Natural Plant Materials as a Source of Neuroprotective Peptides


如何引用文章

全文:

详细

:In many circumstances, some crucial elements of the neuronal defense system fail, slowly leading to neurodegenerative diseases. Activating this natural process by administering exogenous agents to counteract unfavourable changes seems promising. Therefore, looking for neuroprotective therapeutics, we have to focus on compounds that inhibit the primary mechanisms leading to neuronal injuries, e.g., apoptosis, excitotoxicity, oxidative stress, and inflammation. Among many compounds considered neuroprotective agents, protein hydrolysates and peptides derived from natural materials or their synthetic analogues are good candidates. They have several advantages, such as high selectivity and biological activity, a broad range of targets, and high safety profile. This review aims to provide biological activities, the mechanism of action and the functional properties of plant-derived protein hydrolysates and peptides. We focused on their significant role in human health by affecting the nervous system and having neuroprotective and brain-boosting properties, leading to memory and cognitive improving activities. We hope our observation may guide the evaluation of novel peptides with potential neuroprotective effects. Research into neuroprotective peptides may find application in different sectors as ingredients in functional foods or pharmaceuticals to improve human health and prevent diseases.

作者简介

Agnieszka Skibska

Department of Biomolecular Chemistry, Faculty of Medicine, Medical University

Email: info@benthamscience.net

Renata Perlikowska

Department of Biomolecular Chemistry, Faculty of Medicine, Medical University

编辑信件的主要联系方式.
Email: info@benthamscience.net

参考

  1. Muddapu, V.R.; Dharshini, S.A.P.; Chakravarthy, V.S.; Gromiha, M.M. Neurodegenerative diseases-Is metabolic deficiency the root cause? Front. Neurosci., 2020, 14(213), 213. doi: 10.3389/fnins.2020.00213 PMID: 32296300
  2. Qin, N.; Geng, A.; Xue, R. Activated or impaired: An overview of DNA repair in neurodegenerative diseases. Aging Dis., 2022, 13(4), 987-1004. doi: 10.14336/AD.2021.1212 PMID: 35855336
  3. Tan, S.H.; Karri, V.; Tay, N.W.R.; Chang, K.H.; Ah, H.Y.; Ng, P.Q.; Ho, H.S.; Keh, H.W.; Candasamy, M. Emerging pathways to neurodegeneration: Dissecting the critical molecular mechanisms in Alzheimer’s disease, Parkinson’s disease. Biomed. Pharmacother., 2019, 111, 765-777. doi: 10.1016/j.biopha.2018.12.101 PMID: 30612001
  4. Ayeni, E.A.; Aldossary, A.M.; Ayejoto, D.A.; Gbadegesin, L.A.; Alshehri, A.A.; Alfassam, H.A.; Afewerky, H.K.; Almughem, F.A.; Bello, S.M.; Tawfik, E.A. Neurodegenerative diseases: Implications of environmental and climatic influences on neurotransmitters and neuronal hormones activities. Int. J. Environ. Res. Public Health, 2022, 19(19), 12495. doi: 10.3390/ijerph191912495 PMID: 36231792
  5. Dailah, H.G. Potential of therapeutic small molecules in apoptosis regulation in the treatment of neurodegenerative diseases: An updated review. Molecules, 2022, 27(21), 7207. doi: 10.3390/molecules27217207 PMID: 36364033
  6. Vajda, F.J.E. Neuroprotection and neurodegenerative disease. J. Clin. Neurosci., 2002, 9(1), 4-8. doi: 10.1054/jocn.2001.1027 PMID: 11749009
  7. Burbach, J.P.H. Neuropeptides from concept to online database www.neuropeptides.nl. Eur J Pharmacol., 2010, 626(1), 27-48. doi: 10.1016/j.ejphar.2009.10.015 PMID: 19837055
  8. Yeo, X.Y.; Cunliffe, G.; Ho, R.C.; Lee, S.S.; Jung, S. Potentials of neuropeptides as therapeutic agents for neurological diseases. Biomedicines, 2022, 10(2), 343. doi: 10.3390/biomedicines10020343 PMID: 35203552
  9. Zheng, Y.; Zhang, L.; Xie, J.; Shi, L. The emerging role of neuropeptides in Parkinson’s disease. Front. Aging Neurosci., 2021, 13, 646726. doi: 10.3389/fnagi.2021.646726 PMID: 33762925
  10. Behl, T.; Madaan, P.; Sehgal, A.; Singh, S.; Makeen, H.A.; Albratty, M.; Alhazmi, H.A.; Meraya, A.M.; Bungau, S. Demystifying the neuroprotective role of neuropeptides in Parkinson's disease: A newfangled and eloquent therapeutic perspective. Int. J. Mol. Sci., 2022, 23(9), 1-34. doi: 10.3390/ijms23094565
  11. Ben-Shushan, S.; Miller, Y. Neuropeptides: Roles and activities as metal chelators in neurodegenerative diseases. J. Phys. Chem. B, 2021, 125(11), 2796-2811. doi: 10.1021/acs.jpcb.0c11151 PMID: 33570949
  12. Mirchandani-Duque, M.; Barbancho, M.A.; López-Salas, A.; Alvarez-Contino, J.E.; García-Casares, N.; Fuxe, K.; Borroto-Escuela, D.O.; Narváez, M. Galanin and neuropeptide Y interaction enhances proliferation of granule precursor cells and expression of neuroprotective factors in the rat hippocampus with consequent augmented spatial memory. Biomedicines, 2022, 10(6), 1297. doi: 10.3390/biomedicines10061297 PMID: 35740319
  13. Akbarian, M.; Khani, A.; Eghbalpour, S.; Uversky, V.N. Bioactive peptides: Synthesis, sources, applications and proposed mechanisms of action. Int. J. Mol. Sci., 2022, 23(3), 1-30.
  14. Sarmadi, B.H.; Ismail, A. Antioxidative peptides from food proteins: A review. Peptides, 2010, 31(10), 1949-1956. doi: 10.1016/j.peptides.2010.06.020 PMID: 20600423
  15. H, M.; J, F.G. Biofunctional peptides from milk proteins: mineral binding and cytomodulatory effects. Curr. Pharm. Des., 2003, 9(16), 1289-1295. doi: 10.2174/1381612033454847 PMID: 12769737
  16. Sánchez, A.; Vázquez, A. Bioactive peptides: A review. Food Qual. Saf., 2017, 1(1), 29-46. doi: 10.1093/fqs/fyx006
  17. Perlikowska, R. Whether short peptides are good candidates for future neuroprotective therapeutics? Peptides, 2021, 140(170528), 170528. doi: 10.1016/j.peptides.2021.170528 PMID: 33716091
  18. Katayama, S.; Nakamura, S. Emerging roles of bioactive peptides on brain health promotion. Int. J. Food Sci. Technol., 2019, 54(6), 1949-1955. doi: 10.1111/ijfs.14076
  19. Lee, S.Y.; Hur, S.J. Mechanisms of neuroprotective effects of peptides derived from natural materials and their production and assessment. Compr. Rev. Food Sci. Food Saf., 2019, 18(4), 923-935. doi: 10.1111/1541-4337.12451 PMID: 33336993
  20. Wang, S.; Sun-Waterhouse, D.; Neil Waterhouse, G.I.; Zheng, L.; Su, G.; Zhao, M. Effects of food-derived bioactive peptides on cognitive deficits and memory decline in neurodegenerative diseases: A review. Trends Food Sci. Technol., 2021, 116, 712-732. doi: 10.1016/j.tifs.2021.04.056
  21. Galland, F.; de Espindola, J.S.; Lopes, D.S.; Taccola, M.F.; Pacheco, M.T.B. Food-derived bioactive peptides: Mechanisms of action underlying inflammation and oxidative stress in the central nervous system. Food Chem. Adv., 2022, 1(100087), 100087. doi: 10.1016/j.focha.2022.100087
  22. Nwachukwu, I.D.; Aluko, R.E. Structural and functional properties of food protein-derived antioxidant peptides. J. Food Biochem., 2019, 43(1), e12761. doi: 10.1111/jfbc.12761 PMID: 31353492
  23. Giovannini, D.; Andreola, F.; Spitalieri, P.; Krasnowska, E.K.; Colini Baldeschi, A.; Rossi, S.; Sangiuolo, F.; Cozzolino, M.; Serafino, A. Natriuretic peptides are neuroprotective on in vitro models of PD and promote dopaminergic differentiation of hiPSCs-derived neurons via the Wnt/β-catenin signaling. Cell Death Discov., 2021, 7(1), 330. doi: 10.1038/s41420-021-00723-6 PMID: 34725335
  24. Ikeda, Y.; Nagase, N.; Tsuji, A.; Kitagishi, Y.; Matsuda, S. Neuroprotection by dipeptidyl-peptidase-4 inhibitors and glucagon-like peptide-1 analogs via the modulation of AKT-signaling pathway in Alzheimer’s disease. World J. Biol. Chem., 2021, 12(6), 104-113. doi: 10.4331/wjbc.v12.i6.104 PMID: 34904048
  25. Park, J.E.; Leem, Y.H.; Park, J.S.; Kim, D.Y.; Kang, J.L.; Kim, H.S. Anti-inflammatory and neuroprotective mechanisms of gts-21, an α7 nicotinic acetylcholine receptor agonist, in neuroinflammation and Parkinson's disease mouse models. Int. J. Mol. Sci., 2022, 23(8), 1-19.
  26. Prasasty, V.; Radifar, M.; Istyastono, E. Natural peptides in drug discovery targeting acetylcholinesterase. Molecules, 2018, 23(9), 1-21. doi: 10.3390/molecules23092344
  27. Sosalagere, C.; Adesegun Kehinde, B.; Sharma, P. Isolation and functionalities of bioactive peptides from fruits and vegetables: A reviews. Food Chem., 2022, 366, 130494. doi: 10.1016/j.foodchem.2021.130494 PMID: 34293544
  28. Fan, H.; Liu, H.; Zhang, Y.; Zhang, S.; Liu, T.; Wang, D. Review on plant-derived bioactive peptides: biological activities, mechanism of action and utilizations in food development. J. Fut. Foods, 2022, 2(2), 143-159. doi: 10.1016/j.jfutfo.2022.03.003
  29. Viel, T.A.; Toricelli, M.; Pereira, A.A.R.; Souza Abrao, G.; Malerba, H.N.; Maia, J.; Buck, H.S. Mechanisms of neuroplasticity and brain degeneration: strategies for protection during the aging process. Neural Regen. Res., 2021, 16(1), 58-67. doi: 10.4103/1673-5374.286952 PMID: 32788448
  30. Gitler, A.D.; Dhillon, P.; Shorter, J. Neurodegenerative disease: models, mechanisms, and a new hope. Dis. Model. Mech., 2017, 10(5), 499-502. doi: 10.1242/dmm.030205 PMID: 28468935
  31. Fricker, L.D. Neuropeptides and other bioactive peptides: From discovery to function. Colloq. Ser. Neuropeptides, 2012, 1(2), 1-122. doi: 10.4199/C00058ED1V01Y201205NPE003
  32. Moujalled, D.; Strasser, A.; Liddell, J.R. Molecular mechanisms of cell death in neurological diseases. Cell Death Differ., 2021, 28(7), 2029-2044. doi: 10.1038/s41418-021-00814-y PMID: 34099897
  33. Gan, L.; Cookson, M.R.; Petrucelli, L.; La Spada, A.R. Converging pathways in neurodegeneration, from genetics to mechanisms. Nat. Neurosci., 2018, 21(10), 1300-1309. doi: 10.1038/s41593-018-0237-7 PMID: 30258237
  34. Liu, J.; Chang, L.; Song, Y.; Li, H.; Wu, Y. The role of NMDA receptors in Alzheimer’s disease. Front. Neurosci., 2019, 13, 43. doi: 10.3389/fnins.2019.00043 PMID: 30800052
  35. Lee, J.H.; Jeong, S.K.; Kim, B.C.; Park, K.W.; Dash, A. Donepezil across the spectrum of Alzheimer’s disease: dose optimization and clinical relevance. Acta Neurol. Scand., 2015, 131(5), 259-267. doi: 10.1111/ane.12386 PMID: 25690270
  36. Sharma, N.K.; Sethy, N.K.; Meena, R.N.; Ilavazhagan, G.; Das, M.; Bhargava, K. Activity-dependent neuroprotective protein (ADNP)-derived peptide (NAP) ameliorates hypobaric hypoxia induced oxidative stress in rat brain. Peptides, 2011, 32(6), 1217-1224. doi: 10.1016/j.peptides.2011.03.016 PMID: 21453737
  37. Sharma, K. Cholinesterase inhibitors as Alzheimer’s therapeutics (Review). Mol. Med. Rep., 2019, 20(2), 1479-1487. PMID: 31257471
  38. Finkel, S.I. Effects of rivastigmine on behavioral and psychological symptoms of dementia in Alzheimer’s disease. Clin. Ther., 2004, 26(7), 980-990. doi: 10.1016/S0149-2918(04)90172-5 PMID: 15336465
  39. Iarkov, A.; Barreto, G.E.; Grizzell, J.A.; Echeverria, V. Strategies for the treatment of Parkinson’s disease: Beyond dopamine. Front. Aging Neurosci., 2020, 12(4), 4. doi: 10.3389/fnagi.2020.00004 PMID: 32076403
  40. Quinn, N. Fortnightly review: Drug treatment of Parkinson’s disease. BMJ, 1995, 310(6979), 575-579. doi: 10.1136/bmj.310.6979.575 PMID: 7888935
  41. Jatana, N.; Apoorva, N.; Malik, S.; Sharma, A.; Latha, N. Inhibitors of catechol-O-methyltransferase in the treatment of neurological disorders. Cent. Nerv. Syst. Agents Med. Chem., 2014, 13(3), 166-194. doi: 10.2174/1871524913666140109113341 PMID: 24450388
  42. Le, W.D.; Jankovic, J. Are dopamine receptor agonists neuroprotective in Parkinson’s disease? Drugs Aging, 2001, 18(6), 389-396. doi: 10.2165/00002512-200118060-00001 PMID: 11419913
  43. Bonuccelli, U.; Colzi, A.; Del Dotto, P. Pergolide in the treatment of patients with early and advanced Parkinson’s disease. Clin. Neuropharmacol., 2002, 25(1), 1-10. doi: 10.1097/00002826-200201000-00001 PMID: 11852289
  44. Cai, Z. Monoamine oxidase inhibitors: Promising therapeutic agents for Alzheimer’s disease (Review). Mol. Med. Rep., 2014, 9(5), 1533-1541. doi: 10.3892/mmr.2014.2040 PMID: 24626484
  45. Amato, A.; Terzo, S.; Mulè, F. Natural compounds as beneficial antioxidant agents in neurodegenerative disorders: A focus on Alzheimer’s disease. Antioxidants, 2019, 8(12), 608-622. doi: 10.3390/antiox8120608 PMID: 31801234
  46. Zakharova, M. Modern approaches in gene therapy of motor neuron diseases. Med. Res. Rev., 2021, 41(5), 2634-2655. doi: 10.1002/med.21705 PMID: 32638429
  47. Doxakis, E. Therapeutic antisense oligonucleotides for movement disorders. Med. Res. Rev., 2021, 41(5), 2656-2688. doi: 10.1002/med.21706 PMID: 32656818
  48. Bento-Pereira, C.; Dinkova-Kostova, A.T. Activation of transcription factor Nrf2 to counteract mitochondrial dysfunction in Parkinson’s disease. Med. Res. Rev., 2021, 41(2), 785-802. doi: 10.1002/med.21714 PMID: 32681666
  49. Hussain, R.; Zubair, H.; Pursell, S.; Shahab, M. Neurodegenerative diseases: Regenerative mechanisms and novel therapeutic approaches. Brain Sci., 2018, 8(9), 177. doi: 10.3390/brainsci8090177 PMID: 30223579
  50. Albertini, C.; Salerno, A.; Sena Murteira Pinheiro, P.; Bolognesi, M.L. From combinations to multitarget-directed ligands: A continuum in Alzheimer’s disease polypharmacology. Med. Res. Rev., 2021, 41(5), 2606-2633. doi: 10.1002/med.21699 PMID: 32557696
  51. Durães, F.; Pinto, M.; Sousa, E. Old drugs as new treatments for neurodegenerative diseases. Pharmaceuticals (Basel), 2018, 11(2), 44. doi: 10.3390/ph11020044 PMID: 29751602
  52. Mucke, H.A.M. The case of galantamine: Repurposing and late blooming of a cholinergic drug. Future Sci. 2015, 1(4), FSO73, 1-6, 2015, 1(4), 1-6.
  53. Heinrich, M. Galanthamine from Galanthus and other Amaryllidaceae--chemistry and biology based on traditional use. Alkaloids Chem. Biol., 2010, 68, 157-165. doi: 10.1016/S1099-4831(10)06804-5 PMID: 20334038
  54. Lee, H.M.; Kim, Y. Drug repurposing is a new opportunity for developing drugs against neuropsychiatric disorders. Schizophr. Res. Treatment, 2016, 2016(6378137), 1-12. doi: 10.1155/2016/6378137 PMID: 27073698
  55. Biagini, G.; Frasoldati, A.; Fuxe, K.; Agnati, L.F. The concept of astrocyte-kinetic drug in the treatment of neurodegenerative diseases: Evidence for l-deprenyl-induced activation of reactive astrocytes. Neurochem. Int., 1994, 25(1), 17-22. doi: 10.1016/0197-0186(94)90047-7 PMID: 7950964
  56. Pålhagen, S.; Heinonen, E.; Hägglund, J.; Kaugesaar, T.; Mäki-Ikola, O.; Palm, R. Selegiline slows the progression of the symptoms of Parkinson disease. Neurology, 2006, 66(8), 1200-1206. doi: 10.1212/01.wnl.0000204007.46190.54 PMID: 16540603
  57. Elufioye, T.O.; Berida, T.I.; Habtemariam, S. Plants-derived neuroprotective agents: Cutting the cycle of cell death through multiple mechanisms. Evid. Based Complement. Alternat. Med., 2017, 2017(3574012), 1-27. doi: 10.1155/2017/3574012 PMID: 28904554
  58. Khazdair, M.R.; Anaeigoudari, A.; Hashemzehi, M.; Mohebbati, R. Neuroprotective potency of some spice herbs, a literature review. J. Tradit. Complement. Med., 2019, 9(2), 98-105. doi: 10.1016/j.jtcme.2018.01.002 PMID: 30963044
  59. Chen, H.; Zhao, M.; Lin, L.; Wang, J.; Sun-Waterhouse, D.; Dong, Y.; Zhuang, M.; Su, G. Identification of antioxidative peptides from defatted walnut meal hydrolysate with potential for improving learning and memory. Food Res. Int., 2015, 78, 216-223. doi: 10.1016/j.foodres.2015.10.008 PMID: 28433285
  60. Wang, S.; Zheng, L.; Zhao, T.; Zhang, Q.; Su, G.; Zhao, M. The neuroprotective effect of walnut-derived peptides against glutamate-induced damage in PC12 cells: mechanism and bioavailability. Food Sci. Hum. Wellness, 2022, 11(4), 933-942. doi: 10.1016/j.fshw.2022.03.021
  61. Wang, S.; Su, G.; Zhang, Q.; Zhao, T.; Liu, Y.; Zheng, L.; Zhao, M. Walnut (Juglans regia) peptides reverse sleep deprivation-induced memory impairment in rat via alleviating oxidative stress. J. Agric. Food Chem., 2018, 66(40), 10617-10627. doi: 10.1021/acs.jafc.8b03884 PMID: 30226056
  62. Lorenzo, J.M.; Munekata, P.E.S.; Gómez, B.; Barba, F.J.; Mora, L.; Pérez-Santaescolástica, C.; Toldrá, F. Bioactive peptides as natural antioxidants in food products – A review. Trends Food Sci. Technol., 2018, 79, 136-147. doi: 10.1016/j.tifs.2018.07.003
  63. Matsui, R.; Honda, R.; Kanome, M.; Hagiwara, A.; Matsuda, Y.; Togitani, T.; Ikemoto, N.; Terashima, M. Designing antioxidant peptides based on the antioxidant properties of the amino acid side-chains. Food Chem., 2018, 245, 750-755. doi: 10.1016/j.foodchem.2017.11.119 PMID: 29287436
  64. Zhao, K.; Zhao, G.M.; Wu, D.; Soong, Y.; Birk, A.V.; Schiller, P.W.; Szeto, H.H. Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury. J. Biol. Chem., 2004, 279(33), 34682-34690. doi: 10.1074/jbc.M402999200 PMID: 15178689
  65. Karami, Z.; Akbari-adergani, B. Bioactive food derived peptides: a review on correlation between structure of bioactive peptides and their functional properties. J. Food Sci. Technol., 2019, 56(2), 535-547. doi: 10.1007/s13197-018-3549-4 PMID: 30906011
  66. Barashkova, A.S.; Rogozhin, E.A. Isolation of antimicrobial peptides from different plant sources: Does a general extraction method exist? Plant Methods, 2020, 16(1), 143. doi: 10.1186/s13007-020-00687-1 PMID: 33110440
  67. Liu, W.; Chen, X.; Li, H.; Zhang, J.; An, J.; Liu, X. Anti-inflammatory function of plant-derived bioactive peptides: A review. Foods, 2022, 11(15), 1-16. doi: 10.3390/foods11152361
  68. Aguilar-Toalá, J.E.; Hernández-Mendoza, A.; González-Córdova, A.F.; Vallejo-Cordoba, B.; Liceaga, A.M. Potential role of natural bioactive peptides for development of cosmeceutical skin products. Peptides, 2019, 122, 170170. doi: 10.1016/j.peptides.2019.170170 PMID: 31574281
  69. Chai, K.F.; Voo, A.Y.H.; Chen, W.N. Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development. Compr. Rev. Food Sci. Food Saf., 2020, 19(6), 3825-3885. doi: 10.1111/1541-4337.12651 PMID: 33337042
  70. Jakubczyk, A.; Karaś, M.; Rybczyńska-Tkaczyk, K.; Zielińska, E.; Zieliński, D. Current trends of bioactive peptides-New sources and therapeutic effect. Foods, 2020, 9(7), 1-28. doi: 10.3390/foods9070846
  71. Liu, Y.Q.; Strappe, P.; Shang, W.T.; Zhou, Z.K. Functional peptides derived from rice bran proteins. Crit. Rev. Food Sci. Nutr., 2019, 59(2), 349-356. doi: 10.1080/10408398.2017.1374923 PMID: 28886263
  72. Fadimu, G.J.; Le, T.T.; Gill, H.; Farahnaky, A.; Olatunde, O.O.; Truong, T. Enhancing the biological activities of food protein-derived peptides using non-thermal technologies: A review. Foods, 1823, 11(13), 1-27.
  73. Daliri, E.B.M.; Oh, D.H.; Lee, B.H. Bioactive Peptides. Foods, 2017, 6(5), 1-21. doi: 10.3390/foods6050032
  74. Wang, X.; Yu, H.; Xing, R.; Liu, S.; Chen, X.; Li, P. Effect and mechanism of oyster hydrolytic peptides on spatial learning and memory in mice. RSC Advances, 2018, 8(11), 6125-6135. doi: 10.1039/C7RA13139A PMID: 35539616
  75. Kristinsson, H.G.; Rasco, B.A. Fish protein hydrolysates: production, biochemical, and functional properties. Crit. Rev. Food Sci. Nutr., 2000, 40(1), 43-81. doi: 10.1080/10408690091189266 PMID: 10674201
  76. Jiang, L.; Xu, H.; Li, Y. Enzymolysis for preparation of ACE inhibitory peptides from walnut protein and studies on its function. J. Chin. Inst. Food Sci. Technol., 2015, 15(2), 79-85.
  77. Li, W.; Zhao, T.; Zhang, J.; Wu, C.; Zhao, M.; Su, G. Comparison of neuroprotective and cognition-enhancing properties of hydrolysates from soybean, walnut, and peanut protein. J. Chem., 2016, 2016, 1-8. doi: 10.1155/2016/9358285
  78. Li, X.; Guo, M.; Chi, J.; Ma, J. Bioactive peptides from walnut residue protein. Molecules,, 2020, 25(6), 1-14. doi: 10.3390/molecules25061285
  79. Gu, M.; Chen, H.P.; Zhao, M.M.; Wang, X.; Yang, B.; Ren, J.Y.; Su, G.W. Identification of antioxidant peptides released from defatted walnut (Juglans Sigillata Dode) meal proteins with pancreatin. Lebensm. Wiss. Technol., 2015, 60(1), 213-220. doi: 10.1016/j.lwt.2014.07.052
  80. Meloni, B.P.; Mastaglia, F.L.; Knuckey, N.W. Cationic arginine-rich peptides (CARPs): A novel class of neuroprotective agents with a multimodal mechanism of action. Front. Neurol., 2020, 11(108), 108. doi: 10.3389/fneur.2020.00108 PMID: 32158425
  81. Wang, S.; Su, G.; Fan, J.; Xiao, Z.; Zheng, L.; Zhao, M.; Wu, J. Arginine-containing peptides derived from walnut protein against cognitive and memory impairment in scopolamine-induced zebrafish: Design, release, and neuroprotection. J. Agric. Food Chem., 2022, 70(37), 11579-11590. doi: 10.1021/acs.jafc.2c05104 PMID: 36098553
  82. Feng, L.; Peng, F.; Wang, X.; Li, M.; Lei, H.; Xu, H. Identification and characterization of antioxidative peptides derived from simulated in vitro gastrointestinal digestion of walnut meal proteins. Food Res. Int., 2019, 116, 518-526. doi: 10.1016/j.foodres.2018.08.068 PMID: 30716976
  83. Wang, S.; Zheng, L.; Zhao, T.; Zhang, Q.; Liu, Y.; Sun, B.; Su, G.; Zhao, M. Inhibitory effects of walnut (Juglans regia) peptides on neuroinflammation and oxidative stress in lipopolysaccharide-induced cognitive impairment mice. J. Agric. Food Chem., 2020, 68(8), 2381-2392. doi: 10.1021/acs.jafc.9b07670 PMID: 32037817
  84. Sheng, J.; Yang, X.; Liu, Q.; Luo, H.; Yin, X.; Liang, M.; Liu, W.; Lan, X.; Wan, J.; Yang, X. Coadministration with tea polyphenols enhances the neuroprotective effect of defatted walnut meal hydrolysate against scopolamine-induced learning and memory deficits in mice. J. Agric. Food Chem., 2020, 68(3), 751-758. doi: 10.1021/acs.jafc.9b05081 PMID: 31861959
  85. Sheng, J.; Yang, X.; Chen, J.; Peng, T.; Yin, X.; Liu, W.; Liang, M.; Wan, J.; Yang, X. Antioxidative effects and mechanism study of bioactive peptides from defatted walnut (Juglans regia L.) meal hydrolysate. J. Agric. Food Chem., 2019, 67(12), 3305-3312. doi: 10.1021/acs.jafc.8b05722 PMID: 30817142
  86. Ren, D.; Zhao, F.; Liu, C.; Wang, J.; Guo, Y.; Liu, J.; Min, W. Antioxidant hydrolyzed peptides from Manchurian walnut (Juglans mandshurica Maxim.) attenuate scopolamine-induced memory impairment in mice. J. Sci. Food Agric., 2018, 98(13), 5142-5152. doi: 10.1002/jsfa.9060 PMID: 29652442
  87. Liu, C.; Guo, Y.; Zhao, F.; Qin, H.; Lu, H.; Fang, L.; Wang, J.; Min, W. Potential mechanisms mediating the protective effects of a peptide from walnut (Juglans mandshurica Maxim.) against hydrogen peroxide induced neurotoxicity in PC12 cells. Food Funct., 2019, 10(6), 3491-3501. doi: 10.1039/C8FO02557F PMID: 31143910
  88. Zhao, F.; Wang, J.; Lu, H.; Fang, L.; Qin, H.; Liu, C.; Min, W. Neuroprotection by walnut-derived peptides through autophagy promotion via Akt/mTOR signaling pathway against oxidative stress in PC12 cells. J. Agric. Food Chem., 2020, 68(11), 3638-3648. doi: 10.1021/acs.jafc.9b08252 PMID: 32090563
  89. Prajapati, P.; Sripada, L.; Singh, K.; Bhatelia, K.; Singh, R.; Singh, R. TNF-α regulates miRNA targeting mitochondrial complex-I and induces cell death in dopaminergic cells. Biochim. Biophys. Acta Mol. Basis Dis., 2015, 1852(3), 451-461. doi: 10.1016/j.bbadis.2014.11.019 PMID: 25481834
  90. Zheng, L.; Su, G.; Ren, J.; Gu, L.; You, L.; Zhao, M. Isolation and characterization of an oxygen radical absorbance activity peptide from defatted peanut meal hydrolysate and its antioxidant properties. J. Agric. Food Chem., 2012, 60(21), 5431-5437. doi: 10.1021/jf3017173 PMID: 22577732
  91. Katayama, S.; Imai, R.; Sugiyama, H.; Nakamura, S. Oral administration of soy peptides suppresses cognitive decline by induction of neurotrophic factors in SAMP8 mice. J. Agric. Food Chem., 2014, 62(16), 3563-3569. doi: 10.1021/jf405416s PMID: 24678753
  92. Shimizu, A.; Mitani, T.; Tanaka, S.; Fujii, H.; Maebuchi, M.; Amiya, Y.; Tanaka, M.; Matsui, T.; Nakamura, S.; Katayama, S. Soybean-derived glycine–arginine dipeptide administration promotes neurotrophic factor expression in the mouse brain. J. Agric. Food Chem., 2018, 66(30), 7935-7941. doi: 10.1021/acs.jafc.8b01581 PMID: 29985005
  93. Ju, D.T.; Kumar, A.K.; Kuo, W.W.; Ho, T.J.; Chang, R.L.; Lin, W.T.; Day, C.H.; Viswanadha, V.V.P.; Liao, P.H.; Huang, C.Y. Bioactive peptide VHVV upregulates the long-term memory-related biomarkers in adult spontaneously hypertensive rats. Int. J. Mol. Sci., 20(12), 1-13. doi: 10.3390/ijms20123069
  94. Tanaka, M.; Kiyohara, H.; Yoshino, A.; Nakano, A.; Takata, F.; Dohgu, S.; Kataoka, Y.; Matsui, T. Brain-transportable soy dipeptide, Tyr-Pro, attenuates amyloid β peptide25-35-induced memory impairment in mice. NPJ Sci. Food, 2020, 4(1), 7. doi: 10.1038/s41538-020-0067-3 PMID: 32377566
  95. Maebuchi, M.; Samoto, M.; Kohno, M.; Ito, R.; Koikeda, T.; Hirotsuka, M.; Nakabou, Y. Improvement in the intestinal absorption of soy protein by enzymatic digestion to oligopeptide in healthy adult men. Food Sci. Technol. Res., 2007, 13(1), 45-53. doi: 10.3136/fstr.13.45
  96. Ichinose, T.; Moriyasu, K.; Nakahata, A.; Tanaka, M.; Matsui, T.; Furuya, S. Orally administrated dipeptide Ser-Tyr efficiently stimulates noradrenergic turnover in the mouse brain. Biosci. Biotechnol. Biochem., 2015, 79(9), 1542-1547. doi: 10.1080/09168451.2015.1044932 PMID: 25996770
  97. Ichinose, T.; Murasawa, H.; Ishijima, T.; Okada, S.; Abe, K.; Matsumoto, S.; Matsui, T.; Furuya, S. Tyr-Trp administration facilitates brain norepinephrine metabolism and ameliorates a short-term memory deficit in a mouse model of Alzheimer's disease. PLoS One., 2020, 15(5), 1-17.
  98. Kannan, A.; Hettiarachchy, N.; Mahadevan, M. Peptides derived from rice bran protect cells from obesity and Alzheimer’s disease. Int. J. Biomed. Res., 2012, 3(3), 131-135. doi: 10.7439/ijbr.v3i3.299
  99. Hettiarachchy, N.S. Bioactive Pentapeptides from Rice Bran and Use Thereof. U.S. Patent 8575310B2, 2013.,
  100. Wu, J.; Li, P.; Shi, Y.; Fang, Y.; Zhu, Y.; Fan, F.; Pei, F.; Xia, J.; Xie, M.; Hu, Q. Neuroprotective effects of two selenium-containing peptides, TSeMMM and SeMDPGQQ, derived from selenium-enriched rice protein hydrolysates on Pb2+-induced oxidative stress in HT22 cells. Food Chem. Toxicol., 2020, 135(110932), 110932. doi: 10.1016/j.fct.2019.110932 PMID: 31682935
  101. Lu, R.R.; Qian, P.; Sun, Z.; Zhou, X.H.; Chen, T.P.; He, J.F.; Zhang, H.; Wu, J. Hempseed protein derived antioxidative peptides: Purification, identification and protection from hydrogen peroxide-induced apoptosis in PC12 cells. Food Chem., 2010, 123(4), 1210-1218. doi: 10.1016/j.foodchem.2010.05.089
  102. Rodriguez-Martin, N.M.; Toscano, R.; Villanueva, A.; Pedroche, J.; Millan, F.; Montserrat-de la Paz, S.; Millan-Linares, M.C. Neuroprotective protein hydrolysates from hemp (Cannabis sativa L.) seeds. Food Funct., 2019, 10(10), 6732-6739. doi: 10.1039/C9FO01904A PMID: 31576391
  103. Montserrat-de la Paz, S.; Carrillo-Berdasco, G.; Rivero-Pino, F.; Villanueva-Lazo, A.; Millan-Linares, M.C. Hemp protein hydrolysates modulate inflammasome-related genes in microglial cells. Biology (Basel), 2022, 12(1), 49. doi: 10.3390/biology12010049 PMID: 36671742
  104. Wattanathorn, J.; Thukham-mee, W.; Muchimapura, S.; Wannanon, P.; Tong-un, T.; Tiamkao, S. Preventive effect of cashew-derived protein hydrolysate with high fiber on cerebral ischemia. BioMed Res. Int., 2017, 2017(6135023), 1-14. doi: 10.1155/2017/6135023 PMID: 29457029
  105. Sato, N.; Furuta, T.; Takeda, T.; Miyabe, Y.; Ura, K.; Takagi, Y.; Yasui, H.; Kumagai, Y.; Kishimura, H. Antioxidant activity of proteins extracted from red alga dulse harvested in Japan. J. Food Biochem, 2019, 43(2), 1-7. doi: 10.1111/jfbc.12709
  106. Zhu, K.X.; Guo, X.; Guo, X.N.; Peng, W.; Zhou, H.M. Protective effects of wheat germ protein isolate hydrolysates (WGPIH) against hydrogen peroxide-induced oxidative stress in PC12 cells. Food Res. Int., 2013, 53(1), 297-303. doi: 10.1016/j.foodres.2013.05.007
  107. Chen, J.; Liu, X.; Li, Z.; Qi, A.; Yao, P.; Zhou, Z.; Dong, T.T.X.; Tsim, K.W.K. A review of dietary Ziziphus jujuba fruit (Jujube): Developing health food supplements for brain protection. Evid. Based Complement. Alternat. Med., 2017, 2017(3019568), 3019568. PMID: 28680447
  108. Zare-Zardini, H.; Tolueinia, B.; Hashemi, A.; ebrahimi, L.; Fesahat, F. Antioxidant and cholinesterase inhibitory activity of a new peptide from Ziziphus jujuba fruits. Am. J. Alzheimers Dis. Other Demen., 2013, 28(7), 702-709. doi: 10.1177/1533317513500839 PMID: 24005854
  109. Kanbargi, K.D.; Sonawane, S.K.; Arya, S.S. Functional and antioxidant activity of Ziziphus jujube seed protein hydrolysates. J. Food Meas. Charact., 2016, 10(2), 226-235. doi: 10.1007/s11694-015-9297-5
  110. Lemus-Conejo, A.; Millan-Linares, M.C.; Toscano, R.; Millan, F.; Pedroche, J.; Muriana, F.J.G.; Montserrat-de la Paz, S. GPETAFLR, a peptide from Lupinus angustifolius L. prevents inflammation in microglial cells and confers neuroprotection in brain. Nutr. Neurosci., 2022, 25(3), 472-484. doi: 10.1080/1028415X.2020.1763058 PMID: 32401697
  111. Yang, S.; Kawamura, Y.; Yoshikawa, M. Effect of rubiscolin, a δ opioid peptide derived from Rubisco, on memory consolidation. Peptides, 2003, 24(2), 325-328. doi: 10.1016/S0196-9781(03)00044-5 PMID: 12668220
  112. Yoshikawa, M. Bioactive peptides derived from natural proteins with respect to diversity of their receptors and physiological effects. Peptides, 2015, 72, 208-225. doi: 10.1016/j.peptides.2015.07.013 PMID: 26297549
  113. Mitsumoto, Y.; Sato, R.; Tagawa, N.; Kato, I. Rubiscolin-6, a δ-opioid peptide from spinach RuBisCO, exerts antidepressant-like effect in restraint-stressed mice. J. Nutr. Sci. Vitaminol. (Tokyo), 2019, 65(2), 202-204. doi: 10.3177/jnsv.65.202 PMID: 31061291
  114. Perlikowska, R.; Silva, J.; Alves, C.; Susano, P.; Pedrosa, R. The therapeutic potential of naturally occurring peptides in counteracting SH-SY5Y cells injury. Int. J. Mol. Sci., 2022, 23(19), 1-18.
  115. Wang, L.; Wang, N.; Zhang, W.; Cheng, X.; Yan, Z.; Shao, G.; Wang, X.; Wang, R.; Fu, C. Therapeutic peptides: current applications and future directions. Signal Transduct. Target. Ther., 2022, 7(1), 48. doi: 10.1038/s41392-022-00904-4 PMID: 35165272
  116. Baig, M.H.; Ahmad, K.; Saeed, M.; Alharbi, A.M.; Barreto, G.E.; Ashraf, G.M.; Choi, I. Peptide based therapeutics and their use for the treatment of neurodegenerative and other diseases. Biomed. Pharmacother., 2018, 103, 574-581. doi: 10.1016/j.biopha.2018.04.025 PMID: 29677544
  117. MRC Clinical Trials Unit at UCL, Our Research: Neurodegenerative diseases. Available from: https://www.mrcctu.ucl.ac.uk/our-research/neurodegenerative-diseases/ (Accessed August 11, 2023).
  118. US National Library of Medicine, Clinical Trials Available from: https://clinicaltrials.gov/ct2/results?cond=Neurodegenerative+Diseases&term=neurodegeneration&cntry=&state=&city=&dist= (Accessed August 11, 2023).
  119. US National Library of Medicine, Clinical Trials: Safety Study of CN-105 Neuroprotective Peptide for Intracerebral Hemorrhage. Available from: https://clinicaltrials.gov/ct2/show/NCT02670824 (Accessed August 11, 2023).
  120. Wang, H.; Faw, T.D.; Lin, Y.; Huang, S.; Venkatraman, T.N.; Cantillana, V.; Lascola, C.D.; James, M.L.; Laskowitz, D.T. Neuroprotective pentapeptide, CN-105, improves outcomes in translational models of intracerebral hemorrhage. Neurocrit. Care, 2021, 35(2), 441-450. doi: 10.1007/s12028-020-01184-y PMID: 33474632
  121. Weisgraber, K.H. Apolipoprotein E: structure-function relationships. Adv. Protein Chem., 1994, 45, 249-302. doi: 10.1016/S0065-3233(08)60642-7 PMID: 8154371
  122. James, M.L.; Komisarow, J.M.; Wang, H.; Laskowitz, D.T. Therapeutic development of apolipoprotein E mimetics for acute brain injury: Augmenting endogenous responses to reduce secondary injury. Neurotherapeutics, 2020, 17(2), 475-483. doi: 10.1007/s13311-020-00858-x PMID: 32318912
  123. James, M.L.; Sullivan, P.M.; Lascola, C.D.; Vitek, M.P.; Laskowitz, D.T. Pharmacogenomic effects of apolipoprotein e on intracerebral hemorrhage. Stroke, 2009, 40(2), 632-639. doi: 10.1161/STROKEAHA.108.530402 PMID: 19109539
  124. Li, S.; Wangqin, R.; Meng, X.; Li, H.; Wang, Y.; Wang, H.; Laskowitz, D.; Chen, X.; Wang, Y. Tolerability and pharmacokinetics of single escalating and repeated doses of CN-105 in healthy participants. Clin. Ther., 2022, 44(5), 744-754. doi: 10.1016/j.clinthera.2022.03.006 PMID: 35562205
  125. Yenjerla, M.; LaPointe, N.E.; Lopus, M.; Cox, C.; Jordan, M.A.; Feinstein, S.C.; Wilson, L. The neuroprotective peptide NAP does not directly affect polymerization or dynamics of reconstituted neural microtubules. J. Alzheimers Dis., 2010, 19(4), 1377-1386. doi: 10.3233/JAD-2010-1335 PMID: 20061604
  126. Gozes, I.; Morimoto, B.H.; Tiong, J.; Fox, A.; Sutherland, K.; Dangoor, D.; Holser-Cochav, M.; Vered, K.; Newton, P.; Aisen, P.S.; Matsuoka, Y.; Dyck, C.H.; Thal, L. NAP: research and development of a peptide derived from activity-dependent neuroprotective protein (ADNP). CNS Drug Rev., 2005, 11(4), 353-368. doi: 10.1111/j.1527-3458.2005.tb00053.x PMID: 16614735
  127. Geerts, H. AL-108 and AL-208, formulations of the neuroprotective NAP fragment of activity-dependent neuroprotective protein, for cognitive disorders. Curr. Opin. Investig. Drugs, 2008, 9(7), 800-811. PMID: 18600585
  128. US National Library of Medicine, Clinical Trials: Study to Evaluate the Safety and Efficacy of Davunetide for the Treatment of Progressive Supranuclear Palsy. Available from: https://clinicaltrials.gov/ct2/show/NCT01110720 (Accessed August 11, 2023).
  129. Zemlyak, I.; Furman, S.; Brenneman, D.E.; Gozes, I. A Novel peptide prevents death in enriched neuronal cultures. Regul. Pept., 2000, 96(1-2), 39-43. doi: 10.1016/S0167-0115(00)00198-1 PMID: 11102650
  130. Vulih-Shultzman, I.; Pinhasov, A.; Mandel, S.; Grigoriadis, N.; Touloumi, O.; Pittel, Z.; Gozes, I. Activity-dependent neuroprotective protein snippet NAP reduces tau hyperphosphorylation and enhances learning in a novel transgenic mouse model. J. Pharmacol. Exp. Ther., 2007, 323(2), 438-449. doi: 10.1124/jpet.107.129551 PMID: 17720885
  131. Alzforum, Networking for a Cure, Clinical Trials: Davunetide. Available from: https://www.alzforum.org/therapeutics/davunetide (Accessed August 11, 2023).
  132. Boxer, A.L.; Lang, A.E.; Grossman, M.; Knopman, D.S.; Miller, B.L.; Schneider, L.S.; Doody, R.S.; Lees, A.; Golbe, L.I.; Williams, D.R.; Corvol, J.C.; Ludolph, A.; Burn, D.; Lorenzl, S.; Litvan, I.; Roberson, E.D.; Höglinger, G.U.; Koestler, M.; Jack, C.R., Jr; Van Deerlin, V.; Randolph, C.; Lobach, I.V.; Heuer, H.W.; Gozes, I.; Parker, L.; Whitaker, S.; Hirman, J.; Stewart, A.J.; Gold, M.; Morimoto, B.H. Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial. Lancet Neurol., 2014, 13(7), 676-685. doi: 10.1016/S1474-4422(14)70088-2 PMID: 24873720

补充文件

附件文件
动作
1. JATS XML

版权所有 © Bentham Science Publishers, 2024