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Its structure allows researchers to focus on specific matrix-related pathway behavior, cellular response, and structure-function relationships under laboratory conditions

In both peptides, the N-terminal histidine sits in an enclosed pocket forming hydrophobic and hydrogen bond interactions with E364 6 .53 , E387 7 .42 , R310 5 .40 , Y241 3 .44 , W306 5 .36 , I313 5 .43 and Q234 3 .37 however, these interactions are more persistent with GLP-1, and this is likely linked to the stability of interactions of Glu9 and with residues at the base of the binding cavity (Supplemental Table 3, Supplemental Movie 1)

This combination targets both joint healing and soft tissue repair simultaneously