Identification, protein antiglycation, antioxidant, antiproliferative, and molecular docking of novel bioactive peptides produced from hydrolysis of
            Lens culinaris

In addition to their nutritional and physiological role, proteins are recognized as the major compounds responsible for the rheological properties of food products and their stability during manufacture and storage. Furthermore, proteins have been shown to be source of bioactive peptides able to exert beneficial effects on human health. In recent years, scholarly interest has focused on the incorporation of high-quality proteins into the diet. This fact, together with the new trends of consumers directed to avoid the intake of animal proteins, has boosted the search for novel and sustainable protein sources and the development of suitable, cost-affordable, and environmentally friendly technologies to extract high concentrations of valuable proteins incorporated into food products and supplements. In this review, current data on emergent and promising methodologies applied for the extraction of proteins from natural sources are summarized. Moreover, the advantages and disadvantages of these novel methods, compared with conventional methods, are detailed. Additionally, this work describes the combination of these technologies with the enzymatic hydrolysis of extracted proteins as a powerful strategy for releasing bioactive peptides.

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Functionalized Oxoindolin Hydrazine Carbothioamide Derivatives as Highly Potent Inhibitors of Nucleoside Triphosphate Diphosphohydrolases

Frontiers in Pharmacology ◽

10.3389/fphar.2020.585876 ◽

2020 ◽

Vol 11 ◽

Author(s):

Saira Afzal ◽

Mariya al-Rashida ◽

Abdul Hameed ◽

Julie Pelletier ◽

Jean Sévigny ◽

...

Keyword(s):

Gene Expression ◽

Insulin Secretion ◽

Molecular Docking ◽

Docking Studies ◽

Nucleoside Triphosphate ◽

Membrane Bound ◽

Hydrolysis Of ◽

Extracellular Environment ◽

Micromolar Range

Ectonucleoside triphosphate diphosphohydrolases (NTPDases) are ectoenzymes that play an important role in the hydrolysis of nucleoside triphosphate and diphosphate to nucleoside monophosphate. NTPDase1, -2, -3 and -8 are the membrane bound members of this enzyme family that are responsible for regulating the levels of nucleotides in extracellular environment. However, the pathophysiological functions of these enzymes are not fully understood due to lack of potent and selective NTPDase inhibitors. Herein, a series of oxoindolin hydrazine carbothioamide derivatives is synthesized and screened for NTPDase inhibitory activity. Four compounds were identified as selective inhibitors of h-NTPDase1 having IC50 values in lower micromolar range, these include compounds 8b (IC50 = 0.29 ± 0.02 µM), 8e (IC50 = 0.15 ± 0.009 µM), 8f (IC50 = 0.24 ± 0.01 µM) and 8l (IC50 = 0.30 ± 0.03 µM). Similarly, compound 8k (IC50 = 0.16 ± 0.01 µM) was found to be a selective h-NTPDase2 inhibitor. In case of h-NTPDase3, most potent inhibitors were compounds 8c (IC50 = 0.19 ± 0.02 µM) and 8m (IC50 = 0.38 ± 0.03 µM). Since NTPDase3 has been reported to be associated with the regulation of insulin secretion, we evaluated our synthesized NTPDase3 inhibitors for their ability to stimulate insulin secretion in isolated mice islets. Promising results were obtained showing that compound 8m potently stimulated insulin secretion without affecting the NTPDase3 gene expression. Molecular docking studies of the most potent compounds were also carried out to rationalize binding site interactions. Hence, these compounds are useful tools to study the role of NTPDase3 in insulin secretion.

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Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

Molecules ◽

10.3390/molecules24244562 ◽

2019 ◽

Vol 24 (24) ◽

pp. 4562 ◽

Cited By ~ 3

Author(s):

Yajun Zheng ◽

Xian Wang ◽

Yongliang Zhuang ◽

Yan Li ◽

Hailong Tian ◽

...

Keyword(s):

Liquid Chromatography ◽

Molecular Docking ◽

In Silico ◽

Bioactive Peptides ◽

Docking Simulation ◽

Reversed Phase ◽

Scavenging Activity ◽

Antioxidant Peptides ◽

Ace Inhibitory

Albumin is the major fraction of quinoa protein that is characterized as having high nutritional value. However, until now, scant information is available on the bioactivity of quinoa albumin or its hydrolysates. To promote its usage, we extracted albumin in this study from quinoa bran assisted with cellulase and hemicellulose, and hydrolyzed it by alcalase and trypsin to produce bioactive peptides. The hydrolysates (QBAH) were purified by gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC), followed by identification using liquid chromatography–mass spectrometry (LC-MS/MS). Furthermore, based on in silico analysis, one angiotensin-I converting enzyme (ACE)-inhibitory and antioxidant peptide, RGQVIYVL (946.6 Da), and two antioxidant peptides, ASPKPSSA (743.8 Da), and QFLLAGR (803.5 Da), from QBAH were synthesized. RGQVIYVL showed a high ACE-inhibitory activity (IC50 = 38.16 μM) with competitive mode of inhibition, and showed significant antihypertensive effect in spontaneously hypertensive rats at a concentration of 100–150 mg/kg body weight (bw). Molecular docking simulation showed that it could interact with the active ACE site via hydrogen bonds with high binding power. Moreover, RGQVIYVL, ASPKPSSA, and QFLLAGR all demonstrated high ·OH scavenging activity (IC50 = 61.69–117.46 μM), ABTS+ scavenging activity (58.29–74.28%) and Fe2+ chelating ability (32.54–82.48% at 0.5 mg/mL). They could also retain activity after gastrointestinal enzyme digestion. These results indicate that quinoa albumin is a potential source of bioactive peptides possessing antioxidant and ACE-inhibitory activities.

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Identification, protein antiglycation, antioxidant, antiproliferative, and molecular docking of novel bioactive peptides produced from hydrolysis of Lens culinaris

Simultaneous hydrolysis of proteins from different sources to enhance their antibacterial properties through the synergistic action of bioactive peptides

A strategy based on gene sequencing and molecular docking for analysis and prediction of bioactive peptides in Shuxuetong injection

Characterization of bioactive peptides produced from green lentil ( Lens culinaris ) seed protein concentrate using Alcalase and Flavourzyme in single and sequential hydrolysis

Hydrolysis of whey protein as a useful approach to obtain bioactive peptides and a β-Lg fraction with different biotechnological applications

ISOLATION AND IN VITRO HYDROLYSIS OF GLOBULIN G1 FROM LENTILS (LENS CULINARIS, MEDIK)

Determination of reaction kinetics of hydrolysis of tilapia (Oreochromis niloticus) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin-I-converting enzyme inhibitory activity and Ca-binding properties

Hydrolysis of milk-derived bioactive peptides by cell-associated extracellular peptidases of Streptococcus thermophilus

A Review on the Extraction and Processing of Natural Source-Derived Proteins through Eco-Innovative Approaches

Functionalized Oxoindolin Hydrazine Carbothioamide Derivatives as Highly Potent Inhibitors of Nucleoside Triphosphate Diphosphohydrolases

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking