Design of PLGA-functionalized quercetin nanoparticles for potential use in Alzheimer's disease

Colloids and Surfaces B: Biointerfaces

Volumn 148, Issue , 2016, Pages 116-129

  Sun, Dongdong ^a   Li, Nuan ^a   Zhang, Weiwei ^a   Zhao, Zhiwei ^a   Mou, Zhipeng ^a   Huang, Donghui ^a   Liu, Jie ^b   Wang, Weiyun ^a  

^a ANHUI AGRICULTURAL UNIVERSITY   (China)

^b JINAN UNIVERSITY   (China)

Author keywords

Alzheimer's disease; Amyloid ; Nanoparticles; PLGA; Quercetin

Indexed keywords

BIOCOMPATIBILITY; BIODEGRADABLE POLYMERS; CONTROLLED DRUG DELIVERY; DRUG INTERACTIONS; FLAVONOIDS; FUNCTIONAL POLYMERS; GENE THERAPY; GLYCOPROTEINS; MAMMALS; MEDICAL APPLICATIONS; METAL IONS; METAL NANOPARTICLES; METALS; NANOPARTICLES; OLIGONUCLEOTIDES; PEPTIDES; PHENOLS; PROTEINS; TOXICITY;

ALZHEIMER'S DISEASE; BIOMEDICAL APPLICATIONS; DRUG DELIVERY CARRIER; HISTOLOGICAL ANALYSIS; PLGA; QUERCETIN; THERAPEUTIC STRATEGY; US FOOD AND DRUG ADMINISTRATION;

NEURODEGENERATIVE DISEASES;

AMYLOID BETA PROTEIN[1-42]; NANOPARTICLE; POLYGLACTIN; QUERCETIN NANOPARTICLE; UNCLASSIFIED DRUG; LACTIC ACID; POLYGLYCOLIC ACID; POLYLACTIC ACID-POLYGLYCOLIC ACID COPOLYMER; QUERCETIN;

ALZHEIMER DISEASE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ASSAY; CELL LINE; CELL VIABILITY; CIRCULAR DICHROISM; COGNITIVE DEFECT; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOTOXICITY; DRUG RELEASE; FEMALE; HISTOLOGY; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MEMORY DISORDER; MORRIS WATER MAZE TEST; MOUSE; NERVE CELL; NEUROBLASTOMA CELL; NEUROTOXICITY; NONHUMAN; NOVEL OBJECT RECOGNITION TEST; PRIORITY JOURNAL; PROTEIN AGGREGATION; SH SY5Y CELL LINE; THT ASSAY; TRANSMISSION ELECTRON MICROSCOPY; WEIGHT CHANGE; CHEMISTRY; ULTRAVIOLET SPECTROPHOTOMETRY;

ALZHEIMER DISEASE; CIRCULAR DICHROISM; HUMANS; LACTIC ACID; MICROSCOPY, ELECTRON, TRANSMISSION; NANOPARTICLES; POLYGLYCOLIC ACID; QUERCETIN; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 84984858982     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2016.08.052     Document Type: Article

References (65)

1. [1] Pepys, M.B., Amyloidosis. Annu. Rev. Med. 57 (2006), 223–241.
2. [2] Brookmeyer, R., Evans, D.A., Hebert, L., Langa, K.M., Heeringa, S.G., Plassman, B.L., Kukull, W.A., National estimates of the prevalence of Alzheimer's disease in the United States. Alzheimers Dement. 7 (2011), 61–73.
3. [3] López, L.C., Reis, S.R., Espargaro, A., Carrodeguas, J.A., Maddelein, M.L., Ventura, S., Sancho, J., Discovery of novel inhibitors of amyloid β-peptide 1–42 aggregation. J. Med. Chem. 55 (2012), 9521–9530.
4. [4] Ohta, K., Mizuno, A., Li, S., Itoh, M., Ueda, M., Ohta, E., Hida, Y., Wang, M.X., Furoi, M., Tsuzuki, Y., Sobajima, M., Bohmoto, Y., Fukushima, T., Kobori, M., Inuzuka, T., Nakagawa, T., Endoplasmic reticulum stress enhances γ-secretase activity. Biochem. Biophys. Res. Commun. 416 (2011), 362–366.
5. [5] Coyle, J.T., Price, D.L., Delong, M.R., Alzheimer's disease: a disorder of cortical cholinergic innervation. Science 219 (1983), 1184–1190.
6. [6] Trèves, T., Epidemiology of Alzheimer's disease. Psychiatr. Clin. N. Am. 14 (1991), 251–265.
7. [7] Choi, R.C.Y., Zhu, J.T.T., Leung, K.W., Chu, G.K.Y., Xie, H.Q., Chen, V.P., Zheng, K.Y.Z., Lau, D.T.W., Dong, T.T.X., Chow, P.C.Y., Han, Y.F., Wang, Z.T., Tsim, K.W.K., A flavonol glycoside, isolated from roots of Panax notoginseng, reduces amyloid-beta-induced neurotoxicity in cultured neurons: signaling transduction and drug development for Alzheimer's disease. J. Alzheimers Dis. 19 (2010), 795–811.
8. [8] Tanzi, R.E., Bertram, L., Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120 (2005), 545–555.
9. [9] Galimberti, D., Scarpini, E., Alzheimer's disease: from pathogenesis to disease-modifying approaches. CNS Neurol. Disord.-Dr. 10 (2011), 163–174.
10. [10] Jakob-Roetne, R., Jacobsen, H., Alzheimer's disease: from pathology to therapeutic approaches. Angew. Chem. Int. Ed. 48 (2009), 3030–3059.
11. [11] Buxbaum, J.N., Linke, R.P., A molecular history of the amyloidoses. J. Mol. Biol. 421 (2012), 142–159.
12. [12] Arvi, R., The chemistry of Alzheimer's disease. Chem. Soc. Rev. 40 (2009), 2698–2715.
13. [13] Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D.W., Golde, T., McGowan, E., Aβ40 inhibits amyloid deposition in vivo. J. Neurosci. 27 (2007), 627–633.
14. [14] Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers-Nolten, I., Werf, K.V.D., Subramaniam, V., Braeken, D., Callewaert, G., Bartic, C., D'Hooge, R., Martins, I.C., Rousseau, F., Schymkowitz, J., Strooper, B.D., Neurotoxicity of Alzheimer's disease Abeta peptides is induced by small changes in the Aβ42 to Aβ40 ratio. EMBO J. 29 (2010), 3408–3420.
15. [15] Pauwels, K., Williams, T.L., Morris, K.L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L.C., Broersen, K., The structural basis for increased toxicity of pathological Aβ42: Aβ40 ratios in Alzheimer's disease. J. Biol. Chem. 287 (2012), 5650–5660.
16. [16] Nguyen, M., Robert, A., Sournia-Saquet, A., Vendier, L., Meunier, B., Characterization of new specific copper chelators as potential drugs for the treatment of Alzheimer's disease. Chem.-Eur. J. 20 (2014), 6771–6785.
17. [17] Savelieff, M.G., Lee, S., Liu, Y., Lim, M.H., Untangling amyloid-β, tau, and metals in Alzheimer's disease. ACS Chem. Biol. 8 (2013), 856–865.
18. [18] Ma, G.L., Wang, E.Q., Wei, H., Wei, K.J., Zhu, P.P., Liu, Y.Z., Identification of [PtCl 2 (phen)] binding modes in amyloid-β peptide and the mechanism of aggregation inhibition. Chem.-Eur. J. 17 (2011), 11657–11666.
19. [19] Ma, G.L., Huang, F., Pu, X.W., Jia, L.Y., Jiang, T., Li, L.Z., Liu, Y.Z., PtCl2(phen) disrupts the metal ions binding to amyloid-β peptide. Metallomics 5 (2013), 879–887.
20. [20] Franz, K.J., Clawing back: broadening the notion of metal chelators in medicine. Curr. Opin. Chem. Biol. 17 (2013), 143–149.
21. [21] Sahni, J.K., Doggui, S., Ali, J., Baboota, S., Dao, L., Ramassamy, C., Neurotherapeutic applications of nanoparticles in Alzheimer's disease. J. Control. Release 152 (2011), 208–231.
22. [22] Li, M., Xu, C., Wu, L., Ren, J., Wang, E., Qu, X., Self-assembled peptide-polyoxometalate hybrid nanospheres: two in one enhances targeted inhibition of amyloid β-peptide aggregation associated with Alzheimer's disease. Small 9 (2013), 3455–3461.
23. [23] Jagota, S., Rajadas, J., Effect of phenolic compounds against Aβ aggregation and Aβ-induced toxicity in transgenic C. elegans. Neurochem. Res. 37 (2012), 40–48.
24. [24] Shi, C., Zhao, L., Zhu, B., Li, Q., Yew, D.T., Yao, Z., Xu, J., Protective effects of Ginkgo biloba extract (EGb761) and its constituents quercetin and ginkgolide B against β-amyloid peptide-induced toxicity in SH-SY5Y cells. Chem.-Biol. Interact. 181 (2009), 115–123.
25. [25] Jameson, L.P., Smith, N.W., Dzyuba, S.V., Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assembly. Acs Chem. Neurosci. 3 (2012), 807–819.
26. [26] Sun, S., Chen, W., Cao, W., Zhang, F., Song, J., Tian, C., Research on the chelation between quercetin and Cr (III) ion by density functional theory (DFT) method. J. Mol. Struct. Theochem. 60:8 (2008), 40–44.
27. [27] Spencer, J.P.E., Chowrimootoo, G., Choudhury, R., Debnam, E.S., Srai, S.K., Evans, C.R., The small intestine can both absorb and glucuronidate luminal flavonoids. FEBS Lett. 458 (1999), 224–230.
28. [28] Gao, Y., Wang, Y., Ma, Y., Yu, A., Cai, F., Shao, W., Zhai, G., Formulation optimization and in situ absorption in rat intestinal tract of quercetin-loaded microemulsion. Colloids Surf. B 71 (2009), 306–314.
29. [29] Ratnam, D.V., Ankola, D.D., Bhardwaj, V., Sahana, D.K., Kumar, M.N.V.R., Role of antioxidants in prophylaxis and therapy: a pharmaceutical perspective. J. Control. Release 113 (2006), 189–207.
30. [30] Jain, A.K., Das, M., Swarnakar, N.K., Jain, S., Engineered PLGA nanoparticles: an emerging delivery tool in cancer therapeutics. Crit. Rev. Ther. Drug 28 (2011), 1–45.
31. [31] Thanki, K., Gangwal, R., Sangamwar, A.T., Jain, S., Oral delivery of anticancer drugs: challenges and opportunities. J. Control. Release 170 (2013), 15–40.
32. [32] Ansari, M.A., Abdul, H.M., Joshi, G., Opii, W.O., Butterfield, D.A., Protective effect of quercetin in primary neurons against Aβ(1–42): relevance to Alzheimer's disease. J. Nutr. Biochem. 20 (2009), 269–275.
33. [33] Jeong, Y.I., Song, J.G., Kang, S.S., Ryu, H.H., Lee, Y.H., Choi, C., Shin, B.A., Kim, K.K., Ahn, K.Y., Jung, S., Preparation of poly(d, l -lactide-co-glycolide) microspheres encapsulating all-trans retinoic acid. Int. J. Pharmaceut. 259 (2003), 79–91.
34. [34] Lee, S.C., Oh, J.T., Jang, M.H., Chung, S.I., Quantitative analysis of polyvinyl alcohol on the surface of poly (d, l -lactide-co-glycolide) microparticles prepared by solvent evaporation method: effect of particle size and PVA concentration. J. Control. Release 59 (1999), 123–132.
35. [35] Cirpanli, Y., Unlü, N., Caliş, S., Hincal, A.A., Formulation and in-vitro characterization of retinoic acid loaded poly (lactic-co-glycolic acid) microspheres. J. Microencapsul. 22 (2005), 877–889.
36. [36] Ma, Q., Wei, G., Yang, X., Influence of Au nanoparticles on the aggregation of amyloid-β-(25–35) peptides. Nanoscale 5 (2013), 10397–10403.
37. [37] Ban, T., Hamada, D., Hasegawa, K., Naiki, H., Goto, Y., Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278 (2003), 16462–16465.
38. [38] D'Amico, M., Schirò, G., Cupane, A., D'Alfonso, L., Leone, M., Militello, V., Vetri, V., High fluorescence of thioflavin T confined in mesoporous silica xerogels. Langmuir 29 (2013), 10238–10246.
39. [39] Loynachan, C.N., Romero, G., Christiansen, M.G., Chen, R., Ellison, R., O'Malley, T.T., Froriep, U.P., Walsh, D.M., Anikeeva, P., Targeted magnetic nanoparticles for remote magnetothermal disruption of amyloid-β aggregates. Adv. Healthc. Mater. 4 (2015), 2100–2109.
40. [40] Bartolini, M., Bertucci, C., Bolognesi, M.L., Cavalli, A., Melchiorre, C., Andrisano, V., Insight into the kinetic of amyloid β (1-42) peptide self-aggregation: elucidation of inhibitors’ mechanism of action. Chembiochem 8 (2007), 2152–2161.
41. [41] Walsh, D.M., Lomakin, A., Benedek, G.B., Condron, M.M., Teplow, D.B., Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272 (1997), 22364–22372.
42. [42] Xiong, N., Dong, X., Zheng, J., Liu, F., Sun, Y., Design of LVFFARK and LVFFARK-functionalized nanoparticles for inhibiting amyloid β-protein fibrillation and cytotoxicity. ACS Appl. Mater. Interfaces 7 (2015), 5650–5662.
43. [43] Seiffert, J.M., Baradez, M.O., Nischwitz, V., Lekishvili, T., Infante, H.G., Marshall, D., Dynamic monitoring of metal oxide nanoparticle toxicity by label free impedance sensing. Chem. Res. Toxicol. 25 (2011), 140–152.
44. [44] Fotakis, G., Timbrell, J.A., In vitro cytotoxicity assays: comparison of LDH, neutral red, MTT and protein assay in hepatoma cell lines following exposure to cadmium chloride. Toxicol. Lett. 160 (2006), 171–177.
45. [45] Lobner, D., Comparison of the LDH and MTT assays for quantifying cell death: validity for neuronal apoptosis. J. Neurosci. Methods 96 (2000), 147–152.
46. [46] Decker, T., Matthes, M.L.L., A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity. J. Immunol. Methods 115 (1988), 61–69.
47. [47] Fisichella, M., Dabboue, H., Bhattacharayya, S., Saboungi, M.L., Salvetat, J.P., Hevor, T., Guerin, M., Mesoporous silica nanoparticles enhance MTT formazan exocytosis in HeLa cells and astrocytes. Toxicol. In Vitro 23 (2009), 697–703.
48. [48] Hsiao, I.L., Huang, Y.J., Improving the interferences of methyl thiazolyl tetrazolium and IL-8 assays in assessing the cytotoxicity of nanoparticles. J. Nanosci. Nanotechnol. 11 (2011), 5228–5233.
49. [49] Hooge, R.D., Deyn, P.P.D., Applications of the Morris water maze in the study of learning and memory. Brain Res. Rev. 36 (2001), 60–90.
50. [50] Brandeis, R., Brandys, Y., Yehuda, S., The use of the Morris Water Maze in the study of memory and learning. Int. J. Neurosci. 48 (2009), 29–69.
51. [51] Mcnamara, R.K., Skelton, R.W., The neuropharmacological and neurochemical basis of place learning in the Morris water maze. Brain Res. Rev. 18 (1993), 33–49.
52. [52] Ghosh, N., Chakraborty, T., Mallick, S., Mana, S., Singha, D., Ghosh, B., Roy, S., Synthesis, characterization and study of antioxidant activity of quercetin-magnesium complex. Spectrochim. Acta A 151 (2015), 807–813.
53. [53] Niu, P., Hao, J., Fabrication of titanium dioxide and tungstophosphate nanocomposite films and their photocatalytic degradation for methyl orange. Langmuir 27 (2011), 13590–13597.
54. [54] Nilsson, M.R., Techniques to study amyloid fibril formation in vitro. Methods 34 (2004), 151–160.
55. [55] Bleiholder, C., Dupuis, N.F., Wyttenbach, T., Bowers, M.T., Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation. Nat. Chem. 3 (2011), 172–177.
56. [56] Tickler, A.K., Smith, D.G., Ciccotosto, G.D., Tew, D.J., Curtain, C.C., Carrington, D., Masters, C.L., Bush, A.I., Cherny, R.A., Cappai, R., Wade, J.D., Barnham, K.J., Methylation of the imidazole side chains of the Alzheimer disease amyloid-beta peptide results in abolition of superoxide dismutase-like structures and inhibition of neurotoxicity. J. Biol. Chem. 280 (2005), 13355–13363.
57. [57] Blanchard, B.J., Chen, A., Rozeboom, L.M., Stafford, K.A., Weigele, P., Ingram, V.M., Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 14326–14332.
58. [58] Sood, A., Abid, M., Sauer, C., Hailemichael, S., Foster, M., Török, B., Török, M., Disassembly of preformed amyloid beta fibrils by small organofluorine molecules. Bioorg. Med. Chem. Lett. 21 (2011), 2044–2047.
59. [59] Fredenberg, S., Wahlgren, M., Reslow, M., Axelsson, A., The mechanisms of drug release in poly (lactic-co-glycolic acid)-based drug delivery systems-a review. Int. J. Pharma. 415 (2011), 34–52.
60. [60] Chitkara, D., Nikalaje, S.K., Mittal, A., Chand, M., Kumar, N., Development of quercetin nanoformulation and in vivo evaluation using streptozotocin induced diabetic rat model. Drug Deliv. Transl. Res. 2 (2012), 112–123.
61. [61] Cho, C.E., Zhang, Q., Xia, Y., The effect of sedimentation and diffusion on cellular uptake of gold nanoparticles. Nat. Nanotechnol. 6 (2011), 385–391.
62. [62] Gonzalez, L.O., Alvarez, R.S., Boitano, S., Field, J.A., Application and validation of an impedance-based real time cell analyzer to measure the toxicity of nanoparticles impacting human bronchial epithelial cells. Environ. Sci. Technol. 46 (2012), 10271–10278.
63. [63] Xing, J., Zhu, L., Jackson, J.A., Gabos, S., Sun, X., Wang, X., Xu, X., Dynamic monitoring of cytotoxicity on microelectronic sensors. Chem. Res. Toxicol. 18 (2005), 154–161.
64. [64] Liu, R., Zhang, T., Zhou, D., Bai, X., Zhou, W., Huang, C., Song, J., Meng, F., Wu, C., Li, L., Du, G., Quercetin protects against the Aβ 25-35 − induced amnesic injury: involvement of inactivation of RAGE-mediated pathway and conservation of the NVU. Neuropharmacology 67 (2013), 419–431.
65. [65] She, W., Li, N., Luo, K., Guo, C., Wang, G., Geng, Y., Gu, Z., Dendronized heparin-doxorubicin conjugate based nanoparticle aspH-responsive drug delivery system for cancer therapy. Biomaterials 34 (2013), 2252–2264.