## 4 Discussion
Proline is reported as a desirable residue, but also aliphatic peptides such lysine is responsible for the ACE-inhibitory capacity. The molecular docking interactions in this study also corroborate kinetic analyses in our previous work, where cricket peptides demonstrated mixed-type inhibition towards ACE, indicating that binding was possible with both free enzyme and enzyme-substrate complex, to suppress ACE activity [40]. YKPRP, PHGAP, and VGPPQ all coordinate with residues within the active site, as well as non-catalytic residues. This suggests that these peptides might be able to stabilize in an inactive state, even if bound to its target substrate. [PERSON] et al. [41] also isolated ACE inhibitory peptides from cricket (_G. sigillatus_) protein hydrolysates. They identified the sequences IIAPPER, LAPSTIK, KAPEEHPV, KVEGDLK, which showed no homology to the peptides identified in this study. These differences were attributed to conditions used to liberate bioactive peptides and pretreatment techniques, also demonstrated in their study (i.e., raw vs boiling before extraction). To the best of our knowledge, the bioactive pentapeptide sequences derived from this study using CPHD were not previously reported. Based on the results obtained in this study, analyzing the molecular mechanism involved between these identified peptide sequences on hypertensive, glycemic, and inflammatory responses, as well as their in vivo bioactive effects, will be the focus of future studies. Considering the variety of activity displayed in this study, enhanced potency post-fractionation, and affinity of novel peptides towards ACE (a central regulator \begin{table}
\begin{tabular}{c c c c c c c c c c c} \hline \hline \multirow{2}{*}{**Legend**} & \multirow{2}{*}{**Affinity Energy**} & \multirow{2}{*}{**Zn (II) Coordination**} & \multicolumn{6}{c}{**Interaction with ACE Active Site Residues *} \\ \cline{3-10}  & & & & **Glu384** & & **Ty523** & **Ala354** & **Gln281** & **Ty520** & **Lys511** & **His513** & **His353** \\ \hline \multirow{2}{*}{Captopril} & \multirow{2}{*}{–24.26} & sulfhydryl group of & \multirow{2}{*}{captopril} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} \\  & & & & & & & & & & & \\ YKPRP & \multirow{2}{*}{–39.75} & None & \multirow{2}{*}{–} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{–} & \multirow{2}{*}{–} & \multirow{2}{*}{–} & \multirow{2}{*}{+} & \multirow{2}{*}{+} \\  & & & & & & & & & & \\ PHGAP & \multirow{2}{*}{–36.82} & carboxylic acid group & \multirow{2}{*}{–} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{–} & \multirow{2}{*}{+} & \multirow{2}{*}{+} \\  & & & & & & & & & & \\  & & & & & & & & & & \\ VGPPQ & \multirow{2}{*}{–36.87} & carboxylic acid group & \multirow{2}{*}{+} & \multirow{2}{*}{+} & \multirow{2}{*}{–} & \multirow{2}{*}{–} & \multirow{2}{*}{–} & \multirow{2}{*}{+} & \multirow{2}{*}{+} \\  & & & & & & & & & & \\ \hline \multicolumn{10}{l}{* Interactions are denoted with a “+-” indicating that there was an interaction between the ACE residue and ligand} \\ \multicolumn{10}{l}{ or “–”indicating no interaction.} \\ \end{tabular}
\end{table} 
Table 3: Predicted binding energies, ZN(II) coordination, and ACE residues that interact with the docked ligands. of the renin-angiotensin aldosteroneone system and known target for treating hypertension) highlights that cricket-derived peptides could play a significant beneficial role in the pathology involved in cardiovascular dysfunction.