Identification and in silico characterization of a novel peptide inhibitor of angiotensin converting enzyme from pigeon pea ( Cajanus cajan )

Nawaz, Kiran; David, Swapna Merlin; Easwaran, Murugesh; Thandeeswaran, Murugesan; Kiran, Kalarikkal Gopikrishnan; Mahendran, Ratha; Palaniswamy, Muthusamy; Angayarkanni, Jayaraman

doi:10.1016/j.phymed.2017.09.013

Cited by 38 publications

(28 citation statements)

References 28 publications

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“…Competitive inhibitors can compete with the substrate for the catalytic site of the enzyme or can alter the conformation of the enzyme, ultimately inhibiting its activity [ 43 ]. In recent years, many competitive ACE inhibitory peptides have been reported, such as YQK (Tyr-Gln-Lys) from bovine casein [ 44 ], RYL (Arg-Tyr-Leu) from Silkworm Pupa [ 45 ], VVSLSIPR (Val-Val-Ser-Leu-Ser-Ile-Pro-Arg) from pigeon pea ( Cajanus cajan ) [ 46 ], and YLYELAR (Tyr-Leu-Tyr-Glu-Leu-Ala-Arg), AFPYYGHHLG (Ala-Phe-Pro-Tyr-Tyr-Gly-His-His-Leu-Gly) from scorpion ( Hemiscorpius lepturus ) venom. In addition, commercial functional foods or dietary supplements [ 16 , 17 ], as well as many antihypertensive drugs [ 47 ], have also been reported to be competitive inhibitors of ACE.…”

Section: Resultsmentioning

confidence: 99%

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Zhang

Luo

et al. 2018

Marine Drugs

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Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements.

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Section: Resultsmentioning

confidence: 99%

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Zhang

Luo

et al. 2018

Marine Drugs

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“…The ACE inhibitory activity of Ala-Gly-Pro-Pro-Gly-Ser-Asp-Gly-Gln-Pro-Gly-Ala-Lys (IC 50 = 420 ± 20 μM) was lower than that of Ala-Lys-Lys (IC 50 = 3.1 μM) [ 21 ], Trp-Leu-Ala-His-Lys (IC 50 = 77 μM) [ 26 ], and Leu-Ser-Lys (IC 50 = 34.7 μM) [ 27 ]. These differences indicated that the low molecular weight of peptide is also an important factor of its ACE inhibitory activity [ 28 ].…”

Section: Resultsmentioning

confidence: 99%

Processing Optimization and Characterization of Angiotensin-Ι-Converting Enzyme Inhibitory Peptides from Lizardfish (Synodus macrops) Scale Gelatin

et al. 2018

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Hypertension can cause coronary heart disease. Synthetic angiotensin-converting enzyme (ACE) inhibitors are effective antihypertensive drugs but often cause side effects. The aim of this study was to prepare potential ACE inhibitors from scales. Gelatin was extracted from lizardfish scales. Then, scale gelatin was enzymolyzed to prepare ACE inhibitory peptides using response surface methodology. Proteolytic conditions after optimization were as follows: pH 7.0, enzyme substrate ratio 3.2%, temperature 47 °C, and proteolysis lasting 2 h and 50 min. The experimental ACE inhibitory activity under optimal conditions was 86.0 ± 0.4%. Among the 118 peptides identified from gelatin hydrolysates, 87.3% were hydrophilic and 93.22% had a molecular weight <2000 Da. Gelatin peptides had high stability upon exposure to high temperature and pH as well as gastrointestinal tract enzymes. Gelatin peptides showed an antihypertensive effect in spontaneously hypertensive rats at a dosage of 2 g/kg in the long-term experiments. A new ACE inhibitory peptide was isolated from gelatin hydrolysates, and was identified as AGPPGSDGQPGAK with an IC50 value of 420 ± 20 μM. In this way, ACE inhibitory peptides derived from scale gelatin have the potential to be used as healthy ACE-inhibiting drug raw materials.

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“…A major challenge of the in silico approach is the dearth of in vitro analysis to confirm bioactivity (Agyei et al, ). Using the classic approach, recent studies reported that fermented/hydrolyzed pigeon pea seeds/flour have strong potential for exploration as antioxidative and antihypertensive food ingredients (Nawaz et al, ; Olagunju, Omoba, Enujingha, Alashi, & Aluko, ; Olagunju, Omoba, Enujingha, Alashi, & Aluko, ; Olagunju et al, ). The objectives for this study were to use the bioinformatics approach to assess the potential of nutrient reservoir (storage) proteins in pigeon pea as precursors of DPP‐4‐inhibiting peptides, and to evaluate the relationship between structural features of the proteins and biofunctional parameters of released peptides.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Boachie

Okoro²,

Imai

et al. 2019

J Food Biochem

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Abbreviations: ANS, 8-anilino-1-naphthalenesulphonic acid; BSA, bovine serum albumin; DPP-4, dipeptidyl peptidase-4; GIP, glucose-dependent insulinotropic polypeptide; GLP-1, glucagon-like peptide-1; GRAVY, grand average of hydropathicity; OPA, o-phthalaldehyde; pI, theoretical isoelectric point; RMSE, root mean square error; T2DM, type 2 diabetes mellitus; UPLC, ultra-performance liquid chromatography. AbstractIn silico and in vitro parameters were used to assess the potential of pigeon pea (Cajanus cajan) nutrient reservoir proteins as sources of dipeptidyl peptidase (DPP)-4 inhibitors. In silico, 40 pigeon pea proteins evaluated had 46% of amino acids associated with DPP-4 inhibition. After virtual hydrolysis, pepsin had the highest frequency of release and bioactivity of released DPP-4 inhibiting peptides, compared to papain and thermolysin. In vitro, thermolysin released the most active DPP-4 inhibitors.The protein hydrolysates contained similar amino acids but different particle sizes.Thus, the bioactivity patterns are attributable to the different nature and behavior of proteins/peptides under actual and virtual conditions. Using eight physicochemical variables, a random forest model with moderate prediction accuracy was developed for predicting DPP-4 inhibitory activity of papain hydrolysates. The findings demonstrate that proteins from pigeon pea are precursors of DPP-4 inhibitors, with potential use in formulating functional food for managing type 2 diabetes. | In silico analysis of physicochemical properties of pigeon pea proteinsPhysicochemical properties of the 40 mature pigeon pea proteins/ domains and BSA were calculated using the ProtParam feature of UniProtKB. The properties include the protein chain length, theoretical isoelectric point (pI), molecular weight, grand average of K E Y W O R D S bioactive peptides, bioinformatics, Cajanus cajan, dipeptidyl peptidase-4, in silico, pigeon pea S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Boachie RT, Okoro FL, Imai K, et al. Enzymatic release of dipeptidyl peptidase-4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments. J Food Biochem.

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Identification and in silico characterization of a novel peptide inhibitor of angiotensin converting enzyme from pigeon pea ( Cajanus cajan )

Cited by 38 publications

References 28 publications

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Processing Optimization and Characterization of Angiotensin-Ι-Converting Enzyme Inhibitory Peptides from Lizardfish (Synodus macrops) Scale Gelatin

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

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