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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...

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Autores principales: Mune Mune, Martin Alain, Miyabe, Yoshikatsu, Shimizu, Takeshi, Matsui, Wataru, Kumagai, Yuya, Kishimura, Hideki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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.
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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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