraldehyde in different concentrations
Summary
Packaging and food industry are increasingly focusing on the development of biodegradable packaging materials, protein films play a very important role in this field. Wang and Rhim reported that collagen was mixed with agar and alginate to obtain a film with strong antibacterial properties.[1] What is more, collagen exhibits excellent biocompatibility and low antigenicity and benefits numerous cellular behaviours, so it has been widely utilized in tissue engineering. Heo and his colleagues suggested that the mechanical properties of collagen scaffold after photo crosslinking had been significantly improved, so it was better used in meniscus tissue engineering.[2] Collagen mainly distributed in the skin, tendons and other organizations. It is composed of three polypeptide chains forming three helical structures, and its amino acids present (Gly-X-Y)n periodic arrangement, where the positions of X and Y are proline and hydroxyproline, which are the specific amino acids of collagen, accounting for about 25%, and it is
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