Identification of a Novel ACE Inhibitory Hexapeptide from Camellia Seed Cake and Evaluation of Its Stability

Zhu, Qiaonan; Xue, Jiawen; Wang, Peng; Wang, Xianbo; Zhang, Jiaojiao; Fang, Xuezhi; He, Zhiping; Wu, Fenghua

doi:10.3390/foods12030501

Cited by 10 publications

(2 citation statements)

References 38 publications

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“…MD simulation [ 18 , 26 ], molecular interactions [ 18 , 27 ], simulated digestion in vitro [ 9 , 10 , 11 , 20 , 25 , 28 ], and antihypertensive effects evaluation in vivo [ 14 , 22 , 29 ] effectively verify and reveal the ACE inhibition mechanism. The peptide–receptor complex’s interaction mode and conformation changes can help improve our understanding of the inhibition mechanism.…”

Section: Discussionmentioning

confidence: 99%

Structure–Activity Relationship of Novel ACE Inhibitory Undecapeptides from Stropharia rugosoannulata by Molecular Interactions and Activity Analyses

Li,

Chen,

Wang

et al. 2023

Foods

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Undecapeptide is the central peptide molecule in the peptide base material of Stropharia rugosoannulata, and angiotensin-converting enzyme (ACE) plays a crucial role in hypertension. To fully explore the interaction mechanism and ACE-inhibitory activity of long-chain peptides from Stropharia rugosoannulata, the binding conformations of twenty-seven undecapeptides with the ACE receptor were revealed by molecule docking. The undecapeptide GQEDYDRLRPL with better receptor binding capacity and higher secondary mass spectral abundance was screened. All amino acid residues except proline in GQEDYDRLRPL interacted with the ACE receptor. GQEDYDRLRPL interfered with the receptor’s overall structure, with significant fluctuations in amino acid residues 340–355, including two residues in the receptor’s active pockets. The binding constants of GQEDYDRLRPL to the ACE receptors were at the μM level, with a kinetic binding constant of 9.26 × 10−7 M, which is a strong binding, and a thermodynamic binding constant of 3.06 × 10−6 M. Intermolecular interaction were exothermic, enthalpy-driven, and specific binding reactions. GQEDYDRLRPL had an IC50 value of 164.41 μmol/L in vitro and superior antihypertensive effects at low-gavage administration in vivo. Obtaining information on the interaction mechanism of ACE-inhibitory undecapeptides from S. rugosoannulata with the ACE receptor will help to develop and utilize ACE inhibitors of natural origin.

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Section: Discussionmentioning

confidence: 99%

Structure–Activity Relationship of Novel ACE Inhibitory Undecapeptides from Stropharia rugosoannulata by Molecular Interactions and Activity Analyses

Li,

Chen,

Wang

et al. 2023

Foods

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“…A slight modification of the research methodology based on the previous study [ 48 ] was implemented. With slight modification, the peptide samples were dissolved in deionized water (1 mg/mL), adjusted the pH to 2 with 1 M HCl, pepsin (2% w / w ) was added, and the reaction was run for 2 h at 37 °C in the temperature shaker.…”

Section: Methodsmentioning

confidence: 99%

Biodirected Screening and Preparation of Larimichthys crocea Angiotensin-I-Converting Enzyme-Inhibitory Peptides by a Combined In Vitro and In Silico Approach

Yang,

Wang,

Huang

et al. 2024

Molecules

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Food-derived angiotensin-I-converting enzyme (ACE)-inhibitory peptides have gained attention for their potent and safe treatment of hypertensive disorders. However, there are some limitations of conventional methods for preparing ACE-inhibitory peptides. In this study, in silico hydrolysis, the quantitative structure–activity relationship (QSAR) model, LC-MS/MS, inhibition kinetics, and molecular docking were used to investigate the stability, hydrolyzability, in vitro activity, and inhibition mechanism of bioactive peptides during the actual hydrolysis process. Six novel ACE-inhibitory peptides were screened from the Larimichthys crocea protein (LCP) and had low IC50 values (from 0.63 ± 0.09 µM to 10.26 ± 0.21 µM), which were close to the results of the QSAR model. After in vitro gastrointestinal simulated digestion activity of IPYADFK, FYEPFM and NWPWMK were found to remain almost unchanged, whereas LYDHLGK, INEMLDTK, and IHFGTTGK were affected by gastrointestinal digestion. Meanwhile, the inhibition kinetics and molecular docking results were consistent in that ACE-inhibitory peptides of different inhibition forms could effectively bind to the active or non-central active centers of ACE through hydrogen bonding. Our proposed method has better reproducibility, accuracy, and higher directivity than previous methods. This study can provide new approaches for the deep processing, identification, and preparation of Larimichthys crocea.

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The Synergistic Activity and Interaction Mechanism of Linoleic Acid and a Bioactive Pentapeptide (Tyr-Val-Pro-His-Trp) from Walnut Meal in the Treatment of Alzheimer’s Disease

Wang

Ling

Liang

et al. 2023

Int J Pept Res Ther

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Identification of a Novel ACE Inhibitory Hexapeptide from Camellia Seed Cake and Evaluation of Its Stability

Cited by 10 publications

References 38 publications

Structure–Activity Relationship of Novel ACE Inhibitory Undecapeptides from Stropharia rugosoannulata by Molecular Interactions and Activity Analyses

Structure–Activity Relationship of Novel ACE Inhibitory Undecapeptides from Stropharia rugosoannulata by Molecular Interactions and Activity Analyses

Biodirected Screening and Preparation of Larimichthys crocea Angiotensin-I-Converting Enzyme-Inhibitory Peptides by a Combined In Vitro and In Silico Approach

The Synergistic Activity and Interaction Mechanism of Linoleic Acid and a Bioactive Pentapeptide (Tyr-Val-Pro-His-Trp) from Walnut Meal in the Treatment of Alzheimer’s Disease

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