Food-Derived Opioid Peptides in Human Health: A Review
Abstract
:1. Introduction
Opioid Peptides
2. Classification of Opioid Peptides
2.1. Endogenous Opioid Peptides
2.2. Food Derived Exogenous Opioid Peptides
3. Production of Opioid Peptides from Food Proteins
3.1. The Traditional Approach
3.2. The In Silico Approach
3.3. Chemical Synthesis Approach
3.4. The Integrated Approach
3.5. Screening for Bioactive Peptides
4. Mechanism of Action
Transport of Opioid Peptides in the Body
5. Clinical and Animal Studies Related to Exogenous Opioid Peptides in Stress-Related Conditions
Stress, Anxiety, and Depression
6. Conclusions
Author Contributions
Funding
Conflicts of Interest
References
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Peptides | Functions | References |
---|---|---|
Colostrinin | Promotes acquisition of spatial learning in aged rats | [28] |
Corticotropin-releasing factor (CRF) | Improves memory retention Enhance learning performance | [17,29] |
Neuropeptide Y (NPY) | Neuroprotection as by control of feeding works against neurodegenerative diseases | [17,30] |
Substance P (SP) | Improves functional recovery and increases the learning ability | [17,31] |
Nociceptin/orphanin FQ (N/OFQ) | Impairs spatial learning in animal models. Facilitate memory | [32,33,34] |
Angiotensin-vasopressin (AVP) and Oxytocin (OT) | Promote social memory and learning behaviors. Deficiency of AVP results in memory impairment | [35,36] |
Cholecystokinin (CCK) | CCK peptides improve learning and memory performance in the patients Help in anxiety states Lack of CCK-A receptors cause impaired learning and memory functions. Play a role in conditioned fear stress and anxiety | [29,37,38] |
Atrial natriuretic peptide (ANP), Brain-derived natriuretic peptide (BNP), C-type natriuretic peptide (CNP) | Promote action on memory consolidation | [39,40] |
Pituitary adenylate cyclase-activating polypeptide (PACAP) | Promote learning (consolidation and retrieval) | [41] |
Galanin | Impairs the learning and memory performances overexpression impairs cognition | [42,43,44] |
Bombesin/gastrin-releasing peptide (BN/GRP) and Neuromedin (NM) | Improve memory performance | [45,46] |
Hippocampal cholinergic neurostimulation Peptide (HCNP) | Abnormal accumulation and expression associated with memory and learning disorders | [47] |
Calcitonin-gene related peptide (CGRP), Substance P(SP) and Neuropeptide Y (NPY) | Enhance memory retention. SP improves functional recovery and increases learning ability. NPY enhances memory | [30] |
Insulin | Improves short-term memory | [48] |
Orexin-A | Inhibits long-term potentiation (LTP) and retards spatial learning | [49,50] |
(A) | ||||
Opioid Peptide | Amino-Acid Sequence | Protein Precursor | References | |
endomorphin-1 | Tyr-Pro-Trp-Phe-NH2 | pro-endomorphin | [57,58] | |
endomorphin-2 | Tyr-Pro-Phe-Phe-NH2 | pro-endomorphin | [57,58] | |
met-enkephalin | Tyr-Gly-Gly-Phe-Met | pro-enkephalin | [16], | |
leu-enkephalin | Tyr-Gly-Gly-Phe-Leu | pro-enkephalin | [16,59] | |
β-endorphin | Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-ThrPro-Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala-Ile-Ile-LysAsn-Ala-Tyr-Lys-Lys-Gly-Glu | pro-opiomelanocortin | [60,61] | |
dynorphin A | Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-LeuLys-Trp-Asp-Asn-Gln | pro-dynorphin | [62,63] | |
dynorphin B | Phe-Gly-Gly-Phe-Thr-Gly-Ala-Arg-Lys-Ser-Ala-ArgLys-Leu-Ala-Asn-Gln | pronociceptin | [62,63] | |
(B) | ||||
Sequence | IC50 (nM) | Ratio of IC50 Ratio δ/µ | References | |
Affity (µ-Receptor) | Affity (δ-Receptor) | |||
Endomorphins Modified at First Amino Acid Position | ||||
d-Tyr1-Pro-Phe-Phe-NH2 | 32.1 ± 1.5 | 4121 ± 1492 | 128 | [64] |
Dmt1-Pro-Trp-Phe-NH2 | 0.014 ± 0.003 | 12.0 ± 4.05 | 857 | [65] |
Mmt1-Pro-Phe-Phe-NH2 | 0.132 ± 0.008 | 528.6 ± 47 | 4005 | [65] |
Emt1-Pro-Phe-Phe NH2 | 0.063 ± 0.006 | 55.7 ± 6.2 | 884 | [65] |
Dit1-Pro-Phe-Phe-NH2 | 2.29 ± 0.37 | 105 ± 16 | 46 | [65] |
Det1-Pro-Phe-Phe-NH2 | 0.084 ± 0.006 | 69.7 ± 5.3 | 830 | [65] |
Tmt1-Pro-Phe-Phe-NH2 | 1.111 ± 0.002 | 593.5 ± 80 | 5347 | [65] |
Endomorphins Modified at Second Amino Acid Position | ||||
Tyr-d-Pro2-Phe-Phe-NH2 | 512.4 ± 29 | 30,641 ± 419 | 60 | [64] |
Tyr-Aze2-Trp-Phe-NH2 | 2.3 ± 0.23 | 3500 ± 360 | 1500 | [66] |
Tyr-δAla2-Phe-Phe-NH2 | 34 ± 6.3 | 710 ± 130 | 21 | [66] |
Tyr-3Aze2-Phe-Phe-NH2 | 210 ± 51 | 6900 ± 1200 | 32 | [66] |
Tyr-Aze2-Phe-Phe-NH2 | 5.6 ± 1.2 | 5100 ± 600 | 920 | [66] |
Endomorphins Modified at Third Amino Acid Position | ||||
Tyr-Pro-d-Phe3-Phe-NH2 | 203.2 ± 83 | 4230 ± 344 | 21 | [64] |
Tyr-Pro-Phe3-(p-NH2)-Phe-NH2 | 185 ± 36 | >10,000 | >1.9 | [67] |
TyrProPhe3(p-NHCOCH2Br)-PheNH2 | 7210 ± 820 | >10,000 | >1.4 | [67] |
Tyr-Pro-(2S,3R)-βMePhe3-Phe-NH2 | 106 ± 9 | >10,000 | >10 | [68] |
Tyr-Pro-(2S,3S)-βMePhe3-Phe-NH2 | 45.3 ± 4.1 | 179 ± 15 | 4 | [68] |
Tyr-Pro-(2R,3S)-βMePhe3-Phe-NH2 | 4910 ± 328 | >10,000 | >2 | [68] |
Tyr-Pro-(2R,3R)-βMePhe3-Phe-NH2 | 7090 ± 131 | 6760 ± 865 | 1 | [68] |
Tyr-Pro-(F5)-Phe3-Phe-NH2 | 11.7 ± 0.503 | 11,700 ± 1010 | 1000 | [69] |
Endomorphins Modified at C-TERMINAL Position | ||||
Tyr-Pro-Phe-d-Phe4-NH2 | 45.9 ± 8.6 | 8159 ± 1569 | 177 | [64] |
Tyr-Pro-Phe-(p-NH2)-Phe4-NH2 | 36.7 ± 2.2 | >10,000 | >270 | [67] |
TyrProPhePhe4(p-NHCOCH2Br)-NH2 | 158 ± 23 | 1940 ± 310 | 12 | [67] |
Tyr-Pro-Phe-(p-NCS)-Phe4-NH2 | 345 ± 128 | >10,000 | >29 | [67] |
Tyr-Pro-Trp-Dmp4-NH2 | 13.2 ± 1.9 | 7624 ± 2571 | 578 | [70] |
Tyr-Pro-Trp-d-Dmp4-NH2 | 106 ± 20 | 1765 ± 834 | 17 | [70] |
Tyr-Pro-Phe-Phe4-NH-(CH2)5-CODap(6DMN)-NH2 | 244.5 ± 14 | 5939 ± 1396 | 24 | [71] |
Tyr-Pro-Phe-d-Val4-NH-Bn | 4.97 ± 1.24 | 3358 ± 414 | 676 | [72] |
Tyr-Pro-Trp-d-Val4-NH-Bn | 2.32 ± 0.15 | 3287 ± 456 | 1417 | [72] |
Source | Sequences | Peptide Name | References |
---|---|---|---|
Bovine milk β-casein | Tyr-Pro-Phe-Pro | βb-casomorphin-4 | [87] |
Tyr-Pro-Phe-Pro-Gly | βb-casomorphin-5 | ||
Tyr-Pro-Phe-Pro-Gly-Pro | βb-casomorphin-6 | ||
Tyr-Pro-Phe-Pro-Gly-Pro-Ile | βb-casomorphin-7 | ||
Tyr-Pro-Val-Glu-Pro-Phe | Neocasomorphin-6 | [111] | |
Bovine milk α-lactalbumin | Tyr-Gly-Leu-Phe-NH2 | αb-lactorphin | [22] |
Human milk β-casein | Tyr-Pro-Phe-Val | βh-casomorphin-4 | [22] |
Tyr-Pro-Phe-Val-Glu | βh-casomorphin-5 | [57] | |
Tyr-Pro-Phe-Val-Glu-Pro-Ile | βh-casomorphin-7 | [88] | |
Tyr-Pro-Phe-Val-Glu-Pro-Ile-pro | βh-casomorphin-8 | [22,88] | |
Human milk lactalbumin | Tyr-Gly-Leu-Phe-NH2 | αh-lactorphin | [22,94] |
Bovine/bovine milk lactoferrin | Tyr-Leu-Gly-Ser-Gly-Tyr-OCH3 | lactoferrsoxin A | [96] |
Arg-Tyr-Tyr-Gly-Tyr-OCH3 | lactoferrsoxin B | ||
Lys-Tyr-Leu-Gly-Pro-Gln-Tyr-OCH3 | lactoferrsoxin C | ||
Soy β-conglycinin | Tyr-Pro-Phe-Val-Val | Soymorphin-5 | [93] |
Tyr-Pro-Phe-Val-Val-Asn | Soymorphin-6 | ||
Tyr-Pro-Phe-Val-Val-Asn-Ala | Soymorphin-7 | ||
Wheat HMW glutenin | Gly-Tyr-Tyr-Pro | gluten exorphin A4 | [78,112] |
Gly-Tyr-Tyr-Pro-Thr | gluten exorphin A5 | ||
Tyr-Gly-Gly-Trp | gluten exorphin B4 | ||
Tyr-Gly-Gly-Trp-Leu | gluten exorphin B5 | ||
Tyr-Pro-Ile-Ser-Leu | gluten exorphin C | [78,113] | |
Spinach RuBisCo | Tyr-Pro-Leu-Asp-Leu | rubiscolin-5 | [93,114] |
Tyr-Pro-Leu-Asp-Leu-Phe | rubiscolin-6 |
Opioid Peptide | Opioid Activity (IC50 in µM) | µ/δ Ratio | Reference | |
---|---|---|---|---|
Mouse (vas Deferens) (δ) | Guinea-Pig (ileum) (µ) | |||
rubiscolin-5 | 51 | 1110 | 21.8 | [114] |
rubiscolin-6 | 24.4 | 748 | 30.7 | [114] |
βb-casomorphin-4 | 84 | 22 | 0.26 | [87] |
βb-casomorphin-5 | 40 | 6.5 | 0.16 | [87] |
βb-casomorphin-6 | >150 | 27.4 | <0.18 | [87] |
βb-casomorphin-7 | >200 | 57 | <0.29 | [87] |
βh-casomorphin-4 | 750 | 19 | 0.025 | [94] |
βh-casomorphin-5 | ND | 14 | ND | [94] |
βh-casomorphin-6 | 350 | 25 | 0.071 | [94] |
βh-casomorphin-8 | 540 | 25 | 0.047 | [94] |
gluten-exorphin A4 | 70 | >1000 | ND | [112] |
gluten exorphin A5 | 60 | 1000 | 60.7 | [112] |
gluten exorphin B4 | 3.4 | 1.5 | 0.44 | [112] |
gluten exorphin B5 | 0.017 | 0.05 | 2.9 | [112] |
gluten exorphin C | 30 | 110 | 3.7 | [113] |
soymorphin-5 | 50 | 6 | 0.12 | [93] |
soymorphin-6 | 32 | 9.2 | 0.287 | [93] |
soymorphin-7 | 50 | 13 | 0.26 | [93] |
Human milk lactalbumin (α-lactorphin) | >1000 | 50 | ND | [94] |
Bovine milk lactoferrin (lactoferrsoxin) | 4.38 | 5.68 | 0.77 | [96] |
Opioid Peptide | Animal Model | Dosage | Administration Route | Effect | Time Duration | Reference |
---|---|---|---|---|---|---|
rubiscolin-5 | Mice | 3 nM/mouse | i.c.v | antinociception | Effects observed up to 30 min post-injection | [114] |
rubiscolin-6 | Mice | 1 nM/mouse | i.c.v | |||
rubiscolin–6 | Mice | 100 mg/kg 3 nM/mouse | Oral i.c.v | enhancement in memory consolidation | Effects observed up to 24 h post-injection | [100] |
β-casomorphin- 4,-5,-6,-7 | Rat | 60–2000 nM | i.c.v | analgesic, naloxone reversible | Effects observed up to 30–40 min post-injection | [115] |
β-casomorphin-5 | Mice Rat | 1mg/kg 166 nM | i.p i.v | improvement in learning and memory, analgestic | Effects observed up to 30-min post-injection Significant analgesia l0-min after injection up to 60 min post-injection | [116,117] |
β-casomorphin-7 | Rat | 0.1–20 nM | i.c.v | food-intake stimulation | Effects observed up to 6 h post-injection | [118] |
gluten exorphin C | Mice | 5mg/kg | i.p | improvement in learning and behavior, decreased anxiety | Effects observed up to 15–20 min post-injection | [110] |
Gluten-exorphin B5 | Rat | 3 mg/kg | i.v | stimulated prolactin secretion | Effects observed after 20 min post-injection | [109] |
soymorphin-5, 6, and 7 | Mice | 10–30 mg/kg or 3 mg/kg | Oral i.p | anxiolytic effect | Oral—Effects observed up to 20–25 min post-injection i.p—Effects observed <30min of post-injection | [93] |
soymorphin-5 and 7 | Mice | 30 mg/kg or 48 µ mol/kg | oral | reduced food intake and showed anorexigenic activity | Effects observed after 2 h of oral administration | [119] |
soymorphin-5 amide | Rat | 5 mg/kg | i.p | decreased anxiety | Effects observed after 30 min of administration | [120] |
Databases Name | Address | Role |
---|---|---|
NeuroPIpred | https://webs.iiitd.edu.in/raghava/neuropipred | Neuropeptide database |
NeuroPP | http://i.uestc.edu.cn/neuropeptide/neuropp/home.html | Neuropeptide database |
BIOPEP (Bioactivity) (digestion) (Protein) (toxicity) | http://www.uwm.edu.pl/biochemia/index.php/en/biopep | Prediction for precursors of bioactive peptides, |
ToxinPred (Toxicity) | http://crdd.osdd.net/raghava//toxinpred/ | Prediction of toxicity of peptides |
I-TASSER (Protein Structure) | https://zhanglab.ccmb.med.umich.edu/I-TASSER/ | Structure and function prediction |
NCBI (Protein Database) | https://www.ncbi.nlm.nih.gov/ | Protein sequences information |
AlgPred (Toxicity) | http://crdd.osdd.net/raghava//algpred/ | Prediction of toxicity of peptides |
ProtParam (phytochemical) | http://web.expasy.org/protparam/ | Compute GRAVY (grand average of hydropathicity) |
UniProtKB (Protein database) | http://www.uniprot.org/ | Structure and sequences information |
APD (Peptide database) | http://aps.unmc.edu/AP/main.html | Bioactive peptide prediction |
AntiBP2 (Bioactivity prediction) | http://crdd.osdd.net/raghava//antibp2/ | Antibacterial peptide prediction |
PEPstrMOD (Peptide database) | http://osddlinux.osdd.net/raghava/pepstrmod | Prediction of tertiary structures |
Sequence | Half-Life (Mouse Brain) [min] | Reference |
---|---|---|
[d-Ala2, p-Cl-Phe4]EM-1 | >300 | [181] |
[Dmt1,Nip2]EM-1 | 30.9 ± 3.29 | [182] |
[(2S,3S)β-MePhe4]EM-2 | 35.8 ± 1.8 | [68] |
[(1S,2R)ACHC2]EM-1 | >12 h | [183] |
Guanidino-[d-Pro2Gly3, p-Cl-Phe5]EM-1 | 187.3 ± 24 | [181] |
[(1S,2R)ACPC2]EM-2 | >12 h | [183] |
[Dmt1,Nip2]EM-2 | 10.7 ± 0.3 | [182] |
Guanidino-[d-Pro2-Gly3]EM-1 | 111.8 ± 19.2 | [181] |
Guanidino-[Sar2]EM-1 | 43.9 ± 2.4 | [181] |
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Tyagi, A.; Daliri, E.B.-M.; Kwami Ofosu, F.; Yeon, S.-J.; Oh, D.-H. Food-Derived Opioid Peptides in Human Health: A Review. Int. J. Mol. Sci. 2020, 21, 8825. https://doi.org/10.3390/ijms21228825
Tyagi A, Daliri EB-M, Kwami Ofosu F, Yeon S-J, Oh D-H. Food-Derived Opioid Peptides in Human Health: A Review. International Journal of Molecular Sciences. 2020; 21(22):8825. https://doi.org/10.3390/ijms21228825
Chicago/Turabian StyleTyagi, Akanksha, Eric Banan-Mwine Daliri, Fred Kwami Ofosu, Su-Jung Yeon, and Deog-Hwan Oh. 2020. "Food-Derived Opioid Peptides in Human Health: A Review" International Journal of Molecular Sciences 21, no. 22: 8825. https://doi.org/10.3390/ijms21228825