Abstract:

In this study, acylated collagen from pig skin was prepared by succinic anhydride modification. The degree of
retention of the collagen triple helix structure was detected by instrumental analysis, and then the biological activity of
acylated collagen was further investigated through atomic force microscopy and fibroblast culture. The results showed that
the acylation degree of collagen was 62.4%, and the isoelectric point of acylated collagen decreased to 4.1. X-Ray diffraction
(XRD) analysis, thermal denaturation temperature determination, and circular dichroism analysis indicated that the triple
helix structure of collagen was not destroyed after modification by succinic anhydride. The acetylated collagen presented
specific fiber structure under atomic force microscope. Fibroblast culture experiments showed the acetylated collagen could
be compatible with fibroblast cells, and partly promote their proliferation. To conclude, acetylation does not destroy the
biological activity and structure of collagen.

Key words: collagen, succinic anhydride, bioactivity