2. Academic Validation
  3. Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda

Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda

  • Mar Drugs. 2023 Jan 11;21(1):49. doi: 10.3390/md21010049.
Martin Alain Mune Mune 1,  Yoshikatsu Miyabe 2 3,  Takeshi Shimizu 4,  Wataru Matsui 2,  Yuya Kumagai 5,  Hideki Kishimura 5
Affiliations

Affiliations

  • 1 Faculty of Science, University of Maroua, Maroua P.O. Box 814, Cameroon.
  • 2 Chair of Marine Chemical Resource Development, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, Hokkaido, Japan.
  • 3 Aomori Prefectural Industrial Technology Research Center, Hachinohe 031-0831, Aomori, Japan.
  • 4 Hokkaido Industrial Technology Center, Department of Research and Development, Hakodate 041-0801, Hokkaido, Japan.
  • 5 Laboratory of Marine Chemical Resource Development, Faculty of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, Hokkaido, Japan.
PMID: 36662222 DOI: 10.3390/md21010049
Abstract

In this study, we studied the bioactive peptides produced by thermolysin hydrolysis of a water-soluble protein (WSP) from the red alga Gracilariopsis chorda, whose major components are phycobiliproteins and Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCo). The results showed that WSP hydrolysate exhibited significantly higher ACE inhibitory activity (92% inhibition) compared to DPP-IV inhibitory activity and DPPH scavenging activity. The phycobiliproteins and RuBisCo of G. chorda contain a high proportion of hydrophobic (31.0-46.5%) and aromatic (5.1-46.5%) amino acid residues, which was considered suitable for the formation of peptides with strong ACE inhibitory activity. Therefore, we searched for peptides with strong ACE inhibitory activity and identified two novel peptides (IDHY and LVVER). Then, their interaction with human ACE was evaluated by molecular docking, and IDHY was found to be a promising inhibitor. In silico analysis was then performed on the structural factors affecting ACE inhibitory peptide release, using the predicted 3D structures of phycobiliproteins and RuBisCo. The results showed that most of the ACE inhibitory peptides are located in the highly solvent accessible α-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides.

Keywords

ACE inhibitory activity; DPP-IV inhibitory activity; DPPH scavenging activity; Gracilariopsis chorda; bioactive peptides; red alga.

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