Characterization of peptides from common bean protein isolates and their potential to inhibit markers of type‐2 diabetes, hypertension and oxidative stress

Mojica, Luis; Luna‐Vital, Diego A.; Mejı́a, Elvira González de

doi:10.1002/jsfa.8053

Cited by 90 publications

(73 citation statements)

References 44 publications

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“…The antioxidant activity was also observed in peptides with less than 20 amino acid residues per molecule, because these small peptides have a better ability to cross the intestinal barrier and exert their biological effects . Finally, peptides with hydrophobicity ≤20 kcal mol −1 are more effective for penetrating the cell membrane and to exercise effects on the molecule . Interestingly, most of the peptides found in DTP and digested protein fractions from chia seed showed these characteristics, which may explain the benefits found in the present study.…”

Section: Discussionmentioning

confidence: 50%

“…[53] Finally, peptides with hydrophobicity ࣘ20 kcal mol −1 are more effective for penetrating the cell membrane and to exercise effects on the molecule. [54] Interestingly, most of the peptides found in DTP and digested protein fractions from chia seed showed these characteristics, [14,32] which may explain the benefits found in the present study.…”

Section: Discussionmentioning

confidence: 58%

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Chia (Salvia hispanica L.) Seed Total Protein and Protein Fractions Digests Reduce Biomarkers of Inflammation and Atherosclerosis in Macrophages In Vitro

Grancieri

Martino

Mejía

2019

Molecular Nutrition Food Res

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Scope The objectives are to evaluate the anti‐inflammatory and anti‐atherosclerotic effects of digested total protein and digested protein fractions from chia seed in macrophages in vitro. Methods and results Total protein and protein fractions (albumin, globulin, glutelin, and prolamin) are isolated from chia seed and digested using simulated gastrointestinal conditions, resulting in digested total protein (DTP) and digested protein fractions (DPF). DTP and DPF are applied (1.0 mg mL−1) in RAW 264.4 macrophages stimulated with LPS (1 µg mL−1) for inflammation or ox‐LDL (80 µg mL−1) for atherosclerosis. In the inflammatory process, DTP and DPF reduce p‐NF‐κB, iNOS, p‐JNK, and AP‐1. Digested glutelin reduces the secretion of nitric oxide (65.1%), reactive oxygen species (19.7%), prostaglandins (34.6%), TNF‐α (24.1%), MCP‐1 (18.9%), IL‐6 (39.6%), and IL‐10 (68.7%). DTP and DPF reduce the NF‐κB translocation to nuclei. DTP and digested glutelin reduce iCAM expression (86.4%, 80.8%), LOX‐1 (37.3%, 35.7%), iNOS (67.0%, 42.2%), and NF‐κB (57.5%, 71.1%). DTP is effective in reducing secretion of nitric oxide (43.4%), lipid accumulation (41.9%), prostaglandins (41.9%), TNF‐α (43.3%), MCP‐1 (47.6%), and IL‐6 (50.5%). Peptides from chia DTP and DPF are also characterized. Conclusion DTP and digested glutelin from chia seed reduce expression and secretion of markers related to inflammation and atherosclerosis pathways.

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Section: Discussionmentioning

confidence: 50%

Section: Discussionmentioning

confidence: 58%

Chia (Salvia hispanica L.) Seed Total Protein and Protein Fractions Digests Reduce Biomarkers of Inflammation and Atherosclerosis in Macrophages In Vitro

Grancieri

Martino

Mejía

2019

Molecular Nutrition Food Res

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“…Due to the enzyme's central role in regulating postprandial glucose release, α-glucosidase inhibitors have been developed for type 2 diabetes management. The presence of hydrophobic amino acids Pro, Met and Ala, close to the C-terminal of the peptide, was observed to contribute in promoting the inhibitory activity (Kang et al, 2013;Mojica et al, 2017). Molecular docking studies also revealed that hydrophobic amino acid residues of peptides predominantly interact with residues in the active site of α-glucosidase (Mojica and de Mejía, 2016;Di Stefano et al, 2018).…”

Section: Alpha-glucosidase Inhibitionmentioning

confidence: 99%

Role of hydrophobicity in food peptide functionality and bioactivity

Acquah¹,

Stefano²,

Udenigwe³

2018

Journal of Food Bioactives

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Peptides are important compounds used in the development of functional biomaterials, functional foods and nutraceuticals. The functional and bioactive properties of peptides are directly linked to their structural features, including molecular size, presence or absence of charges, amino acid sequence, hydrophobicity, and hydrophilicity. The role of peptide structures in their bioactivities and functionalities is still emerging. Some bioactive peptides have undesirable taste, which can influence consumer interests in novel peptide-based food applications. In this review, we discussed the role of peptide hydrophobicity in their bioavailability, bioactivity, bitterness property, emulsion stability, aggregation and self-assembly for application in novel food formulations and nutraceutical/ drug delivery.

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“…Therefore, besides attempting to increase the potency of food protein hydrolysates/peptides, the search for peptides having multiple bioactivities is of particular interest. In this context, hydrolysates and peptides displaying a range of in vitro bioactivities including other antidiabetic (e.g., α‐glucosidase inhibition), antioxidant, and antihypertensive effects have been described in the literature (Connolly, Piggott, & FitzGerald, ; Harnedy & FitzGerald, ; Lacroix, Meng, Cheung, & Li‐Chan, ; Mojica, Luna‐Vital, & González de Mejía, ; Neves, Harnedy, & FitzGerald, ; Nongonierma & FitzGerald, ; T.‐Y. Wang, Hsieh, et al, ; C. Zhang, Zhang, Wang, Chen, & Luo, ). Potent DPP‐IV inhibitory peptides have been identified in several food protein‐derived hydrolysates.…”

Section: Future Directionsmentioning

confidence: 99%

Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins

2017

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Dipeptidyl peptidase IV (DPP-IV) is involved in incretin hormone processing and therefore plays a key role in glycemic regulation. This review summarizes the latest developments in food proteinderived DPP-IV inhibitory peptides. The in silico approaches currently used to develop targeted strategies for the enzymatic release of DPP-IV inhibitory peptides from food proteins are outlined.The features within the primary sequences of potent DPP-IV inhibitory di-, tri-, and larger peptides, having half maximal inhibitory activity (IC 50 ) < 100 mM, were evaluated and the outcomes are presented herein. It is proposed that detailed analysis of those food derived peptides identified in humans following ingestion may constitute a practical strategy for the targeted identification of novel bioavailable DPP-IV inhibitory peptides. Human intervention studies are required as the specific role of food protein-derived DPP-IV inhibitory peptides in the regulation of glycaemia in humans remains to be fully elucidated.

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Characterization of peptides from common bean protein isolates and their potential to inhibit markers of type‐2 diabetes, hypertension and oxidative stress

Abstract: Peptides from common bean have antidiabetic and antihypertensive potential regardless of their antioxidant capacity. © 2016 Society of Chemical Industry.

Cited by 90 publications

References 44 publications

Chia (Salvia hispanica L.) Seed Total Protein and Protein Fractions Digests Reduce Biomarkers of Inflammation and Atherosclerosis in Macrophages In Vitro

Chia (Salvia hispanica L.) Seed Total Protein and Protein Fractions Digests Reduce Biomarkers of Inflammation and Atherosclerosis in Macrophages In Vitro

Role of hydrophobicity in food peptide functionality and bioactivity

Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins

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