Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel <i>Gigantidas vrijenhoeki</i>
oleh: Seong-Yeong Heo, Nalae Kang, Eun-A Kim, Junseong Kim, Seung-Hong Lee, Ginnae Ahn, Je Hyeok Oh, A Young Shin, Dongsung Kim, Soo-Jin Heo
| Format: | Article |
|---|---|
| Diterbitkan: | MDPI AG 2023-08-01 |
Deskripsi
The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, <i>Gigantidas vrijenhoeki</i>. The <i>G. vrijenhoeki</i> protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activity and was fractionated into four molecular weight ranges by ultrafiltration. The <1 kDa fraction exhibited the highest ACE inhibitory activity and was found to have 11 peptide sequences. Among the analyzed peptides, KLLWNGKM exhibited stronger ACE inhibitory activity and an IC<sub>50</sub> value of 0.007 μM. To investigate the ACE-inhibitory activity of the analyzed peptides, a molecular docking study was performed. KLLWNGKM exhibited the highest binding energy (−1317.01 kcal/mol), which was mainly attributed to the formation of hydrogen bonds with the ACE active pockets, zinc-binding motif, and zinc ion. These results indicate that <i>G. vrijenhoeki</i>-derived peptides can serve as nutritional and pharmacological candidates for controlling blood pressure.