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It has a trans-3-hexenoic acid moiety at the N terminus which makes it resistant to enzymatic degradation, by dipeptidyl peptidases in particular

doi: 10.3389/FANIM.2023.1269775/BIBTEX 26 Cantalapiedra-HijarG.Ortigues-MartyI.SepchatB.TitgemeyerE.BahloulL

The peptide sequence consists of fifteen amino acids arranged as Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, forming a stable molecular structure that demonstrates resistance to enzymatic degradation compared to other peptide compounds

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