Purification, molecular docking and in vivo analyses of novel angiotensin-converting enzyme inhibitory peptides from protein hydrolysate of moth bean (Vigna aconitifolia (Jacq.) Màrechal) seeds

Bhadkaria, Amita; Narvekar, Dakshita Tanaji; Sah, Sangeeta Pilkwal; Bhagyawant, Sameer Suresh

doi:10.1016/j.ijbiomac.2023.123138

Cited by 16 publications

(9 citation statements)

References 52 publications

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“…Thrombus is one of the most common clinical symptoms in cardiovascular and cerebrovascular In this study, the anticoagulant peptide P9 was puri ed and characterized for the rst time from ESW and its anticoagulant effect was demonstrated in in vitro and in vivo experiments (Fu et al 2022). Our isolation process showed that fractions with smaller molecular weights had better anticoagulant activity, which could be attributed to the fact that low molecular weight peptides are more likely to bind to target molecules as compared to high molecular weight peptides, and hence they exhibit higher anticoagulant activity (Bhadkaria et al 2023). According to sequence analysis, in silico analysis and molecular docking, a P9 (HTWNLHWWR) with a mass of 1335.5 Da binds to the catalytic luminal active site of thrombin via van der Waals forces, hydrogen bonding, alkyl bonding, and pi-alkyl bonding (Fig.…”

Section: Discussionmentioning

confidence: 87%

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

Li,

Zhuang,

et al. 2024

Int J Pept Res Ther

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Eupolyphaga sinensis Walker (ESW), an animal drug in traditional Chinese medicine, has been used clinically for thousands of years for cardiovascular disease and osteoarthritis. Many studies of ESW have reported that it had have anti-in ammatory and anti-tumor activities due to the small-molecule ingredients. However, large-molecule compounds of ESW representing signi cant pharmacological effects such as anti-thrombotic, anti-cancer, and anti-in ammatory have not been revealed yet. Here, a novel anticoagulant peptide (P9) containing 9 amino acids was isolated from the hydrolysate of aqueous extracts of ESW. Further, P9 synthesized by solid-phase synthesis was able to prolong APTT and TT and bind to thrombin in a mixed mode. Molecular docking and spectroscopy demonstrated that P9 was able to inhibit thrombin activity by binding to the active site of thrombin and altering the secondary structure of thrombin. In an in vivo study, P9 was able to reduce the intensity of Phenylhydrazine (PHZ)-induced cardiac staining in thrombosed zebra sh with antithrombotic activity. The results suggest that peptides originated from ESW hydrolysates could exert an anticoagulant effect, which is likely to be a potential source of bioactive peptides with anticoagulant activity.

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Section: Discussionmentioning

confidence: 87%

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

Li,

Zhuang,

et al. 2024

Int J Pept Res Ther

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“…The inhibitory activity of ACE-inhibitory peptides in hydrolysates has been reported to be related to their molecular weights [ 22 ]. The inhibitory effects of the LC P digest and different molecular weight fractions on ACE are shown in Figure 1 .…”

Section: Resultsmentioning

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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“…Peptide profiling identification [ 7 , 9 , 10 , 11 ], toxicological prediction [ 12 , 13 ], and molecular docking [ 7 , 9 , 11 , 12 , 13 , 14 , 15 , 16 , 17 ] are effective means to obtain peptides with high ACE-inhibitory activity in vitro rapidly. Researchers have reported a variety of food-derived ACE-inhibitory peptides from animal protein sources such as dairy products [ 9 ] and seafood [ 7 , 12 , 16 , 18 , 19 ], as well as from soy products [ 14 , 20 ], high-quality crops or low-value plant protein [ 15 , 21 , 22 , 23 , 24 ]. The varied sequences of amino acids in peptides have increased the diversity of food-derived peptides.…”

Section: Discussionmentioning

confidence: 99%

“…Food-derived ACE-inhibitory peptides were mainly water-soluble and non-toxic. Their inhibited mechanism often includes mixed or competitive mode, binding to ACE’s active or inactive sites through hydrogen bonds, electrostatic interactions, and hydrophobic interactions [ 12 , 13 , 14 , 15 , 16 , 25 ]. The 27 undecapeptides could inhibit ACE activity in a mixed mode by forming hydrogen bonds and electrostatic interaction forces with amino acid residues in the active and inactive sites of the ACE receptor.…”

Section: Discussionmentioning

confidence: 99%

“…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%

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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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Purification, molecular docking and in vivo analyses of novel angiotensin-converting enzyme inhibitory peptides from protein hydrolysate of moth bean (Vigna aconitifolia (Jacq.) Màrechal) seeds

Cited by 16 publications

References 52 publications

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

Purification and Characterization of a Novel Anticoagulant Peptide from Protein Hydrolysate of Eupolyphaga sinensis Walker

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

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

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