Screening, ACE-inhibitory mechanism and structure-activity relationship of a novel ACE-inhibitory peptide from Lepidium meyenii (Maca) protein hydrolysate

Lin, Zhengli; Lai, Junwen; He, Ping; Pan, Leiman; Zhang, Yizhe; Zhang, Mengmeng; Wu, Hui

doi:10.1016/j.fbio.2023.102374

Cited by 18 publications

(21 citation statements)

References 44 publications

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“…PEAKS Studio8.5 was used to analyze the raw MS files, and 359 peptides were identified. The traditional bioactive peptide screening method is time-consuming and laborious [ 27 ]. Hence, bioinformatics is used to replace traditional methods for rapid screening of peptides.…”

Section: Resultsmentioning

confidence: 99%

“…In the silicon analysis based on the PeptideRanker database, in order to reduce false negatives and obtain as many potential bioactive peptides as possible, we set the score screening threshold to 0.5; that is, peptides with a score higher than 0.5 are considered to have potential biological activity [ 27 ]. A total of 17 peptides meet the requirements.…”

Section: Resultsmentioning

confidence: 99%

“…Conversely, GYGL, which hardly meets the rules, shows strong activity. The difference in the results may be due to the fact that the amino acid composition may not fully determine the ACE inhibitory activity of the peptide; and that the activity may be affected by other factors such as spatial conformation and hydrophobicity [ 27 ]. Because VW-7 has the strongest ACE inhibitory activity, it was chosen for further study.…”

Section: Resultsmentioning

confidence: 99%

“…Meanwhile, the tetrahedral ligand that Zn 2+ forms with His387, His383, and Glu411 is crucial to the binding affinity between ACE and inhibitors [ 30 , 39 ]. This active site region is also known as the HEXXH zinc-binding motif [ 27 ]. Many ACE inhibitors, including captopril and enalapril, can interact with Zn 2+ [ 40 ].…”

Section: Resultsmentioning

confidence: 99%

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Purification, Identification, and Inhibitory Mechanisms of a Novel ACE Inhibitory Peptide from Torreya grandis

Wu¹,

Luo

Zhang

et al. 2023

Nutrients

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Torreya grandis meal has a high protein content and an appropriate amino acid ratio, making it an excellent protein source for producing ACE inhibitory peptides. To promote its application in food, medicine, and other fields, an alkaline protease hydrolysate of Torreya grandis was used in this study to isolate and identify a novel angiotensin-converting enzyme inhibitory peptide, VNDYLNW (VW-7), using ultrafiltration, gel chromatography purification, LC-MS/MS, and in silico prediction. The results show that the IC50 value of VW-7 was 205.98 µM. The Lineweaver–Burk plot showed that VW-7 had a mixed-type inhibitory effect on ACE. Meanwhile, according to the results of molecular docking, VW-7 demonstrated a strong affinity for ACE (binding energy −10 kcal/mol). VW-7 was bound to ACE through multiple binding sites. In addition, VW-7 could remain active during gastrointestinal digestion in vitro. Nitric oxide (NO) generation in human endothelial cells could rise after receiving a pretreatment with VW-7. These results indicated that Torreya grandis meal protein can be developed into products with antihypertensive function, and VW-7 has broad application prospects in the field of antihypertensive.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Purification, Identification, and Inhibitory Mechanisms of a Novel ACE Inhibitory Peptide from Torreya grandis

Wu¹,

Luo

Zhang

et al. 2023

Nutrients

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“…To evaluate the biological activities of the identified peptides, both Peptide Ranker (http://distilldeep.ucd.ie/PeptideRanker/) and the "Profiles of potential biological activity" tab in BIOPEP-UWM can be subsequently used (Lin et al, 2023;Tian et al, 2022). In addition, ADMETlab can be used to systematically predict the in vivo pharmacokinetic properties (including absorption, distribution, metabolism, excretion, and toxicity) of the active peptides, providing evaluations that are especially conducive to the preliminary screening of the peptides ( Dong et al, 2018;Lin et al, 2023). By combining the above bioinformatics tools, it is possible to greatly reduce the complexity of the workflow required for screening ACE inhibitory peptides.…”

Section: Introductionmentioning

confidence: 99%

A novel ACE inhibitory peptide from Pelodiscus sinensis Wiegmann meat

Liu,

Sun,

Zhang

et al. 2024

Preprint

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Pelodiscus sinensis meat is a nutritional food and tonic with angiotensin-converting enzyme (ACE) inhibitory activities. To identify the bioactive substances responsible, several bioinformatics methods were integrated to enable a virtual screening for bioactive peptides in proteins identified within a water-soluble protein fraction of Pelodiscus sinensis meat by Shotgun proteomics. The peptides were generated from the identified proteins by in silico proteolysis using six proteases. A comparison of the numbers of proteins suitable for digestion with each enzyme and the iBAQ (intensity-based absolute quantification) values for these proteins revealed that bromelain and papain were the most suitable proteases for this sample. Next, the water solubility, toxicity, and ADMET (absorption/ distribution/ metabolism/ excretion/ toxicity) properties of these peptides were evaluated in silico. Finally, a novel ACE inhibitory peptide IEWEF with an IC50 value of 42.34 µM was identified. The activity of the synthesized peptide was verified in vitro, and it was shown to be a non-competitive ACE inhibitor. Molecular docking revealed that IEWEF could tightly bind to ACE, C-ACE, and N-ACE with energies of-8.9,-9.4, and-8.7 kJ·mol-1 , respectively. These results provide evidence that bioactive peptides in the water-soluble protein fraction account for (at least) some of the ACE inhibitory activities observed in Pelodiscus sinensis meat. Furthermore, our research provides a workflow for the efficient identification of novel ACE inhibitory peptides from complex protein mixtures.

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A novel ACE inhibitory peptide from Pelodiscus sinensis Wiegmann meat water-soluble protein hydrolysate

Liao,

Liu,

Sun

et al. 2024

Amino Acids

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Pelodiscus sinensis meat is a nutritional food and tonic with angiotensin-converting enzyme (ACE) inhibitory activities. To identify the bioactive substances responsible, several bioinformatics methods were integrated to enable a virtual screening for bioactive peptides in proteins identified within a water-soluble protein fraction of Pelodiscus sinensis meat by Shotgun proteomics. The peptides were generated from the identified proteins by in silico proteolysis using six proteases. A comparison of the numbers of proteins suitable for digestion with each enzyme and the iBAQ (intensity-based absolute quantification) values for these proteins revealed that bromelain and papain were the most suitable proteases for this sample. Next, the water solubility, toxicity, and ADMET (absorption/distribution/metabolism/excretion/toxicity) properties of these peptides were evaluated in silico. Finally, a novel ACE inhibitory peptide IEWEF with an IC50 value of 41.33 µM was identified. The activity of the synthesized peptide was verified in vitro, and it was shown to be a non-competitive ACE inhibitor. Molecular docking revealed that IEWEF could tightly bind to C-ACE, and N-ACE with energies less than 0 kJ mol−1, and the peptide IEWEF can form hydrogen bonds with C-ACE and N-ACE respectively. These results provide evidence that bioactive peptides in the water-soluble protein fraction account for (at least) some of the ACE inhibitory activities observed in Pelodiscus sinensis meat. Furthermore, our research provides a workflow for the efficient identification of novel ACE inhibitory peptides from complex protein mixtures.

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Screening, ACE-inhibitory mechanism and structure-activity relationship of a novel ACE-inhibitory peptide from Lepidium meyenii (Maca) protein hydrolysate

Cited by 18 publications

References 44 publications

Purification, Identification, and Inhibitory Mechanisms of a Novel ACE Inhibitory Peptide from Torreya grandis

Purification, Identification, and Inhibitory Mechanisms of a Novel ACE Inhibitory Peptide from Torreya grandis

A novel ACE inhibitory peptide from Pelodiscus sinensis Wiegmann meat

A novel ACE inhibitory peptide from Pelodiscus sinensis Wiegmann meat water-soluble protein hydrolysate

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