Hydrolysis of food-derived opioids by dipeptidyl peptidase IV from Lactococcus lactis spp. lactis

Arısoy, Sevda; Üstün-Aytekin, Özlem

doi:10.1016/j.foodres.2018.05.068

Cited by 8 publications

(7 citation statements)

References 37 publications

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“…The rate of elimination of α-CZP was faster than that of YPVEPF. This difference may be due to the structure of Pro at the second position of the N terminus, which was resistant to the DPP-IV enzyme . DPP-IV was present in plasma in a soluble form, which played a vital role in the cleavage of peptides when incubated with plasma .…”

Section: Resultsmentioning

confidence: 99%

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect

Qian

Zheng

Zhao³

et al. 2022

J. Agric. Food Chem.

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YPVEPF (Tyr-Pro-Val-Glu-Pro-Phe) is an outstanding sleep-enhancing peptide derived from casein. This study aimed to evaluate the bioavailability of YPVEPF in vitro and in vivo and to explore its structure–activity relationship through a sleep test and cheminformatics. Our results showed that YPVEPF was unstable against gastrointestinal enzymes and almost totally degraded to YPVEP in vitro. However, the pharmaco-kinetics results in vivo showed that the C max of YPVEPF was 10.38 ± 4.01 ng/mL at 5 min, and YPVEPF could be detected in the stomach, intestine, and brain at 12.89 ± 0.55, 10.26 ± 0.23, and 2.47 ± 0.55 ng/g, respectively. The main metabolites including YPVEP, YP, PVEPF, and PVEP were identified. We first explored whether the fragment YPVEP also had a strong sleep-enhancing effect, and the sleep-enhancing effects of PVEPF and PVEP (lacking a Tyr residue) significantly decreased compared with those of YPVEPF and YPVEP. Moreover, molecular docking and quantum calculations revealed that the N-terminus Tyr played a dominant role in YPVEPF and YPVEP. They had distinctive self-folding structures and varying electron-withdrawing properties of the groups at the N terminus, allowing different binding modes and electron/proton transfer.

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Section: Resultsmentioning

confidence: 99%

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect

Qian

Zheng

Zhao³

et al. 2022

J. Agric. Food Chem.

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“…In this study, we first demonstrated that YFYPEL and neocasomorphin-6 YPVEPF had strong sleep-enhancing effects, which verified our hypothesis. It has been proven that this neocasomorphin-6 YPVEPF not only had opioid activity and DPP-IV inhibitory activity but also could up-regulate MUC4 expression to protect the intestine. − Because of this special structure in YPVEPF (Tyr at N-terminal and Pro at the second position of N-terminal), it could bind with the μ-type opioid receptor and DPP-IV enzyme and it also had potential to bind with the GABA A receptor to play a sleep-enhancing role. In brief, considering these results, other peptides existing in CTH could also promote their sleep-enhancing activity.…”

Section: Resultsmentioning

confidence: 99%

Identification and Screening of Potential Bioactive Peptides with Sleep-Enhancing Effects in Bovine Milk Casein Hydrolysate

Qian

Zheng

et al. 2021

J. Agric. Food Chem.

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Casein tryptic hydrolysate (CTH) has been proven to possess stress-relieving and sleep-enhancing effects, but only one decapeptide YLGYLEQLLR (α-CZP) in CTH was reported to exhibit affinity for the benzodiazepine site of a GABAA receptor (GABAAR). This study aimed to compare the sleep-enhancing effects between CTH and α-CZP and to explore novel sleep-enhancing peptides. Our results showed that CTH significantly prolonged sleep duration in mice, which was almost 2-fold longer than that of α-CZP. The α-CZP in CTH was degraded more slowly than the synthetic α-CZP; meanwhile, CTH could release other potential sleep-enhancing peptides during gastrointestinal digestion. Additionally, two peptides YPVEPF and YFYPEL with strong sleep-enhancing activity were explored by virtual screening. Especially, YPVEPF could significantly prolong the sleep duration from 559.00 ± 272.24 to 2501.63 ± 1021.21 s and increase the sleep rate from 58.33 to 83.33% in mice. Moreover, YPVEPF and YFYPEL could bind with the Ser-205 and Phe-77 residues of GABAAR via hydrogen bonds and lipid contacts. They were largely released after digestion with 11.19 ± 0.15 and 1.78 ± 0.01 g/kg, respectively.

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“…The reason for this is the lack of DPPIV enzyme which is negatively correlated with the amount of β-casomorphin [30]. The DPPIV enzyme is also effective on autistic children on the treatment of some symptoms (e.g., insensitivity to pain, digestion problems, attention problems) which are caused by the effects of β-casomorphins and gluteomorphins [31]. β-casomorphins may also cause depression which is a significant risk factor for cardiac patient men [32].…”

Section: Opioid Receptormentioning

confidence: 99%

“…Gluteomorphin C reduced anxiety and developed learning ability after consumption [9]. Casomorphins and gluteomorphins are associated with autism spectrum disorder because these opioid peptides found in the urine samples of autistic patients and removing casein and gluten proteins from autistic children's diet may improve learning abilities, concentration, attention and language problems, eye contact, and digestion problems [21,31].…”

Section: Opioid Peptides Derived From Plant/cereal Proteinmentioning

confidence: 99%

Food-Derived Opioids: Production and the Effects of Opioids on Human Health

Arısoy¹,

Çoban²,

Üstün-Aytekin³

2019

From Conventional to Innovative Approaches for Pain Treatment

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Traditional opioids have been used for the people who suffer from cancer, burns, surgery, HIV/AIDS, and other serious illness pains for years. However, numerous side effects like dizziness, apnea, physical dependence, tolerance, addiction, nausea, and vomiting push the researchers to look forward to the new opioid options. The opioid peptides which derived from foods provide significant advantages as the safe and natural alternative. The researchers reported that it is also promising a new functional food and nutraceutical. In this chapter, the type of food-derived opioids, their origins, possible receptors, their amino acid sequences, opioid effects, production techniques, and health benefits are reviewed.

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Hydrolysis of food-derived opioids by dipeptidyl peptidase IV from Lactococcus lactis spp. lactis

Cited by 8 publications

References 37 publications

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect

Identification and Screening of Potential Bioactive Peptides with Sleep-Enhancing Effects in Bovine Milk Casein Hydrolysate

Food-Derived Opioids: Production and the Effects of Opioids on Human Health

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