Modification of protein could give their new functionality but would affect their intrinsic property and activity. In this paper, a series of succinylated collagen (SCol(n/1)) (n≥1) were prepared by modification… Click to show full abstract
Modification of protein could give their new functionality but would affect their intrinsic property and activity. In this paper, a series of succinylated collagen (SCol(n/1)) (n≥1) were prepared by modification of collagen with succinic anhydride at different molar ratio to amino groups amount of collagen. The impact of grafting density on the intrinsic self-assembly and additional hydrophilicity of succinylated collagen was explored. The results revealed that excessive grafting density of succinylated collagen would improve their hydrophilicity but weaken their self-assembly property, although the triple helix of collagen could be reserved after succinylation. SCol(1/1) (grafting density of 17%) with self-assembly property and good hydrophilicity was chosen to compare with native collagen. Compared to native collagen, thermostability of SCol(1/1) decreased slightly, however, SCol(1/1) could form softer hydrogel, which was more favorable for the proliferation of NIH/3 T3. The present work would help us to further understand the importance of grafting density for the design of modified collagen with intrinsic self-assembly property and additional new functionality.
               
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