Identification of a potent Angiotensin-I converting enzyme inhibitory peptide from Black cumin seed hydrolysate using orthogonal bioassay-guided fractionations coupled with in silico screening

Sutopo, Christoper Caesar Yudho; Sutrisno, Aji; Wang, Lifei; Hsu, Jue‐Liang

doi:10.1016/j.procbio.2020.02.010

Cited by 24 publications

(23 citation statements)

References 45 publications

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“…The purified peptide inhibited the enzyme activity by changing the conformation by which the enzyme could be well protected at both high and low concentrations of substrate. The inhibition modes of ACE inhibitory peptides include competitive, noncompetitive, and the mixed modes (Sutopo et al., 2020). In recent years, some noncompetitive biologically active peptides with ACEI activity were found in macroalga, for example, Gracilariopsis lemaneiformis (Deng et al., 2018).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Yang

Qin

2021

Journal of Food Science

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Hydrolysates containing angiotensin I‐converting enzyme (ACE)‐inhibitory peptide were prepared from protein of Alaska pollack skins using alcalase and trypsin. The protein hydrolysate was separated by ultrafiltration, Sephadex G‐25 gel filtration chromatography and reversed phase high‐performance liquid chromatography (HPLC), from which a novel purified peptide was obtained. Both random coil structure and β‐sheet in the purified peptide were revealed in Fourier transform infrared spectrum. The amino sequence of the purified peptide was identified as GPLGVP, VLYPVK, VFLENVLR, and FEEF by HPLC‐Q‐TOF‐MS (HPLC‐quadrupole time‐of‐flight mass spectrometry). The peptide GPLGVP whose molecular weight was 538.31 Da showed the highest ACE inhibitory activity (IC50 = 105.8 µM). The purified peptide featured a noncompetitive inhibition kinetic mechanism was shown in the Lineweaver–Burk plots and was susceptible to enzymes as indicated in the studies on stability of gastrointestinal proteases. Moreover, the peptide GPLGVP can combine ACE catalytic pocket through hydrogen bonds and other forces with high binding power as disclosed in molecular docking simulation, which provides the inhibitory effect of GPLGVP on ACE.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Yang

Qin

2021

Journal of Food Science

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“…Therefore, a vital step in studying bioactive peptides is to know how to make them more efficiently accessible, thereby reducing researching time and finances to screen and eliminate inferior peptides. According to the different characters of each peptide such as the molecular weight, hydrophobicity, and other physicochemical properties, several orthogonal bioassay-guided methods were applied individually as well as the combination of two or three chromatography techniques which were utilized [ 4 , 26 , 27 , 28 , 29 ]. To fractionate SSTY GI hydrolysates, two column chromatography methods (RP and SCX) with different separation mechanisms were performed in parallel.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study

et al. 2020

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Five novel peptides (LPLF, WLQL, LPSW, VPGLAL, and LVGLPL) bearing dipeptidyl peptidase IV (DPP-IV) inhibitory activities were identified from the gastrointestinal enzymatic hydrolysate of soft-shelled turtle yolk (SSTY) proteins. Peptides were isolated separately using reversed-phase (RP) chromatography in parallel with off-line strong cation exchange (SCX) chromatography followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis to determine sequences. Among these peptides, LPSW showed the highest DPP-IV inhibitory activity with an IC50 value of 269.7 ± 15.91 µM. The results of the pre-incubation experiment and the kinetic study of these peptides indicated that WLQL is a true inhibitor and its inhibition toward DPP-IV is of an uncompetitive model, while LPLF, LPSW, and VPGLAL are real-substrates and competitive inhibitors against DPP-IV. The DPP-IV inhibitory peptides derived from SSTY hydrolysate in study are promising in the management of hyperglycemia in Type 2 diabetes.

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“…Although the term "fragmentomics" is not widely used in publications, it represents one of the common contemporary strategies of research on bioactive peptides. Recent applications of fragmentomics concerning the bioactivity of peptides derived from various food sources have been described by Sutopo et al [41], Alcaide-Hidalgo et al [42], and Kinariwala et al [43].…”

Section: Discussionmentioning

confidence: 99%

Soybean (Glycine max) Protein Hydrolysates as Sources of Peptide Bitter-Tasting Indicators: An Analysis Based on Hybrid and Fragmentomic Approaches

et al. 2020

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The aim of this study was to analyze soybean proteins as sources of peptides likely to be bitter using fragmentomic and hybrid approaches involving in silico and in vitro studies. The bitterness of peptides (called parent peptides) was theoretically estimated based on the presence of bitter-tasting motifs, particularly those defined as bitter-tasting indicators. They were selected based on previously published multilinear stepwise regression results. Bioinformatic-assisted analyses covered the hydrolysis of five major soybean-originating protein sequences using bromelain, ficin, papain, and proteinase K. Verification of the results in experimental conditions included soy protein concentrate (SPC) hydrolysis, RP-HPLC (for monitoring the proteolysis), and identification of peptides using RP-HPLC-MS/MS. Discrepancies between in silico and in vitro results were observed when identifying parent peptide SPC hydrolysate samples. However, both analyses revealed that conglycinins were the most abundant sources of parent peptides likely to taste bitter. The compatibility percentage of the in silico and in vitro results was 3%. Nine parent peptides with the following sequences were identified in SPC hydrolysates: LSVISPK, DVLVIPLG, LIVILNG, NPFLFG, ISSTIV, PQMIIV, PFPSIL, DDFFL, and FFEITPEK (indicators are in bold). The fragmentomic idea of research might provide a supportive method for predicting the bitterness of hydrolysates. However, this statement needs to be confirmed experimentally.

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Identification of a potent Angiotensin-I converting enzyme inhibitory peptide from Black cumin seed hydrolysate using orthogonal bioassay-guided fractionations coupled with in silico screening

Cited by 24 publications

References 45 publications

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Purification and characterization of a novel angiotensin I‐converting enzyme‐inhibitory peptide derived from Alaska pollack skins

Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study

Soybean (Glycine max) Protein Hydrolysates as Sources of Peptide Bitter-Tasting Indicators: An Analysis Based on Hybrid and Fragmentomic Approaches

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