Login Register Cart 0
Generic placeholder image

CNS & Neurological Disorders - Drug Targets

Editor-in-Chief

ISSN (Print): 1871-5273
ISSN (Online): 1996-3181

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Review Article

Rationalizing the Use of Polyphenol Nano-formulations in the Therapy of Neurodegenerative Diseases

Author(s): Namrata Kumari, Nagarjuna Daram, Md. Sabir Alam and Anita Kamra Verma*

Volume 21, Issue 10, 2022

Published on: 30 June, 2022

Page: [966 - 976] Pages: 11

DOI: 10.2174/1871527321666220512153854

Price: $65

Abstract

Neurodegenerative diseases are a heterogeneous group of disorders among aging populations worldwide characterized by the progressive degeneration of the structure and function of brain cells and the nervous system. Alzheimer's disease and Parkinson's disease are common neurodegenerative diseases (NDs). Classic pathological features of AD are the accumulation of the amyloid betaprotein and aggregates of hyperphosphorylated tau protein around the brain cells. Dopaminergic neuronal death in the midbrain and accumulation of α- synuclein in the neurons are the hallmark of Parkinson’s disease. The pathogenesis is multifactorial, and both neurodegenerative disorders have complex etiology. Oxidative stress closely linked with mitochondrial dysfunction, excitotoxicity, nitric oxide toxicity, and neuro-inflammation, is anticipated to trigger neuronal death. Ample evidence has implicated that oxidative stress and inflammation contribute to the pathology of neurodegeneration in AD and PD. Currently, acetylcholinesterase inhibitors are the main treatment option for AD, while L-DOPA is the gold standard therapy for PD. Along with the main therapy, many endogenous antioxidants, like vitamin E, selenium, etc., are also given to the patients to combat oxidative stress. Current treatment for these NDs is limited due to the blood-brain barrier (BBB) that hinders drug targeting towards neurons. In this review, we emphasize adjunct treatment with anti-inflammatory agents that act at the site of the disease and can halt the disease progression by attenuating the effect of ROS triggering neuro-inflammatory response. Polyphenols, either as purified compounds or extracts from various natural plant sources, have been well studied and documented for anti-inflammatory effects, but their use for ND is limited due to their physicochemical attributes. Nanoparticle-mediated drug delivery system exhibits immense potential to overcome these hurdles in drug delivery to the CNS, enabling nanoparticle-based therapies to directly target the inflammation and release bioactive compounds with anti-inflammatory properties to the site of action.

Keywords: Neurodegeneration, Alzheimer's disease, Parkinson's disease, polyphenols, nanoformulations, oxidative stress, neuroinflammation.

« Previous Next »
Graphical Abstract

[1]
Dugger BN, Dickson DW. Pathology of neurodegenerative diseases. Cold Spring Harb Perspect Biol 2017; 9(7): a028035.
[http://dx.doi.org/10.1101/cshperspect.a028035] [PMID: 28062563]
[2]
National institute of environmental health sciences Neurodegenerative diseases 2021. Available from: https://www.niehs.nih.gov/research/supported/health/neurodegenerative/index.cfm
[3]
Scheibye-Knudsen M. Neurodegeneration in accelerated aging. Dan Med J 2016; 63(11): B5308.
[PMID: 27808039]
[4]
Goldman JG, Postuma R. Premotor and nonmotor features of Parkinson’s disease. Curr Opin Neurol 2014; 27(4): 434-41.
[http://dx.doi.org/10.1097/WCO.0000000000000112] [PMID: 24978368]
[5]
National institute of ageing - symptoms of Parkinsons's disease 2017. Available from: https://www.nia.nih.gov/health/parkinsons-disease
[6]
Prince MJ. WA, Guerchet MM, Ali G-C, Wu Y-T, Prina AM Alzheimer’s disease international World Alzheimer Report 2015: The Glob-al Impact of Dementia: An Analysis of Prevalence, Incidence, Cost and Trends. London: Alzheimer’s Disease International 2015.
[7]
Marras C, Beck JC, Bower JH, et al. Prevalence of Parkinson’s disease across North America. NPJ Parkinsons Dis 2018; 4(1): 21.
[http://dx.doi.org/10.1038/s41531-018-0058-0] [PMID: 30003140]
[8]
Kowal SL, Dall TM, Chakrabarti R, Storm MV, Jain A. The current and projected economic burden of Parkinson’s disease in the United States. Mov Disord 2013; 28(3): 311-8.
[http://dx.doi.org/10.1002/mds.25292] [PMID: 23436720]
[9]
Querfurth HW, LaFerla FM. Alzheimer’s disease. N Engl J Med 2010; 362(4): 329-44.
[http://dx.doi.org/10.1056/NEJMra0909142] [PMID: 20107219]
[10]
Dauer W, Przedborski S. Parkinson’s disease: Mechanisms and models. Neuron 2003; 39(6): 889-909.
[http://dx.doi.org/10.1016/S0896-6273(03)00568-3] [PMID: 12971891]
[11]
Tembhurnikar HJ. TN, Patil RJ, Das RK. Review on various factors responsible for neurodegenerative disorders GSC Biol Pharma Sci 2021; 2021: 126-32.
[12]
Roberts JS, Patterson AK, Uhlmann WR. Genetic testing for neurodegenerative diseases: Ethical and health communication challenges. Neurobiol Dis 2020; 141: 104871.
[http://dx.doi.org/10.1016/j.nbd.2020.104871] [PMID: 32302673]
[13]
Moujalled D, Strasser A, Liddell JR. Molecular mechanisms of cell death in neurological diseases. Cell Death Differ 2021; 28(7): 2029-44.
[http://dx.doi.org/10.1038/s41418-021-00814-y] [PMID: 34099897]
[14]
Gandhi S, Abramov AY. Mechanism of oxidative stress in neurodegeneration. Oxidative medicine and cellular longevity 2012; 2012: 428010.
[http://dx.doi.org/10.1155/2012/428010]
[15]
Rekatsina M, Paladini A, Piroli A, Zis P, Pergolizzi JV, Varrassi G. Pathophysiology and therapeutic perspectives of oxidative stress and neurodegenerative diseases: A narrative review. Adv Ther 2020; 37(1): 113-39.
[http://dx.doi.org/10.1007/s12325-019-01148-5] [PMID: 31782132]
[16]
Hansen RA, Gartlehner G, Webb AP, Morgan LC, Moore CG, Jonas DE. Efficacy and safety of donepezil, galantamine, and rivastigmine for the treatment of Alzheimer’s disease: A systematic review and meta-analysis. Clin Interv Aging 2008; 3(2): 211-25.
[PMID: 18686744]
[17]
Lloyd KG, Davidson L, Hornykiewicz O. The neurochemistry of Parkinson’s disease: Effect of L-dopa therapy. J Pharmacol Exp Ther 1975; 195(3): 453-64.
[PMID: 489]
[18]
National Center for Complementary and Integrative Health. Antioxidants: In Depth 2013. Available from: https://www.nccih.nih.gov/health/antioxidants-in-depth
[19]
Lobo V, Patil A, Phatak A, Chandra N. Free radicals, antioxidants and functional foods: Impact on human health. Pharmacogn Rev 2010; 4(8): 118-26.
[http://dx.doi.org/10.4103/0973-7847.70902] [PMID: 22228951]
[20]
Engwa GA. Free radicals and the role of plant phytochemicals as antioxidants against oxidative stress-related diseases. Phytochemicals 2018; 7: 49-74.
[http://dx.doi.org/10.5772/intechopen.76719]
[21]
Tsao R. Chemistry and biochemistry of dietary polyphenols. Nutrients 2010; 2(12): 1231-46.
[http://dx.doi.org/10.3390/nu2121231] [PMID: 22254006]
[22]
Gao S, Hu M. Bioavailability challenges associated with development of anti-cancer phenolics. Mini Rev Med Chem 2010; 10(6): 550-67.
[http://dx.doi.org/10.2174/138955710791384081] [PMID: 20370701]
[23]
Umeno A, Biju V, Yoshida Y. in vivo ROS production and use of oxidative stress-derived biomarkers to detect the onset of diseases such as Alzheimer’s disease, Parkinson’s disease, and diabetes. Free Radic Res 2017; 51(4): 413-27.
[http://dx.doi.org/10.1080/10715762.2017.1315114] [PMID: 28372523]
[24]
Maher P, Hanneken A. The molecular basis of oxidative stress-induced cell death in an immortalized retinal ganglion cell line. Invest Ophthalmol Vis Sci 2005; 46(2): 749-57.
[http://dx.doi.org/10.1167/iovs.04-0883] [PMID: 15671309]
[25]
Zorov DB, Juhaszova M, Sollott SJ. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. Physiol Rev 2014; 94(3): 909-50.
[http://dx.doi.org/10.1152/physrev.00026.2013] [PMID: 24987008]
[26]
Bolisetty S, Jaimes EA. Mitochondria and reactive oxygen species: Physiology and pathophysiology. Int J Mol Sci 2013; 14(3): 6306-44.
[http://dx.doi.org/10.3390/ijms14036306] [PMID: 23528859]
[27]
Olanow CW, Stern MB, Sethi K. The scientific and clinical basis for the treatment of Parkinson disease. Neurology 2009; 72(21)(Suppl. 4): S1-S136.
[http://dx.doi.org/10.1212/WNL.0b013e3181a1d44c] [PMID: 19470958]
[28]
Parker WD Jr, Parks JK, Swerdlow RH. Complex I deficiency in Parkinson’s disease frontal cortex. Brain Res 2008; 1189: 215-8.
[http://dx.doi.org/10.1016/j.brainres.2007.10.061] [PMID: 18061150]
[29]
Jenner P. Oxidative stress in Parkinson’s disease. Ann Neurol 2003; 53(Suppl. 3): S26-36.
[http://dx.doi.org/10.1002/ana.10483] [PMID: 12666096]
[30]
Zhang J, Perry G, Smith MA, et al. Parkinson’s disease is associated with oxidative damage to cytoplasmic DNA and RNA in substantia nigra neurons. Am J Pathol 1999; 154(5): 1423-9.
[http://dx.doi.org/10.1016/S0002-9440(10)65396-5] [PMID: 10329595]
[31]
Alam ZI, Jenner A, Daniel SE, et al. Oxidative DNA damage in the parkinsonian brain: An apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J Neurochem 1997; 69(3): 1196-203.
[http://dx.doi.org/10.1046/j.1471-4159.1997.69031196.x] [PMID: 9282943]
[32]
Gamber KM. Animal models of Parkinson’s disease: New models provide greater translational and predictive value. Biotechniques 2016; 61(4): 210-1.
[http://dx.doi.org/10.2144/000114463]
[33]
Duty S, Jenner P. Animal models of Parkinson’s disease: A source of novel treatments and clues to the cause of the disease. Br J Pharmacol 2011; 164(4): 1357-91.
[http://dx.doi.org/10.1111/j.1476-5381.2011.01426.x] [PMID: 21486284]
[34]
Richardson JR, Quan Y, Sherer TB, Greenamyre JT, Miller GW. Paraquat neurotoxicity is distinct from that of MPTP and rotenone. Toxicol Sci 2005; 88(1): 193-201.
[http://dx.doi.org/10.1093/toxsci/kfi304] [PMID: 16141438]
[35]
Liu X, Yamada N, Maruyama W, Osawa T. Formation of dopamine adducts derived from brain polyunsaturated fatty acids: Mechanism for Parkinson disease. J Biol Chem 2008; 283(50): 34887-95.
[http://dx.doi.org/10.1074/jbc.M805682200] [PMID: 18922792]
[36]
Gibson GE, Huang HM. Mitochondrial enzymes and endoplasmic reticulum calcium stores as targets of oxidative stress in neurodegen-erative diseases. J Bioenerg Biomembr 2004; 36(4): 335-40.
[http://dx.doi.org/10.1023/B:JOBB.0000041764.45552.f3] [PMID: 15377868]
[37]
Munoz P, Huenchuguala S, Paris I, Segura-Aguilar J. Dopamine oxidation and autophagy. Parkinsons Dis 2012; 2012: 920953.
[38]
Schapira AH, Jenner P. Etiology and pathogenesis of Parkinson’s disease. Mov Disord 2011; 26(6): 1049-55.
[http://dx.doi.org/10.1002/mds.23732] [PMID: 21626550]
[39]
Jenner P, Langston JW. Explaining ADAGIO: A critical review of the biological basis for the clinical effects of rasagiline. Mov Disord 2011; 26(13): 2316-23.
[http://dx.doi.org/10.1002/mds.23926] [PMID: 21953831]
[40]
Youdim MB, Edmondson D, Tipton KF. The therapeutic potential of monoamine oxidase inhibitors. Nat Rev Neurosci 2006; 7(4): 295-309.
[http://dx.doi.org/10.1038/nrn1883] [PMID: 16552415]
[41]
Kumar MJ, Andersen JK. Perspectives on MAO-B in aging and neurological disease: Where do we go from here? Mol Neurobiol 2004; 30(1): 77-89.
[http://dx.doi.org/10.1385/MN:30:1:077] [PMID: 15247489]
[42]
Segura-Aguilar J, Huenchuguala S. Aminochrome induces irreversible mitochondrial dysfunction by inducing autophagy dysfunction in Parkinson’s disease. Front Neurosci 2018; 12: 106-6.
[http://dx.doi.org/10.3389/fnins.2018.00106] [PMID: 29593482]
[43]
Norris EH, Giasson BI, Hodara R, et al. Reversible inhibition of α-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J Biol Chem 2005; 280(22): 21212-9.
[http://dx.doi.org/10.1074/jbc.M412621200] [PMID: 15817478]
[44]
Zecca L, Wilms H, Geick S, et al. Human neuromelanin induces neuroinflammation and neurodegeneration in the rat substantia nigra: Implications for Parkinson’s disease. Acta Neuropathol 2008; 116(1): 47-55.
[http://dx.doi.org/10.1007/s00401-008-0361-7] [PMID: 18343932]
[45]
Montine K, Morrow JD, Montine TJ. Isoprostanes and related products of lipid peroxidation in neurodegenerative diseases. Chem Phys Lipids 2004; 128: 117.
[http://dx.doi.org/10.1016/j.chemphyslip.2003.10.010] [PMID: 15037157]
[46]
Montine TJ, Neely MD, Quinn JF, et al. Lipid peroxidation in aging brain and Alzheimer’s disease. Free Radic Biol Med 2002; 33(5): 620-6.
[http://dx.doi.org/10.1016/S0891-5849(02)00807-9] [PMID: 12208348]
[47]
Mattson MP. Metal-catalyzed disruption of membrane protein and lipid signaling in the pathogenesis of neurodegenerative disorders. Ann N Y Acad Sci 2004; 1012(1): 37-50.
[http://dx.doi.org/10.1196/annals.1306.004] [PMID: 15105254]
[48]
Liu W, Kato M, Akhand AA, et al. 4-hydroxynonenal induces a cellular redox status-related activation of the caspase cascade for apop-totic cell death. J Cell Sci 2000; 113(Pt 4): 635-41.
[http://dx.doi.org/10.1242/jcs.113.4.635] [PMID: 10652256]
[49]
Ellis JM, Fell MJ. Current approaches to the treatment of Parkinson’s disease. Bioorg Med Chem Lett 2017; 27(18): 4247-55.
[http://dx.doi.org/10.1016/j.bmcl.2017.07.075] [PMID: 28869077]
[50]
Smith Y, Wichmann T, Factor SA, DeLong MR. Parkinson’s disease therapeutics: New developments and challenges since the introduc-tion of levodopa. Neuropsychopharmacology 2012; 37(1): 213-46.
[http://dx.doi.org/10.1038/npp.2011.212] [PMID: 21956442]
[51]
Brocks DR. Anticholinergic drugs used in Parkinson’s disease: An overlooked class of drugs from a pharmacokinetic perspective. J Pharm Pharm Sci 1999; 2(2): 39-46.
[PMID: 10952768]
[52]
Katzenschlager R, Sampaio C, Costa J, Lees A. Anticholinergics for symptomatic management of Parkinson’s disease. Cochrane Database Syst Rev 2003; 2003(2): CD003735.
[PMID: 12804486]
[53]
Silva RFM, Pogačnik L. Food, polyphenols and neuroprotection. Neural Regen Res 2017; 12(4): 582-3.
[http://dx.doi.org/10.4103/1673-5374.205096] [PMID: 28553336]
[54]
Winslow BT, Onysko MK, Stob CM, Hazlewood KA. Treatment of Alzheimer disease. Am Fam Physician 2011; 83(12): 1403-12.
[PMID: 21671540]
[55]
Robinson DM, Keating GM. Memantine: A review of its use in Alzheimer’s disease. Drugs 2006; 66(11): 1515-34.
[http://dx.doi.org/10.2165/00003495-200666110-00015] [PMID: 16906789]
[56]
van Marum RJ. Update on the use of memantine in Alzheimer’s disease. Neuropsychiatr Dis Treat 2009; 5: 237-47.
[http://dx.doi.org/10.2147/NDT.S4048] [PMID: 19557118]
[57]
Wang R, Zhang Y, Li J, Zhang C. Resveratrol ameliorates spatial learning memory impairment induced by Aβ1-42 in rats. Neuroscience 2017; 344: 39-47.
[http://dx.doi.org/10.1016/j.neuroscience.2016.08.051] [PMID: 27600946]
[58]
Silva RFM, Pogačnik L. Polyphenols from food and natural products: Neuroprotection and safety. Antioxidants 2020; 9(1): E61.
[http://dx.doi.org/10.3390/antiox9010061] [PMID: 31936711]
[59]
Pandareesh MD, Mythri RB, Srinivas Bharath MM. Bioavailability of dietary polyphenols: Factors contributing to their clinical applica-tion in CNS diseases. Neurochem Int 2015; 89: 198-208.
[http://dx.doi.org/10.1016/j.neuint.2015.07.003] [PMID: 26163045]
[60]
Vauzour D, Corona G, Spencer JP. Caffeic acid, tyrosol and p-coumaric acid are potent inhibitors of 5-S-cysteinyl-dopamine induced neurotoxicity. Arch Biochem Biophys 2010; 501(1): 106-11.
[http://dx.doi.org/10.1016/j.abb.2010.03.016] [PMID: 20361927]
[61]
Wang R, Li YH, Xu Y, et al. Curcumin produces neuroprotective effects via activating brain-derived neurotrophic factor/TrkB-dependent MAPK and PI-3K cascades in rodent cortical neurons. Prog Neuropsychopharmacol Biol Psychiatry 2010; 34(1): 147-53.
[http://dx.doi.org/10.1016/j.pnpbp.2009.10.016] [PMID: 19879308]
[62]
Loureiro JA, Andrade S, Duarte A, et al. Resveratrol and grape extract-loaded solid lipid nanoparticles for the treatment of Alzheimer’s disease. Molecules 2017; 22(2): 277.
[http://dx.doi.org/10.3390/molecules22020277] [PMID: 28208831]
[63]
Rezai-Zadeh K, Arendash GW, Hou H, et al. Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impair-ment and modulates tau pathology in Alzheimer transgenic mice. Brain Res 2008; 1214: 177-87.
[http://dx.doi.org/10.1016/j.brainres.2008.02.107] [PMID: 18457818]
[64]
Vauzour D, Rodriguez-Mateos A, Corona G, Oruna-Concha MJ, Spencer JP. Polyphenols and human health: Prevention of disease and mechanisms of action. Nutrients 2010; 2(11): 1106-31.
[http://dx.doi.org/10.3390/nu2111106] [PMID: 22254000]
[65]
Hajieva P. The effect of polyphenols on protein degradation pathways: Implications for neuroprotection. Molecules 2017; 22(1): E159.
[http://dx.doi.org/10.3390/molecules22010159] [PMID: 28106854]
[66]
Shukitt-Hale B, Lau FC, Carey AN, et al. Blueberry polyphenols attenuate kainic acid-induced decrements in cognition and alter inflam-matory gene expression in rat hippocampus. Nutr Neurosci 2008; 11(4): 172-82.
[http://dx.doi.org/10.1179/147683008X301487] [PMID: 18681986]
[67]
Jung M, Triebel S, Anke T, Richling E, Erkel G. Influence of apple polyphenols on inflammatory gene expression. Mol Nutr Food Res 2009; 53(10): 1263-80.
[http://dx.doi.org/10.1002/mnfr.200800575] [PMID: 19764067]
[68]
Zhang L, Fang Y, Xu Y, et al. Curcumin improves amyloid β-peptide (1-42) induced spatial memory deficits through BDNF-ERK signal-ing pathway. PLoS One 2015; 10(6): e0131525.
[http://dx.doi.org/10.1371/journal.pone.0131525] [PMID: 26114940]
[69]
Zheng K, Dai X, Xiao N, et al. Curcumin ameliorates memory decline via inhibiting BACE1 expression and β-Amyloid pathology in 5× FAD transgenic mice. Mol Neurobiol 2017; 54(3): 1967-77.
[http://dx.doi.org/10.1007/s12035-016-9802-9] [PMID: 26910813]
[70]
Wang Y-L, Ju B, Zhang YZ, et al. Protective effect of curcumin against oxidative stress-induced injury in rats with parkinson’s disease through the Wnt/β-catenin signaling pathway. Cell Physiol Biochem 2017; 43(6): 2226-41.
[http://dx.doi.org/10.1159/000484302] [PMID: 29069652]
[71]
Salehi B, Mishra AP, Nigam M, et al. Resveratrol: A double-edged sword in health benefits. Biomedicines 2018; 6(3): 91.
[http://dx.doi.org/10.3390/biomedicines6030091] [PMID: 30205595]
[72]
Huang T-C, Lu KT, Wo YY, Wu YJ, Yang YL. Resveratrol protects rats from Aβ-induced neurotoxicity by the reduction of iNOS ex-pression and lipid peroxidation. PLoS One 2011; 6(12): e29102.
[http://dx.doi.org/10.1371/journal.pone.0029102] [PMID: 22220203]
[73]
Feng Y, Wang XP, Yang SG, et al. Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation. Neurotoxicology 2009; 30(6): 986-95.
[http://dx.doi.org/10.1016/j.neuro.2009.08.013] [PMID: 19744518]
[74]
Abraham J, Johnson RW. Consuming a diet supplemented with resveratrol reduced infection-related neuroinflammation and deficits in working memory in aged mice. Rejuvenation Res 2009; 12(6): 445-53.
[http://dx.doi.org/10.1089/rej.2009.0888] [PMID: 20041738]
[75]
Zhao YN, Li WF, Li F, et al. Resveratrol improves learning and memory in normally aged mice through microRNA-CREB pathway. Biochem Biophys Res Commun 2013; 435(4): 597-602.
[http://dx.doi.org/10.1016/j.bbrc.2013.05.025] [PMID: 23685142]
[76]
Donmez G, Outeiro TF. SIRT1 and SIRT2: Emerging targets in neurodegeneration. EMBO Mol Med 2013; 5(3): 344-52.
[http://dx.doi.org/10.1002/emmm.201302451] [PMID: 23417962]
[77]
Khan MM, Ahmad A, Ishrat T, et al. Resveratrol attenuates 6-hydroxydopamine-induced oxidative damage and dopamine depletion in rat model of Parkinson’s disease. Brain Res 2010; 1328: 139-51.
[http://dx.doi.org/10.1016/j.brainres.2010.02.031] [PMID: 20167206]
[78]
Mitchell MJ, Billingsley MM, Haley RM, Wechsler ME, Peppas NA, Langer R. Engineering precision nanoparticles for drug delivery. Nat Rev Drug Discov 2021; 20(2): 101-24.
[http://dx.doi.org/10.1038/s41573-020-0090-8] [PMID: 33277608]
[79]
Salehi B, Machin L, Monzote L, et al. Therapeutic potential of quercetin: New insights and perspectives for human health. ACS Omega 2020; 5(20): 11849-72.
[http://dx.doi.org/10.1021/acsomega.0c01818] [PMID: 32478277]
[80]
Jiménez-Aliaga K, Bermejo-Bescós P, Benedí J, Martín-Aragón S. Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells. Life Sci 2011; 89(25-26): 939-45.
[http://dx.doi.org/10.1016/j.lfs.2011.09.023] [PMID: 22008478]
[81]
Wang SW, Wang YJ, Su YJ, et al. Rutin inhibits β-amyloid aggregation and cytotoxicity, attenuates oxidative stress, and decreases the production of nitric oxide and proinflammatory cytokines. Neurotoxicology 2012; 33(3): 482-90.
[http://dx.doi.org/10.1016/j.neuro.2012.03.003] [PMID: 22445961]
[82]
Zhang X, Hu J, Zhong L, et al. Quercetin stabilizes apolipoprotein E and reduces brain Aβ levels in amyloid model mice. Neuropharmacology 2016; 108: 179-92.
[http://dx.doi.org/10.1016/j.neuropharm.2016.04.032] [PMID: 27114256]
[83]
Sabogal-Guáqueta AM, Muñoz-Manco JI, Ramírez-Pineda JR, Lamprea-Rodriguez M, Osorio E, Cardona-Gómez GP. The flavonoid quercetin ameliorates Alzheimer’s disease pathology and protects cognitive and emotional function in aged triple transgenic Alzheimer’s disease model mice. Neuropharmacology 2015; 93: 134-45.
[http://dx.doi.org/10.1016/j.neuropharm.2015.01.027] [PMID: 25666032]
[84]
Lv C, Hong T, Yang Z, et al. Effect of quercetin in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced mouse model of Parkin-son’s disease. Evid Based Complement Alternat Med 2012; 2012: 928643.
[85]
Qureshi AA, Tan X, Reis JC, et al. Inhibition of nitric oxide in LPS-stimulated macrophages of young and senescent mice by δ-tocotrienol and quercetin. Lipids Health Dis 2011; 10(1): 239.
[http://dx.doi.org/10.1186/1476-511X-10-239] [PMID: 22185406]
[86]
Singh NA, Mandal AKA, Khan ZA. Potential neuroprotective properties of epigallocatechin-3-gallate (EGCG). Nutr J 2016; 15(1): 60.
[http://dx.doi.org/10.1186/s12937-016-0179-4] [PMID: 27268025]
[87]
Okello EJ, Leylabi R, McDougall GJ. Inhibition of acetylcholinesterase by green and white tea and their simulated intestinal metabolites. Food Funct 2012; 3(6): 651-61.
[http://dx.doi.org/10.1039/c2fo10174b] [PMID: 22418730]
[88]
Qin X-Y, Cheng Y, Yu L-C. Potential protection of green tea polyphenols against intracellular amyloid beta-induced toxicity on primary cultured prefrontal cortical neurons of rats. Neurosci Lett 2012; 513(2): 170-3.
[http://dx.doi.org/10.1016/j.neulet.2012.02.029] [PMID: 22381400]
[89]
Ortiz-López L, Márquez-Valadez B, Gómez-Sánchez A, et al. Green tea compound epigallo-catechin-3-gallate (EGCG) increases neu-ronal survival in adult hippocampal neurogenesis in vivo and in vitro. Neuroscience 2016; 322: 208-20.
[http://dx.doi.org/10.1016/j.neuroscience.2016.02.040] [PMID: 26917271]
[90]
Gong EJ, Park HR, Kim ME, et al. Morin attenuates tau hyperphosphorylation by inhibiting GSK3β. Neurobiol Dis 2011; 44(2): 223-30.
[http://dx.doi.org/10.1016/j.nbd.2011.07.005] [PMID: 21782947]
[91]
Mori T, Rezai-Zadeh K, Koyama N, et al. Tannic acid is a natural β-secretase inhibitor that prevents cognitive impairment and mitigates Alzheimer-like pathology in transgenic mice. J Biol Chem 2012; 287(9): 6912-27.
[http://dx.doi.org/10.1074/jbc.M111.294025] [PMID: 22219198]
[92]
Li J, Ye L, Wang X, et al. (-)-Epigallocatechin gallate inhibits endotoxin-induced expression of inflammatory cytokines in human cere-bral microvascular endothelial cells. J Neuroinflammation 2012; 9(1): 161.
[http://dx.doi.org/10.1186/1742-2094-9-161] [PMID: 22768975]
[93]
D’Archivio M, Filesi C, Varì R, Scazzocchio B, Masella R. Bioavailability of the polyphenols: Status and controversies. Int J Mol Sci 2010; 11(4): 1321-42.
[http://dx.doi.org/10.3390/ijms11041321] [PMID: 20480022]
[94]
Frozza RL, Bernardi A, Paese K, et al. Characterization of trans-resveratrol-loaded lipid-core nanocapsules and tissue distribution stud-ies in rats. J Biomed Nanotechnol 2010; 6(6): 694-703.
[http://dx.doi.org/10.1166/jbn.2010.1161] [PMID: 21361135]
[95]
Lewandowska U, Szewczyk K, Hrabec E, Janecka A, Gorlach S. Overview of metabolism and bioavailability enhancement of polyphe-nols. J Agric Food Chem 2013; 61(50): 12183-99.
[http://dx.doi.org/10.1021/jf404439b] [PMID: 24295170]
[96]
Squillaro T, Cimini A, Peluso G, Giordano A, Melone MAB. Nano-delivery systems for encapsulation of dietary polyphenols: An exper-imental approach for neurodegenerative diseases and brain tumors. Biochem Pharmacol 2018; 154: 303-17.
[http://dx.doi.org/10.1016/j.bcp.2018.05.016] [PMID: 29803506]
[97]
Conte R, Calarco A, Napoletano A, et al. Polyphenols nanoencapsulation for therapeutic applications. J Biomol Res Ther 2016; 5(2): 1000139.
[98]
Anton N, Benoit J-P, Saulnier P. Design and production of nanoparticles formulated from nano-emulsion templates-a review. J Control Release 2008; 128(3): 185-99.
[http://dx.doi.org/10.1016/j.jconrel.2008.02.007] [PMID: 18374443]
[99]
Kothamasu P, Kanumur H, Ravur N, Maddu C, Parasuramrajam R, Thangavel S. Nanocapsules: The weapons for novel drug delivery systems. Bioimpacts 2012; 2(2): 71-81.
[PMID: 23678444]
[100]
Jaiswal M, Dudhe R, Sharma PK. Nanoemulsion: An advanced mode of drug delivery system. 3 Biotech 2015; 5(2): 123-7.
[http://dx.doi.org/10.1007/s13205-014-0214-0]
[101]
Tiwari G, Tiwari R, Rai AK. Cyclodextrins in delivery systems: Applications. J Pharm Bioallied Sci 2010; 2(2): 72-9.
[http://dx.doi.org/10.4103/0975-7406.67003] [PMID: 21814436]
[102]
Szejtli J. Introduction and general overview of cyclodextrin chemistry. Chem Rev 1998; 98(5): 1743-54.
[http://dx.doi.org/10.1021/cr970022c] [PMID: 11848947]
[103]
Zhu X, Zeng X, Zhang X, et al. The effects of quercetin-loaded PLGA-TPGS nanoparticles on ultraviolet B-induced skin damages in vivo. Nanomedicine 2016; 12(3): 623-32.
[http://dx.doi.org/10.1016/j.nano.2015.10.016] [PMID: 26656634]
[104]
Cheng KK, Yeung CF, Ho SW, Chow SF, Chow AH, Baum L. Highly stabilized curcumin nanoparticles tested in an in vitro blood-brain barrier model and in Alzheimer’s disease Tg2576 mice. AAPS J 2013; 15(2): 324-36.
[http://dx.doi.org/10.1208/s12248-012-9444-4] [PMID: 23229335]
[105]
Maiti P, Hall TC, Paladugu L, et al. A comparative study of dietary curcumin, nanocurcumin, and other classical amyloid-binding dyes for labeling and imaging of amyloid plaques in brain tissue of 5×-familial Alzheimer’s disease mice. Histochem Cell Biol 2016; 146(5): 609-25.
[http://dx.doi.org/10.1007/s00418-016-1464-1] [PMID: 27406082]
[106]
Torchilin VP. Structure and design of polymeric surfactant-based drug delivery systems. J Control Release 2001; 73(2-3): 137-72.
[http://dx.doi.org/10.1016/S0168-3659(01)00299-1] [PMID: 11516494]
[107]
Naksuriya O, Okonogi S, Schiffelers RM, Hennink WE. Curcumin nanoformulations: A review of pharmaceutical properties and preclin-ical studies and clinical data related to cancer treatment. Biomaterials 2014; 35(10): 3365-83.
[http://dx.doi.org/10.1016/j.biomaterials.2013.12.090] [PMID: 24439402]
[108]
Yang F, Lim GP, Begum AN, et al. Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 2005; 280(7): 5892-901.
[http://dx.doi.org/10.1074/jbc.M404751200] [PMID: 15590663]
[109]
Sadegh Malvajerd S, Azadi A, Izadi Z, et al. Brain delivery of curcumin using solid lipid nanoparticles and nanostructured lipid carriers: Preparation, optimization, and pharmacokinetic evaluation. ACS Chem Neurosci 2019; 10(1): 728-39.
[http://dx.doi.org/10.1021/acschemneuro.8b00510] [PMID: 30335941]
[110]
Taylor M, Moore S, Mourtas S, et al. Effect of curcumin-associated and lipid ligand-functionalized nanoliposomes on aggregation of the Alzheimer’s Aβ peptide. Nanomedicine 2011; 7(5): 541-50.
[http://dx.doi.org/10.1016/j.nano.2011.06.015] [PMID: 21722618]
[111]
Barbara R, Belletti D, Pederzoli F, et al. Novel Curcumin loaded nanoparticles engineered for blood-brain barrier crossing and able to disrupt abeta aggregates. Int J Pharm 2017; 526(1-2): 413-24.
[http://dx.doi.org/10.1016/j.ijpharm.2017.05.015] [PMID: 28495580]
[112]
Djiokeng Paka G, Doggui S, Zaghmi A, et al. Neuronal uptake and neuroprotective properties of curcumin-loaded nanoparticles on SK-N-SH cell line: Role of poly (lactide-co-glycolide) polymeric matrix composition. Mol Pharm 2016; 13(2): 391-403.
[http://dx.doi.org/10.1021/acs.molpharmaceut.5b00611] [PMID: 26618861]
[113]
Del Prado-Audelo ML, Caballero-Florán IH, Meza-Toledo JA, et al. Formulations of curcumin nanoparticles for brain diseases. Biomolecules 2019; 9(2): 56.
[http://dx.doi.org/10.3390/biom9020056] [PMID: 30743984]
[114]
Yavarpour-Bali H, Ghasemi-Kasman M, Pirzadeh M. Curcumin-loaded nanoparticles: A novel therapeutic strategy in treatment of central nervous system disorders. Int J Nanomedicine 2019; 14: 4449-60.
[http://dx.doi.org/10.2147/IJN.S208332] [PMID: 31417253]
[115]
Tiwari SK, Agarwal S, Seth B, et al. Curcumin-loaded nanoparticles potently induce adult neurogenesis and reverse cognitive deficits in Alzheimer’s disease model via canonical Wnt/β-catenin pathway. ACS Nano 2014; 8(1): 76-103.
[http://dx.doi.org/10.1021/nn405077y] [PMID: 24467380]
[116]
Kundu P, Das M, Tripathy K, Sahoo SK. Delivery of dual drug loaded lipid based nanoparticles across the blood–brain barrier impart enhanced neuroprotection in a rotenone induced mouse model of Parkinson’s disease. ACS Chem Neurosci 2016; 7(12): 1658-70.
[http://dx.doi.org/10.1021/acschemneuro.6b00207] [PMID: 27642670]
[117]
Bollimpelli VS, Kumar P, Kumari S, Kondapi AK. Neuroprotective effect of curcumin-loaded lactoferrin nano particles against rotenone induced neurotoxicity. Neurochem Int 2016; 95: 37-45.
[http://dx.doi.org/10.1016/j.neuint.2016.01.006] [PMID: 26826319]
[118]
Zhang N, Yan F, Liang X, et al. Localized delivery of curcumin into brain with polysorbate 80-modified cerasomes by ultrasound-targeted microbubble destruction for improved Parkinson’s disease therapy. Theranostics 2018; 8(8): 2264-77.
[http://dx.doi.org/10.7150/thno.23734] [PMID: 29721078]
[119]
Ray B, Bisht S, Maitra A, Maitra A, Lahiri DK. Neuroprotective and neurorescue effects of a novel polymeric nanoparticle formulation of curcumin (NanoCurc™) in the neuronal cell culture and animal model: Implications for Alzheimer’s disease. J Alzheimers Dis 2011; 23(1): 61-77.
[http://dx.doi.org/10.3233/JAD-2010-101374] [PMID: 20930270]
[120]
Frozza RL, Bernardi A, Hoppe JB, et al. Lipid-core nanocapsules improve the effects of resveratrol against abeta-induced neuroinflam-mation. J Biomed Nanotechnol 2013; 9(12): 2086-104.
[http://dx.doi.org/10.1166/jbn.2013.1709] [PMID: 24266263]
[121]
Wang Y, Xu H, Fu Q, Ma R, Xiang J. Protective effect of resveratrol derived from Polygonum cuspidatum and its liposomal form on nigral cells in parkinsonian rats. J Neurol Sci 2011; 304(1-2): 29-34.
[http://dx.doi.org/10.1016/j.jns.2011.02.025] [PMID: 21376343]
[122]
da Rocha Lindner G, Bonfanti Santos D, Colle D, et al. Improved neuroprotective effects of resveratrol-loaded polysorbate 80-coated poly(lactide) nanoparticles in MPTP-induced Parkinsonism. Nanomedicine (Lond) 2015; 10(7): 1127-38.
[http://dx.doi.org/10.2217/nnm.14.165] [PMID: 25929569]
[123]
Pangeni R, Sharma S, Mustafa G, Ali J, Baboota S. Vitamin E loaded resveratrol nanoemulsion for brain targeting for the treatment of Parkinson’s disease by reducing oxidative stress. Nanotechnology 2014; 25(48): 485102.
[http://dx.doi.org/10.1088/0957-4484/25/48/485102] [PMID: 25392203]
[124]
Palle S, Neerati P. Improved neuroprotective effect of resveratrol nanoparticles as evinced by abrogation of rotenone-induced behavioral deficits and oxidative and mitochondrial dysfunctions in rat model of Parkinson’s disease. Naunyn Schmiedebergs Arch Pharmacol 2018; 391(4): 445-53.
[http://dx.doi.org/10.1007/s00210-018-1474-8] [PMID: 29411055]
[125]
Zu YG, Yuan S, Zhao XH, Zhang Y, Zhang XN, Jiang R. [Preparation, activity and targeting ability evaluation in vitro on folate mediated epigallocatechin-3-gallate albumin nanoparticles]. Yao Xue Xue Bao 2009; 44(5): 525-31.
[PMID: 19618731]
[126]
Ramesh N, Mandal AKA. Encapsulation of epigallocatechin-3- gallate into albumin nanoparticles improves pharmacokinetic and bioavailability in rat model. 3 Biotech 2019; 9(6): 238.
[http://dx.doi.org/10.1007/s13205-019-1772-y]
[127]
Kumar S, Pandey AK. Chemistry and biological activities of flavonoids: An overview. Sci World J 2013; 2013: 162750.
[http://dx.doi.org/10.1155/2013/162750] [PMID: 24470791]
[128]
Vijayakumar A, Baskaran R, Jang YS, Oh SH, Yoo BK. Quercetin-loaded solid lipid nanoparticle dispersion with improved physico-chemical properties and cellular uptake. AAPS PharmSciTech 2017; 18(3): 875-83.
[http://dx.doi.org/10.1208/s12249-016-0573-4] [PMID: 27368922]
[129]
Huo X, Zhang Y, Jin X, Li Y, Zhang L. A novel synthesis of selenium nanoparticles encapsulated PLGA nanospheres with curcumin molecules for the inhibition of amyloid β aggregation in Alzheimer’s disease. J Photochem Photobiol B 2019; 190: 98-102.
[http://dx.doi.org/10.1016/j.jphotobiol.2018.11.008] [PMID: 30504054]
[130]
Gao C, Chu X, Gong W, et al. Neuron tau-targeting biomimetic nanoparticles for curcumin delivery to delay progression of Alzheimer’s disease. J Nanobiotechnology 2020; 18(1): 71.
[http://dx.doi.org/10.1186/s12951-020-00626-1] [PMID: 32404183]
[131]
Yang R, Zheng Y, Wang Q, Zhao L. Curcumin-loaded chitosan-bovine serum albumin nanoparticles potentially enhanced Aβ 42 phago-cytosis and modulated macrophage polarization in Alzheimer’s disease. Nanoscale Res Lett 2018; 13(1): 330.
[http://dx.doi.org/10.1186/s11671-018-2759-z] [PMID: 30350003]
[132]
Kim MJ, Rehman SU, Amin FU, Kim MO. Enhanced neuroprotection of anthocyanin-loaded PEG-gold nanoparticles against Aβ1-42-induced neuroinflammation and neurodegeneration via the NF-KB/JNK/GSK3β signaling pathway. Nanomedicine 2017; 13(8): 2533-44.
[http://dx.doi.org/10.1016/j.nano.2017.06.022] [PMID: 28736294]
[133]
Lohan S, Raza K, Mehta SK, Bhatti GK, Saini S, Singh B. Anti-Alzheimer’s potential of berberine using surface decorated multi-walled carbon nanotubes: A preclinical evidence. Int J Pharm 2017; 530(1-2): 263-78.
[http://dx.doi.org/10.1016/j.ijpharm.2017.07.080] [PMID: 28774853]
[134]
Yin H, Si J, Xu H, et al. Resveratrol-loaded nanoparticles reduce oxidative stress induced by radiation or amyloid-beta in transgenic Caenorhabditis elegans. J Biomed Nanotechnol 2014; 10(8): 1536-44.
[http://dx.doi.org/10.1166/jbn.2014.1897] [PMID: 25016653]
[135]
Mohammad-Beigi H, Morshedi D, Shojaosadati SA, et al. Gallic acid loaded onto polyethylenimine-coated human serum albumin nano-particles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation. RSC Advances 2016; 6(88): 85312-23.
[http://dx.doi.org/10.1039/C6RA08502D]
[136]
Mourtas S, Canovi M, Zona C, et al. Curcumin-decorated nanoliposomes with very high affinity for amyloid-β1-42 peptide. Biomaterials 2011; 32(6): 1635-45.
[http://dx.doi.org/10.1016/j.biomaterials.2010.10.027] [PMID: 21131044]

Rights & Permissions Print Cite
Article Metrics
42
1
© 2024 Bentham Science Publishers | Privacy Policy