Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda

Mune Mune, Martin Alain; Miyabe, Yoshikatsu; Shimizu, Takeshi; Matsui, Wataru; Kumagai, Yuya; Kishimura, Hideki

Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda

Mune Mune, Martin Alain; Miyabe, Yoshikatsu; Shimizu, Takeshi et al.

Marine drugs, 2023, 21(1), 49

Permalink : https://hdl.handle.net/2115/88100

このアイテムのアクセス数:309件（2026-08-16 23:43 集計）

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ファイル	フォーマット	サイズ	閲覧回数	説明
https://doi.org/10.3390/md21010049			191

論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/88100
タイトル	Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
著者	Mune Mune, Martin Alain ; Miyabe, Yoshikatsu ; Shimizu, Takeshi ; Matsui, Wataru ; Kumagai, Yuya ; Kishimura, Hideki
著者名 Mune Mune, Martin Alain
著者名 Miyabe, Yoshikatsu
著者名 Shimizu, Takeshi
著者名 Matsui, Wataru
e-Rad_Researcher 00589997 著者名 Kumagai, Yuya
e-Rad_Researcher 50204855 著者名 Kishimura, Hideki
言語	英語
キーワード	red alga
	Gracilariopsis chorda
	bioactive peptides
	ACE inhibitory activity
	DPP-IV inhibitory activity
	DPPH scavenging activity
発行日	2023-01
出版者	MDPI
収録物名	Marine drugs
巻(号)	21(1)
ページ	49
抄録	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 alpha-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.3390/md21010049