Multiple effects of polydopamine nanoparticles on Cu2+-mediated Alzheimer's β-amyloid aggregation

doi:10.1016/j.cjche.2022.04.007

中国化学工程学报 ›› 2023, Vol. 54 ›› Issue (2): 144-152.DOI: 10.1016/j.cjche.2022.04.007

• Full Length Article • 上一篇下一篇

Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation

Xueqing Chen, Weiqun Gao, Yan Sun, Xiaoyan Dong

Department of Biochemical Engineering, School of Chemical Engineering and Technology and Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University, Tianjin 300350, China

收稿日期:2022-01-10 修回日期:2022-03-11 出版日期:2023-02-28 发布日期:2023-05-11
通讯作者: Xiaoyan Dong,E-mail:d_xy@tju.edu.cn
基金资助:
This work was funded by the National Natural Science Foundation of China (21978207 and 21621004) and the Natural Science Foundation of Tianjin from Tianjin Municipal Science and Technology Commission (19JCZDJC36800).

Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation

Xueqing Chen, Weiqun Gao, Yan Sun, Xiaoyan Dong

Department of Biochemical Engineering, School of Chemical Engineering and Technology and Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University, Tianjin 300350, China

Received:2022-01-10 Revised:2022-03-11 Online:2023-02-28 Published:2023-05-11
Contact: Xiaoyan Dong,E-mail:d_xy@tju.edu.cn
Supported by:
This work was funded by the National Natural Science Foundation of China (21978207 and 21621004) and the Natural Science Foundation of Tianjin from Tianjin Municipal Science and Technology Commission (19JCZDJC36800).

摘要/Abstract

摘要： Deposition of β-amyloid protein (Aβ) is the main hallmark of Alzheimer's disease (AD), and it has been well recognized that Cu²⁺-mediated Aβ aggregation plays a crucial role in AD pathological processes. Cu²⁺ binding to Aβ can promote the production of reactive oxygen species (ROS) through Fenton-like reactions and produce more toxic Aβ-Cu²⁺ species under Cu²⁺ stimulation. Thus, the development of nanomaterials that can inhibit Cu²⁺-mediated Aβ aggregation and degrade Aβ-Cu²⁺ complexes is considered an effective strategy for the prevention and treatment of AD. In this study, polydopamine nanoparticles (PDA NPs) were prepared and the results reveal that PDA NPs potently inhibit Cu²⁺-mediated Aβ aggregation and effectively reduce the formation of Aβ-Cu²⁺ complexes. In vitro experiments show that PDA NPs efficiently eliminate ROS generation catalyzed by Cu²⁺ or Aβ-Cu²⁺ complexes, thus rescuing cultured cells by reducing intracellular ROS levels. More importantly, PDA NPs can depolymerize Aβ-Cu²⁺ complexes, and the degradation of Aβ-Cu²⁺ complexes is promoted by near-infrared light irradiation due to their high photothermal conversion ability. In vivo studies reveal that PDA NPs significantly reduce the deposition of Aβ plaques in the presence of Cu²⁺ and extend the lifespan of AD nematodes from 11 to 14 d. Thus, the PDA NPs developed herein are multifunctional against Cu²⁺-mediated Aβ aggregation for the potential prevention and treatment of AD.

关键词: Protein, Aggregation, Nanoparticles, Photothermal therapy, Reactive oxygen species, Cu²⁺ chelator

Abstract: Deposition of β-amyloid protein (Aβ) is the main hallmark of Alzheimer's disease (AD), and it has been well recognized that Cu²⁺-mediated Aβ aggregation plays a crucial role in AD pathological processes. Cu²⁺ binding to Aβ can promote the production of reactive oxygen species (ROS) through Fenton-like reactions and produce more toxic Aβ-Cu²⁺ species under Cu²⁺ stimulation. Thus, the development of nanomaterials that can inhibit Cu²⁺-mediated Aβ aggregation and degrade Aβ-Cu²⁺ complexes is considered an effective strategy for the prevention and treatment of AD. In this study, polydopamine nanoparticles (PDA NPs) were prepared and the results reveal that PDA NPs potently inhibit Cu²⁺-mediated Aβ aggregation and effectively reduce the formation of Aβ-Cu²⁺ complexes. In vitro experiments show that PDA NPs efficiently eliminate ROS generation catalyzed by Cu²⁺ or Aβ-Cu²⁺ complexes, thus rescuing cultured cells by reducing intracellular ROS levels. More importantly, PDA NPs can depolymerize Aβ-Cu²⁺ complexes, and the degradation of Aβ-Cu²⁺ complexes is promoted by near-infrared light irradiation due to their high photothermal conversion ability. In vivo studies reveal that PDA NPs significantly reduce the deposition of Aβ plaques in the presence of Cu²⁺ and extend the lifespan of AD nematodes from 11 to 14 d. Thus, the PDA NPs developed herein are multifunctional against Cu²⁺-mediated Aβ aggregation for the potential prevention and treatment of AD.

Key words: Protein, Aggregation, Nanoparticles, Photothermal therapy, Reactive oxygen species, Cu²⁺ chelator

Xueqing Chen, Weiqun Gao, Yan Sun, Xiaoyan Dong. Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation[J]. 中国化学工程学报, 2023, 54(2): 144-152.

Xueqing Chen, Weiqun Gao, Yan Sun, Xiaoyan Dong. Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation[J]. Chinese Journal of Chemical Engineering, 2023, 54(2): 144-152.

参考文献

[1] I. Ahmad, A.B. Mozhi, L. Yang, Q.S. Han, X.J. Liang, C. Li, R. Yang, C. Wang, Graphene oxide-iron oxide nanocomposite as an inhibitor of Aβ 42 amyloid peptide aggregation, Colloids Surf. B Biointerfaces 159 (2017) 540–545.
[2] H. Amiri, K. Saeidi, P. Borhani, A. Manafirad, M. Ghavami, V. Zerbi, Alzheimer's disease: pathophysiology and applications of magnetic nanoparticles as MRI theranostic agents, ACS Chem. Neurosci. 4 (11) (2013) 1417–1429.
[3] W.P. Zhao, L.Y. Jiang, W.J. Wang, J.C. Sang, Q.C. Sun, Q.C. Dong, L. Li, F.P. Lu, F.F. Liu, Design of carboxylated single-walled carbon nanotubes as highly efficient inhibitors against Aβ₄₀ fibrillation based on the HyBER mechanism, J. Mater. Chem. B 9 (34) (2021) 6902–6914.
[4] Y.D. Huang, L. Mucke, Alzheimer mechanisms and therapeutic strategies, Cell 148 (6) (2012) 1204–1222.
[5] X.L. Huo, Y.Q. Zhang, X.C. Jin, Y.A. Li, L. Zhang, 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 Biol. 190 (2019) 98–102.
[6] J. Kowalczyk, E. Grapsi, A. Espargaró, A.B. Caballero, J. Juárez-Jiménez, M.A. Busquets, P. Gamez, R. Sabate, J. Estelrich, Dual effect of Prussian blue nanoparticles on Aβ₄₀ aggregation: β-sheet fibril reduction and copper dyshomeostasis regulation, Biomacromolecules 22 (2) (2021) 430–440.
[7] W. Liu , X.T. Sun , X.Y. Dong , Y. Sun, Chiral LVFFARK enantioselectively inhibits amyloid-β protein fibrillogenesis, Chin. J. Chem. Eng. 48 (2022) 227–235.
[8] L.C. Yang, J. Sun, W.J. Xie, Y.N. Liu, J. Liu, Dual-functional selenium nanoparticles bind to and inhibit amyloid β fiber formation in Alzheimer's disease, J. Mater. Chem. B 5 (30) (2017) 5954–5967.
[9] Y.X. Zhang, Y.J. Tang, D. Zhang, Y.L. Liu, J. He, Y. Chang, J. Zheng, Amyloid cross-seeding between Aβ and hIAPP in relation to the pathogenesis of Alzheimer and type 2 diabetes, Chin. J. Chem. Eng. 30 (2021) 225–235.
[10] F. Huang, A.T. Qu, H.R. Yang, L. Zhu, H. Zhou, J.F. Liu, J.F. Long, L.Q. Shi, Self-assembly molecular chaperone to concurrently inhibit the production and aggregation of amyloid β peptide associated with Alzheimer's disease, ACS Macro Lett. 7 (8) (2018) 983–989.
[11] E. Stefaniak, E. Atrian-Blasco, W. Goch, L. Sabater, C. Hureau, W. Bal, The aggregation pattern of aβ _1–40 is altered by the presence of N-truncated aβ_4–40 and/or Cu II in a similar way through ionic interactions, Chem. Eur. J. 27 (8) (2021) 2798–2809.
[12] D.Q. Yu, Y.J. Guan, F.Q. Bai, Z. Du, N. Gao, J.S. Ren, X.G. Qu, Metal-organic frameworks harness Cu chelating and photooxidation against amyloid β aggregation in vivo, Chem. A Eur. J. 25 (14) (2019) 3489–3495.
[13] C.J. Matheou, N.D. Younan, J.H. Viles, Cu²⁺ accentuates distinct misfolding of Aβ_(1–40) and Aβ_(1–42) peptides, and potentiates membrane disruption, Biochem. J. 466 (2) (2015) 233–242.
[14] K. Rajasekhar, C. Madhu, T. Govindaraju, Natural tripeptide-based inhibitor of multifaceted amyloid β toxicity, ACS Chem. Neurosci. 7 (9) (2016) 1300–1310.
[15] Y.Q. Zhao, Q.M. Xu, W. Xu, D.D. Wang, J. Tan, C.Q. Zhu, X.S. Tan, Probing the molecular mechanism of cerium oxide nanoparticles in protecting against the neuronal cytotoxicity of Aβ_1-42 with copper ions, Metallomics 8 (7) (2016) 644–647.
[16] Z.K. Mathys, A.R. White, Copper and Alzheimer's disease, Adv. Neurobiol. 18 (2017) 199–216.
[17] M.Y. Dong, H.Y. Li, D.K. Hu, W. Zhao, X.Y. Zhu, H.Q. Ai, Molecular dynamics study on the inhibition mechanisms of drugs CQ_1-3 for alzheimer amyloid-β₄₀ aggregation induced by Cu(2.), ACS Chem. Neurosci. 7 (5) (2016) 599–614.
[18] F. Tahmasebinia, S. Emadi, Effect of metal chelators on the aggregation of beta-amyloid peptides in the presence of copper and iron, Biometals 30 (2) (2017) 285–293.
[19] L.Y. Zhu, Y.C. Han, C.Q. He, X. Huang, Y.L. Wang, Disaggregation ability of different chelating molecules on copper ion-triggered amyloid fibers, J. Phys. Chem. B 118 (31) (2014) 9298–9305.
[20] R.K. Chang, X. Chen, H.J. Yu, G.Z. Tan, H.L. Wen, J.X. Huang, Z.F. Hao, Modified EDTA selectively recognized Cu²⁺ and its application in the disaggregation of β-amyloid-Cu (II)/Zn (II) aggregates, J. Inorg. Biochem. 203 (2020) 110929.
[21] D.M. Johnstone, C. Moro, J. Stone, A.L. Benabid, J. Mitrofanis, Turning on lights to stop neurodegeneration: the potential of near infrared light therapy in Alzheimer's and Parkinson's disease, Front. Neurosci. 9 (2016) 500.
[22] W.Z. Pan, C.B. Dai, Y. Li, Y.M. Yin, L. Gong, J.O. Machuki, Y. Yang, S. Qiu, K.J. Guo, F.L. Gao, PRP-chitosan thermoresponsive hydrogel combined with black phosphorus nanosheets as injectable biomaterial for biotherapy and phototherapy treatment of rheumatoid arthritis, Biomaterials 239 (2020) 119851.
[23] Y.W. Xi, J. Ge, M. Wang, M. Chen, W. Niu, W. Cheng, Y.M. Xue, C. Lin, B. Lei, Bioactive anti-inflammatory, antibacterial, antioxidative silicon-based nanofibrous dressing enables cutaneous tumor photothermo-chemo therapy and infection-induced wound healing, ACS Nano 14 (3) (2020) 2904–2916.
[24] Y.T. Zhao, L.P. Tong, Z.B. Li, N. Yang, H.D. Fu, L. Wu, H.D. Cui, W.H. Zhou, J.H. Wang, H.Y. Wang, P.K. Chu, X.F. Yu, Stable and multifunctional dye-modified black phosphorus nanosheets for near-infrared imaging-guided photothermal therapy, Chem. Mater. 29 (17) (2017) 7131–7139.
[25] T.T. Yin, W.J. Xie, J. Sun, L.C. Yang, J. Liu, Penetratin peptide-functionalized gold nanostars: enhanced BBB permeability and NIR photothermal treatment of Alzheimer's disease using ultralow irradiance, ACS Appl. Mater. Interfaces 8 (30) (2016) 19291–19302.
[26] S. Sudhakar, P.B. Santhosh, E. Mani, Dual role of gold nanorods: inhibition and dissolution of aβ fibrils induced by near IR laser, ACS Chem. Neurosci. 8 (10) (2017) 2325–2334.
[27] M. Li, X.J. Yang, J.S. Ren, K.G. Qu, X.G. Qu, Using graphene oxide high near-infrared absorbance for photothermal treatment of Alzheimer's disease, Adv. Mater. 24 (13) (2012) 1722–1728.
[28] M. Li, A.D. Zhao, K. Dong, W. Li, J.S. Ren, X.G. Qu, Chemically exfoliated WS₂ nanosheets efficiently inhibit amyloid β-peptide aggregation and can be used for photothermal treatment of Alzheimer's disease, Nano Res. 8 (10) (2015) 3216–3227.
[29] M. Battaglini, A. Marino, A. Carmignani, C. Tapeinos, V. Cauda, A. Ancona, N. Garino, V. Vighetto, G. la Rosa, E. Sinibaldi, G. Ciofani, Polydopamine nanoparticles as an organic and biodegradable multitasking tool for neuroprotection and remote neuronal stimulation, ACS Appl. Mater. Interfaces 12 (32) (2020) 35782–35798.
[30] S.H. Bhang, S.H. Kwon, S. Lee, G.C. Kim, A.M. Han, Y.H. Kwon, B.S. Kim, Enhanced neuronal differentiation of pheochromocytoma 12 cells on polydopamine-modified surface, Biochem. Biophys. Res. Commun. 430 (4) (2013) 1294–1300.
[31] Y. Fu, L. Yang, J.H. Zhang, J.F. Hu, G.G. Duan, X.H. Liu, Y.W. Li, Z.P. Gu, Polydopamine antibacterial materials, Mater. Horiz. 8 (6) (2021) 1618–1633.
[32] X.J. Chen, L.X. Song, X.L. Li, L.Y. Zhang, L. Li, X.P. Zhang, C.G. Wang, Co-delivery of hydrophilic/hydrophobic drugs by multifunctional yolk-shell nanoparticles for hepatocellular carcinoma theranostics, Chem. Eng. J. 389 (2020) 124416.
[33] J.S. Liu, S.J. Peng, G.F. Li, Y.X. Zhao, X.Y. Meng, X.R. Yu, Z.H. Li, J.M. Chen, Polydopamine nanoparticles for deep brain ablation via near-infrared irradiation, ACS Biomater. Sci. Eng. 6 (1) (2020) 664–672.
[34] P. Xue, L.H. Sun, Q. Li, L. Zhang, J.H. Guo, Z.G. Xu, Y.J. Kang, PEGylated polydopamine-coated magnetic nanoparticles for combined targeted chemotherapy and photothermal ablation of tumour cells, Colloids Surf. B Biointerfaces 160 (2017) 11–21.
[35] C.C. Ho, S.J. Ding, Structure, properties and applications of mussel-inspired polydopamine, J. Biomed. Nanotechnol. 10 (10) (2014) 3063–3084.
[36] D. Hauser, D. Septiadi, J. Turner, A. Petri-Fink, B. Rothen-Rutishauser, From bioinspired glue to medicine: polydopamine as a biomedical material, Materials (Basel) 13 (7) (2020) E1730.
[37] L. Liu, Y. Chang, J. Yu, M.S. Jiang, N. Xia, Two-in-one polydopamine nanospheres for fluorescent determination of beta-amyloid oligomers and inhibition of beta-amyloid aggregation, Sens. Actuat. B Chem. 251 (2017) 359–365.
[38] X.J. Yu, X. Tang, J.K. He, X. Yi, G.Y. Xu, L.L. Tian, R. Zhou, C. Zhang, K. Yang, Polydopamine nanoparticle as a multifunctional nanocarrier for combined radiophotodynamic therapy of cancer, Part. Part. Syst. Charact. 34 (2) (2017) 1600296.
[39] B.J. Geng, D.W. Yang, D.Y. Pan, L. Wang, F.F. Zheng, W.W. Shen, C. Zhang, X.K. Li, NIR-responsive carbon dots for efficient photothermal cancer therapy at low power densities, Carbon 134 (2018) 153–162.
[40] H. Zhang, X.Y. Dong, Y. Sun, Carnosine-LVFFARK-NH₂ conjugate: a moderate chelator but potent inhibitor of Cu²⁺-mediated amyloid β-protein aggregation, ACS Chem. Neurosci. 9 (11) (2018) 2689–2700.
[41] J.N. Yang, W. Liu, Y. Sun, X.Y. Dong, LVFFARK-PEG-stabilized black phosphorus nanosheets potently inhibit amyloid-β fibrillogenesis, Langmuir 36 (7) (2020) 1804–1812.
[42] X. Li, W.J. Wang, X.Y. Dong, Y. Sun, Conjugation of RTHLVFFARK to human lysozyme creates a potent multifunctional modulator for Cu²⁺-mediated amyloid β-protein aggregation and cytotoxicity, J. Mater. Chem. B 8 (11) (2020) 2256–2268.
[43] Q. Liu, Z.H. Pu, A.M. Asiri, A.O. Al-Youbi, X.P. Sun, Polydopamine nanospheres: a biopolymer-based fluorescent sensing platform for DNA detection, Sens. Actuat. B Chem. 191 (2014) 567–571.
[44] Y.J. Chung, B.I. Lee, C.B. Park, Multifunctional carbon dots as a therapeutic nanoagent for modulating Cu(ii)-mediated β-amyloid aggregation, Nanoscale 11 (13) (2019) 6297–6306.
[45] H. Zhang, C. Zhang, X.Y. Dong, J. Zheng, Y. Sun, Design of nonapeptide LVFFARKHH: a bifunctional agent against Cu²⁺-mediated amyloid β-protein aggregation and cytotoxicity, J. Mol. Recognit. 31 (6) (2018) e2697.
[46] W.Q. Gao, W.J. Wang, X.Y. Dong, Y. Sun, Nitrogen-doped carbonized polymer dots: a potent scavenger and detector targeting Alzheimer's β-amyloid plaques, Small 16 (43) (2020) e2002804.
[47] L.G. Jia, W.P. Zhao, J.C. Sang, W.J. Wang, W. Wei, Y. Wang, F. Zhao, F.P. Lu, F.F. Liu, Inhibitory effect of a flavonoid dihydromyricetin against Aβ₄₀ amyloidogenesis and its associated cytotoxicity, ACS Chem. Neurosci. 10 (11) (2019) 4696–4703.
[48] Du Z, Gao N, Wang X, Ren J, Qu X, Near-infrared switchable fullerene-based synergy therapy for Alzheimer's disease, Small (2018) e1801852.

Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation

Multiple effects of polydopamine nanoparticles on Cu²⁺-mediated Alzheimer's β-amyloid aggregation

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