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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
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 hydrol...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864793/ https://www.ncbi.nlm.nih.gov/pubmed/36662222 http://dx.doi.org/10.3390/md21010049 |
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author | Mune Mune, Martin Alain Miyabe, Yoshikatsu Shimizu, Takeshi Matsui, Wataru Kumagai, Yuya Kishimura, Hideki |
author_facet | Mune Mune, Martin Alain Miyabe, Yoshikatsu Shimizu, Takeshi Matsui, Wataru Kumagai, Yuya Kishimura, Hideki |
author_sort | Mune Mune, Martin Alain |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9864793 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98647932023-01-22 Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda Mune Mune, Martin Alain Miyabe, Yoshikatsu Shimizu, Takeshi Matsui, Wataru Kumagai, Yuya Kishimura, Hideki Mar Drugs Article 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. MDPI 2023-01-11 /pmc/articles/PMC9864793/ /pubmed/36662222 http://dx.doi.org/10.3390/md21010049 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Mune Mune, Martin Alain Miyabe, Yoshikatsu Shimizu, Takeshi Matsui, Wataru Kumagai, Yuya Kishimura, Hideki Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title_full | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title_fullStr | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title_full_unstemmed | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title_short | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
title_sort | characterisation of bioactive peptides from red alga gracilariopsis chorda |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864793/ https://www.ncbi.nlm.nih.gov/pubmed/36662222 http://dx.doi.org/10.3390/md21010049 |
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