<i>In vitro</i> antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

Aiemratchanee, Panida; Panyawechamontri, Kulachatr; Phaophu, Phutthaphorn; Reamtong, Onrapak; Panbangred, Watanalai

doi:10.1111/ijfs.14853

Cited by 15 publications

(6 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Aliphatic amino acids (Leu and Ile) were frequently found in the N-terminus of ACE inhibitory peptides, such as peptides from soy protein (LIVTQ and LIVT) and Volutharpa ampullacea perryi (IVTNWDDMEK) . Positively charged amino acids (His) were reported to be a critical residue in the C-terminus tripeptide position of ACE inhibitory peptides, such as fermented milk (LVYPFPGPIH), Tenebrio molitor (YDDGSYKPH), horse gram flour (VTSTGPVGH), and porcine plasma proteins (YTFPFH) . Some studies found that the bulky hydrophobic amino acids with cyclic or aromatic structures at the C-terminus of the peptides show significant ACE inhibitory activity .…”

Section: Discussionmentioning

confidence: 99%

“…32 Positively charged amino acids (His) were reported to be a critical residue in the C-terminus tripeptide position of ACE inhibitory peptides, 48 such as fermented milk (LVYPFPGPIH), 49 Tenebrio molitor (YDDG-SYKPH), 50 horse gram flour (VTSTGPVGH), 50 and porcine plasma proteins (YTFPFH). 51 Some studies found that the bulky hydrophobic amino acids with cyclic or aromatic structures at the C-terminus of the peptides show significant ACE inhibitory activity. 52 Peptides P3 and P12 consist of the aromatic amino acid Tyr (Y), the aliphatic amino Gly (G), and the positively charged and aromatic amino acid His (H) at the C-terminus of the peptide.…”

Section: ■ Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

Zou

Zhou

et al. 2023

J. Agric. Food Chem.

View full text Add to dashboard Cite

This study aimed to identify angiotensin I-converting enzyme (ACE) from in vitro digestion products of pork sausage with partial substitution of NaCl by KCl (PSRK). Peptides from in vitro digestion products of PSRK were identified through liquid chromatography with tandem mass spectrometry analysis coupled with de novo sequencing. Subsequently, the ACE inhibitory peptides LIVGFPAYGH and IVGFPAYGH were screened based on PeptideRanker, in silico absorption, molecular docking, and the determination of ACE inhibitory activity. In addition, the ACE inhibitory peptides LIVGFPAYGH and IVGFPAYGH were mixedtype inhibitors; these peptides' ACE inhibitory activities were expressed as the 50% inhibitory concentration (IC 50 ) values in vitro, which were 196.16 and 150.88 μM, respectively. After 2 h of incubation, LIVGFPAYGH and IVGFPAYGH could be transported through Caco-2 cell monolayers with paracellular passive diffusion. Furthermore, LIVGFPAYGH and IVGFPAYGH significantly increased the levels of ACE2 and nitric oxide while decreasing the levels of ACE, angiotensin II, and endothelin-1 in Ang I-treated human umbilical vein endothelial cells, indicating the ACE inhibitory effect of LIVGFPAYGH and IVGFPAYGH. In summary, LIVGFPAYGH and IVGFPAYGH from PSRK can be used as functional foods with antihypertensive activity.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: ■ Discussionmentioning

confidence: 99%

Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

Zou

Zhou

et al. 2023

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Therefore, bone and bone‐associated protein‐containing tissues demonstrate considerable potentials as sources for the preparation of calcium‐chelating peptides. Similarly, animal blood is rich in plasma proteins, which are also excellent sources of peptides (Aiemratchanee et al., 2020). Iron is a significant component that plays a role in both the structural properties and functionality of hemoglobin.…”

Section: Sources and Preparations Of Food‐derived Mcpsmentioning

confidence: 99%

A critical review of a typical research system for food‐derived metal‐chelating peptides: Production, characterization, identification, digestion, and absorption

Yu,

Liu,

Zhou

2023

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

In the past decade, food‐derived metal‐chelating peptides (MCPs) have attracted significant attention from researchers working towards the prevention of metal (viz., iron, zinc, and calcium) deficiency phenomenon by primarily inhibiting the precipitation of metals caused by the gastrointestinal environment and exogenous substances (including phytic and oxalic acids). However, for the improvement of limits of current knowledge foundations and future investigation directions of MCP or their derivatives, several review categories should be improved and emphasized. The species’ uniqueness and differences in MCP productions highly contribute to the different values of chelating ability with particular metal ions, whereas comprehensive reviews of chelation characterization determined by various kinds of technique support different horizons for explaining the chelation and offer options for the selection of characterization methods. The reviews of chelation mechanism clearly demonstrate the involvement of potential groups and atoms in chelating metal ions. The discussions of digestive stability and absorption in various kinds of absorption model in vitro and in vivo as well as the theory of involved cellular absorption channels and pathways are systematically reviewed and highlighted compared with previous reports as well. Meanwhile, the chelation mechanism on the molecular docking level, the binding mechanism in amino acid identification level, the utilizations of everted rat gut sac model for absorption, and the involvement of cellular absorption channels and pathway are strongly recommended as novelty in this review. This review makes a novel contribution to the literature by the comprehensive prospects for the research and development of food‐derived mineral supplements.

show abstract

“…Furthermore, Aiemratchanee et al. (2021) isolated novel BAPs with antihypertensive characteristics from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of swine blood. The IC 50 values of three peptides possessing the highest ACE‐inhibitory activity from RBCs, comprising RBC 7 (TPYPCV), RBC9 (FLCT), and RBC15 (VVYPWR), were 2.58 ± 0.87, 6.53 ± 0.34, and 5.22 ± 2.56 μM, respectively.…”

Section: Health‐promoting Effects Of Food Bapsmentioning

confidence: 99%

An updated review on food‐derived bioactive peptides: Focus on the regulatory requirements, safety, and bioavailability

Patil

Usman

Zhang

et al. 2022

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

Food‐derived bioactive peptides (BAPs) are recently utilized as functional food raw materials owing to their potential health benefits. Although there is a huge amount of scientific research about BAPs’ identification, purification, characterization, and physiological functions, and subsequently, many BAPs have been marketed, there is a paucity of review on the regulatory requirements, bioavailability, and safety of BAPs. Thus, this review focuses on the toxic peptides that could arise from their primary proteins throughout protein extraction, protein pretreatment, and BAPs’ formulation. Also, the influences of BAPs’ length and administration dosage on safety are summarized. Lastly, the challenges and possibilities in BAPs’ bioavailability and regulatory requirements in different countries were also presented. Results revealed that the human studies of BAPs are essential for approvals as healthy food and to prevent the consumers from misinformation and false promises. The BAPs that escape the gastrointestinal tract epithelium and move to the stomach are considered good peptides and get circulated into the blood using different pathways. In addition, the hydrophobicity, net charge, molecular size, length, amino acids composition/sequences, and structural characteristics of BAPs are critical for bioavailability, and appropriate food‐grade carriers can enhance it. The abovementioned features are also vital to optimize the solubility, water holding capacity, emulsifying ability, and foaming property of BAPs in food products. In the case of safety, the possible allergenic and toxic peptides often exhibit physiological functions and could be produced during the hydrolysis of food proteins. It was also noted that the production of iso‐peptides bonds and undesirable Maillard reaction might occur during protein extraction, sample pretreatments, and peptide synthesis.

show abstract

In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

Cited by 15 publications

References 43 publications

Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

Angiotensin I-Converting Enzyme Inhibitory Activity of Two Peptides Derived from In Vitro Digestion Products of Pork Sausage with Partial Substitution of NaCl by KCl

A critical review of a typical research system for food‐derived metal‐chelating peptides: Production, characterization, identification, digestion, and absorption

An updated review on food‐derived bioactive peptides: Focus on the regulatory requirements, safety, and bioavailability

Contact Info

Product

Resources

About