Effect Of Succinylation On The Bioactive Structure Of Collagen
Keywords
Collagen, Succinic Anhydride, Biological Activity
Abstract
In this experiment, pig skin collagen was used as the research object. Acylated collagen was prepared by modifying succinic anhydride. Instrumental analysis was used to detect the retention degree of the triple helical structure of acylated collagen. On this basis, atomic force microscopy and fibroblasts were used. The biological activity of acylated collagen was further investigated in culture experiments. The results showed that the acylation degree of collagen was 62.4%, and the isoelectric point of acylated collagen was reduced to 4.1. The results of X-ray diffraction (XRD), thermal denaturation temperature, and circular dichroism spectroscopy showed that the modification of succinic anhydride did not destroy the triple helix structure of collagen as a whole; acylated collagen showed collagen under an atomic force microscope. Unique fiber structure. Fibroblast culture experiments found that acylated collagen is compatible with fibroblasts and promotes fibroblast proliferation to a certain extent. Succinylation will not destroy the bioactive structure of collagen.
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Original research was done by Liu Jie, Xu Zhou, Fan Haojun, Chen Yi
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