Study Of Modified Collagen Mimetic Peptide And Its Stability

Collagen, the most abundant protein in animals, is important structure support involved in the various levels of tissue from extracellular matrix to skin proteins, therefore, study for the stability of collagen is extremely important. Much process has obtained about the relationship between the collagen structure and its stability. Studies have shown that both the inter-strand H bond and the ring puckering are crucial for the conformational stability of the collagen triple helix, the substituent steric and stereo-electronic effects also make a difference. The methods to Amp for Yaa position, which has an electron-withdrawing effect and inter-strand H bond with solvent, could find the different role for the stability of collagen between the two effects. Our experimental design to introduce radical and glycosylation label for the Amp marker, apply CD and EPR test the unfold process of collagen mimetic peptide to compare the effect of different labels on conformation stability. In addition, we synthesized galactose -modified Amp molecules and explored the glycosylation collagen triple helix structure by NMR to detect the cis/trans ratio of Pro peptide bond. Study of modified collagen mimetic peptide and its stability not only increase the understanding of the structure and stability of collagen, but also can be a guide for the synthesis of a new biomedical research and artificial functional collagen nanomaterial.