Identification and molecular docking of antioxidant peptides from hemp seed protein hydrolysates

Gao, Jingxin; Li, Tiange; Chen, Duoduo; Gu, Haofeng; Mao, Xueying

doi:10.1016/j.lwt.2021.111453

Cited by 53 publications

(32 citation statements)

References 38 publications

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“…Plant proteins are the essential source of bioactive peptides, their hydrolysates possess various biological activities, such as antioxidant, anticancer, ACE-inhibitory, and antimicrobial. − Several studies have focused on the antimicrobial effect of M. oleifera components, such as oil from M.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus

Zhao

Wang

et al. 2022

J. Agric. Food Chem.

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The present study sought to identify and characterize a novel antimicrobial peptide, named MOp2 from Moringa oleifera seed protein hydrolysates, and elucidate its potential antimicrobial effects on Staphylococcus aureus. MOp2, with the amino acid sequence of His−Val−Leu−Asp−Thr−Pro−Leu−Leu (HVLDTPLL), was characterized as a hydrophobic anionic AMP of the β-sheet structure. MOp2 exhibited negligible hemolytic activity at 2.0× MIC, suggesting its inhibitory effect on the growth of S. aureus (MIC: 2.204 mM). It maintained more than 90% of antimicrobial activity under 5% salt and about 78% of antimicrobial activity at a high temperature of 115 °C for 30 min. Protease, especially acid protease, reduced its antimicrobial activity to different extents. Moreover, MOp2 caused irreversible membrane damage to S. aureus cells by increasing the membrane permeability, resulting in the release of intracellular nucleotide pools. Additionally, molecular docking revealed that MOp2 could inhibit S. aureus growth by interacting with dihydrofolate reductase and DNA gyrase through hydrogen bonding and hydrophobic interactions. Overall, MOp2 could be a potential novel antimicrobial agent against S. aureus in food processing.

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Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus

Zhao

Wang

et al. 2022

J. Agric. Food Chem.

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“…It has been reported that electron transfer (ET) is the main mechanism of ABTS + scavenging, which changes the oxidation state of substances through electron movement between peptides and free radicals [ 54 ]. Gly residues located on the side chain can be neutralized by free radicals; this is achieved through donating protons due to the presence of individual hydrogen atoms [ 55 ]. The P1 obtained in this study had excellent antioxidant capacity, and this was due to the Gly residue at the N-terminus, which formed a hydrogen bond with the ligand ABTS.…”

Section: Resultsmentioning

confidence: 99%

Identification of Antioxidant Peptides Derived from Tilapia (Oreochromis niloticus) Skin and Their Mechanism of Action by Molecular Docking

Zhang

Liu

et al. 2022

Foods

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Antioxidants, which can activate the body’s antioxidant defence system and reduce oxidative stress damage, are important for maintaining free radical homeostasis between oxidative damage and antioxidant defence. Six antioxidant peptides (P1–P6) were isolated and identified from the enzymatic hydrolysate of tilapia skin by ultrafiltration, reversed-phase high-performance liquid chromatography (RP-HPLC) and liquid chromatography–tandem mass spectrometry (LC–MS/MS). Moreover, the scavenging mechanism of the identified peptides against DPPH (2,2-Diphenyl-1-picrylhydrazyl) and ABTS (2-azido-bis (3-ethylbenzothiazoline-6-sulfonic acid) was studied by molecular docking. It was found that Pro, Ala and Tyr were the characteristic amino acids for scavenging free radicals, and hydrogen bonding and hydrophobic interactions were the main interactions between the free radicals and antioxidant peptides. Among them, the peptide KAPDPGPGPM exhibited the highest DPPH free radical scavenging activity (IC50 = 2.56 ± 0.15 mg/mL), in which the hydrogen bond between the free radical DDPH and Thr-6 was identified as the main interaction, and the hydrophobic interactions between the free radical DDPH and Ala, Gly and Pro were also identified. The peptide GGYDEY presented the highest scavenging activity against ABTS (IC50 = 9.14 ± 0.08 mg/mL). The key structures for the interaction of this peptide with the free radical ABTS were identified as Gly-1 and Glu-5 (hydrogen bond sites), and the amino acids Tyr and Asp provided hydrophobic interactions. Furthermore, it was determined that the screened peptides are suitable for applications as antioxidants in the food industry, exhibit good water solubility and stability, are likely nonallergenic and are nontoxic. In summary, the results of this study provide a theoretical structural basis for examining the mechanism of action of antioxidant peptides and the application of enzymatic hydrolysates from tilapia skin.

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“…On the other hand, allergenic effect characteristics showed that most peptides can also cause allergenic effects. In silico toxicity and physicochemical predictions not only save time and money, but also facilitate the design of better therapeutic peptides, with low toxicity without compromising functionality [ 33 , 34 ]. Based on the result shown in Table 4 , all the peptides derived from glycinin and conglycinin are not toxic.…”

Section: Resultsmentioning

confidence: 99%

“…The primary enzyme responsible for the production of ROS in vivo is MPO because heme peroxidase is known to occur in neutrophils and monocytes [ 34 ] MPO can produce highly active ROS (like HOCl) under peroxide H 2 O 2 and halide conditions, leading to cell and tissue damage [ 34 ]. Consequently, molecular docking was performed to assess whether the various peptides were effective.…”

Section: Resultsmentioning

confidence: 99%

In Silico Approach of Glycinin and Conglycinin Chains of Soybean By-Product (Okara) Using Papain and Bromelain

et al. 2022

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This study explores utilization of a sustainable soybean by-product (okara) based on in silico approach. In silico approaches, as well as the BIOPEP database, PeptideRanker database, Peptide Calculator database (Pepcalc), ToxinPred database, and AllerTop database, were employed to evaluate the potential of glycinin and conglycinin derived peptides as a potential source of bioactive peptides. These major protein precursors have been found as protein in okara as a soybean by-product. Furthermore, primary structure, biological potential, and physicochemical, sensory, and allergenic characteristics of the theoretically released antioxidant peptides were predicted in this research. Glycinin and α subunits of β-conglycinin were selected as potential precursors of bioactive peptides based on in silico analysis. The most notable among these are antioxidant peptides. First, the potential of protein precursors for releasing bioactive peptides was evaluated by determining the frequency of occurrence of fragments with a given activity. Through the BIOPEP database analysis, there are several antioxidant bioactive peptides in glycinin and β and α subunits of β-conglycinin sequences. Then, an in silico proteolysis using selected enzymes (papain, bromelain) to obtain antioxidant peptides was investigated and then analyzed using PeptideRanker and Pepcalc. Allergenic analysis using the AllerTop revealed that all in silico proteolysis-derived antioxidant peptides are probably nonallergenic peptides. We also performed molecular docking against MPO (myeloperoxidases) for this peptide. Overall, the present study highlights that glycinin and β and α subunits of β-conglycinin could be promising precursors of bioactive peptides that have an antioxidant peptide for developing several applications.

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Identification and molecular docking of antioxidant peptides from hemp seed protein hydrolysates

Cited by 53 publications

References 38 publications

Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus

Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus

Identification of Antioxidant Peptides Derived from Tilapia (Oreochromis niloticus) Skin and Their Mechanism of Action by Molecular Docking

In Silico Approach of Glycinin and Conglycinin Chains of Soybean By-Product (Okara) Using Papain and Bromelain

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