{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T01:19:43Z","timestamp":1789521583717,"version":"build-2803163510"},"reference-count":132,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T00:00:00Z","timestamp":1746662400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Department of Biomedical and Chemical Engineering at Syracuse University"},{"name":"Department of Biology at Syracuse University"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nanomaterials"],"abstract":"<jats:p>Intrinsically disordered proteins (IDPs), such as tau, beta-amyloid (A\u03b2), and alpha-synuclein (\u03b1Syn), are prone to misfolding, resulting in pathological aggregation and propagation that drive neurodegenerative diseases, including Alzheimer\u2019s disease (AD), frontotemporal dementia (FTD), and Parkinson\u2019s disease (PD). Misfolded IDPs are prone to aggregate into oligomers and fibrils, exacerbating disease progression by disrupting cellular functions in the central nervous system, triggering neuroinflammation and neurodegeneration. Furthermore, aggregated IDPs exhibit prion-like behavior, acting as seeds that are released into the extracellular space, taken up by neighboring cells, and have a propagating pathology across different regions of the brain. Conventional inhibitors, such as small molecules, peptides, and antibodies, face challenges in stability and blood\u2013brain barrier penetration, limiting their efficacy. In recent years, nanotechnology-based strategies, such as multifunctional nanoplatforms or nanoparticles, have emerged as promising tools to address these challenges. These nanoplatforms leverage tailored designs to prevent or remodel the aggregation of IDPs and reduce associated neurotoxicity. This review discusses recent advances in nanoplatforms designed to target tau, A\u03b2, and \u03b1Syn aggregation, with a focus on their roles in reducing neuroinflammation and neurodegeneration. We examine critical aspects of nanoplatform design, including the choice of material backbone and targeting moieties, which influence interactions with IDPs. We also highlight key mechanisms including the interaction between nanoplatforms and IDPs to inhibit their aggregation, redirect aggregation cascade towards nontoxic, off-pathway species, and disrupt fibrillar structures into soluble forms. We further outline future directions for enhancing IDP clearance, achieving spatiotemporal control, and improving cell-specific targeting. These nanomedicine strategies offer compelling paths forward for developing more effective and targeted therapies for neurodegenerative diseases.<\/jats:p>","DOI":"10.3390\/nano15100704","type":"journal-article","created":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T09:58:09Z","timestamp":1746698289000},"page":"704","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Nanoplatforms Targeting Intrinsically Disordered Protein Aggregation for Translational Neuroscience Applications"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2717-4484","authenticated-orcid":false,"given":"Chih Hung","family":"Lo","sequence":"first","affiliation":[{"name":"Department of Biology, Syracuse University, Syracuse, NY 13244, USA"},{"name":"Interdisciplinary Neuroscience Program, Syracuse University, Syracuse, NY 13244, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lenny Yi Tong","family":"Cheong","sequence":"additional","affiliation":[{"name":"Lee Kong Chian School of Medicine, Nanyang Technological University, Singapore 308232, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7802-1432","authenticated-orcid":false,"given":"Jialiu","family":"Zeng","sequence":"additional","affiliation":[{"name":"Interdisciplinary Neuroscience Program, Syracuse University, Syracuse, NY 13244, USA"},{"name":"Department of Biomedical and Chemical Engineering, Syracuse University, Syracuse, NY 13244, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/s41392-021-00678-1","article-title":"Liquid\u2013Liquid Phase Separation in Human Health and Diseases","volume":"6","author":"Wang","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1038\/s41392-024-02070-1","article-title":"Emerging Regulatory Mechanisms and Functions of Biomolecular Condensates: Implications for Therapeutic Targets","volume":"10","author":"Jeon","year":"2025","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Utami, K.H., Morimoto, S., Mitsukura, Y., and Okano, H. (2025). The Roles of Intrinsically Disordered Proteins in Neurodegeneration. Biochim. Biophys. Acta (BBA) Gen. Subj., 1869.","DOI":"10.1016\/j.bbagen.2025.130772"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41593-018-0235-9","article-title":"Protein Misfolding, Aggregation, and Conformational Strains in Neurodegenerative Diseases","volume":"21","author":"Soto","year":"2018","journal-title":"Nat. Neurosci."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Trivedi, R., and Nagarajaram, H.A. (2022). Intrinsically Disordered Proteins: An Overview. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232214050"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/s13024-019-0333-5","article-title":"The Neuropathological Diagnosis of Alzheimer\u2019s Disease","volume":"14","author":"DeTure","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","article-title":"The Amyloid-\u03b2 Pathway in Alzheimer\u2019s Disease","volume":"26","author":"Hampel","year":"2021","journal-title":"Mol. Psychiatry"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/s41419-023-05672-9","article-title":"Alpha-Synuclein in Parkinson\u2019s Disease and Other Synucleinopathies: From Overt Neurodegeneration Back to Early Synaptic Dysfunction","volume":"14","author":"Calabresi","year":"2023","journal-title":"Cell Death Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"440","DOI":"10.3390\/biophysica2040039","article-title":"Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer\u2019s Disease and Related Tauopathies","volume":"2","author":"Lo","year":"2022","journal-title":"Biophysica"},{"key":"ref_10","first-page":"17","article-title":"The Role of Wild-Type Tau in Alzheimer\u2019s Disease and Related Tauopathies","volume":"2","author":"Lo","year":"2021","journal-title":"J Life Sci (Westlake Village)"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1007\/s12551-022-00968-0","article-title":"Intrinsically Disordered Proteins and Proteins with Intrinsically Disordered Regions in Neurodegenerative Diseases","volume":"14","author":"Mirzanli","year":"2022","journal-title":"Biophys. Rev."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e1685","DOI":"10.1002\/wcms.1685","article-title":"Rational Drug Design Targeting Intrinsically Disordered Proteins","volume":"13","author":"Wang","year":"2023","journal-title":"WIREs Comput. Mol. Sci."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"T\u00f3th, G., Neumann, T., Berthet, A., Masliah, E., Spencer, B., Tao, J., Jobling, M.F., Gardai, S.J., Bertoncini, C.W., and Cremades, N. (2019). Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of \u03b1-Synuclein Protect Against Diverse \u03b1-Synuclein Mediated Dysfunctions. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-52598-4"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"108797","DOI":"10.1016\/j.pharmthera.2025.108797","article-title":"Conformationally Adaptive Therapeutic Peptides for Diseases Caused by Intrinsically Disordered Proteins (IDPs). New Paradigm for Drug Discovery: Target the Target, Not the Arrow","volume":"267","author":"Fantini","year":"2025","journal-title":"Pharmacol. Ther."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Kouhi, A., Pachipulusu, V., Kapenstein, T., Hu, P., Epstein, A.L., and Khawli, L.A. (2021). Brain Disposition of Antibody-Based Therapeutics: Dogma, Approaches and Perspectives. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126442"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"4109","DOI":"10.1039\/D0BM00809E","article-title":"Nanomaterial Based Drug Delivery Systems for the Treatment of Neurodegenerative Diseases","volume":"8","author":"Ahlawat","year":"2020","journal-title":"Biomater. Sci."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Asimakidou, E., Tan, J.K.S., Zeng, J., and Lo, C.H. (2024). Blood\u2013Brain Barrier-Targeting Nanoparticles: Biomaterial Properties and Biomedical Applications in Translational Neuroscience. Pharmaceuticals, 17.","DOI":"10.3390\/ph17050612"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1007\/s40291-023-00654-1","article-title":"Recent Advancements in Nanomaterials: A Promising Way to Manage Neurodegenerative Disorders","volume":"27","author":"Nguyen","year":"2023","journal-title":"Mol. Diagn. Ther."},{"key":"ref_19","first-page":"24","article-title":"Current Update on Nanoplatforms as Therapeutic and Diagnostic Tools: A Review for the Materials Used as Nanotheranostics and Imaging Modalities","volume":"16","author":"Siafaka","year":"2021","journal-title":"Asian J. Pharm. Sci."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Taverna, C., Fasolato, C., Brasili, F., Ripanti, F., Rizza, C., De Marcellis, A., Postorino, P., Sennato, S., Nucara, A., and Capocefalo, A. (2025). Probing the Effect of the Molecular Interface of Gold Nanoparticles on the Disassembly of Insulin Amyloid Fibrils. Int. J. Biol. Macromol., 306.","DOI":"10.1016\/j.ijbiomac.2025.141735"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.jcis.2022.04.085","article-title":"High Efficiency and Related Mechanism of Au(RC) Nanoclusters on Disaggregating A\u03b2 Fibrils","volume":"621","author":"Gao","year":"2022","journal-title":"J. Colloid. Interface Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3631","DOI":"10.1002\/smll.201201068","article-title":"Negatively Charged Gold Nanoparticles Inhibit Alzheimer\u2019s Amyloid-\u03b2 Fibrillization, Induce Fibril Dissociation, and Mitigate Neurotoxicity","volume":"8","author":"Liao","year":"2012","journal-title":"Small"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Jagaran, K., and Singh, M. (2021). Nanomedicine for Neurodegenerative Disorders: Focus on Alzheimer\u2019s and Parkinson\u2019s Diseases. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22169082"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Nayab, D.E., Din, F.U., Ali, H., Kausar, W.A., Urooj, S., Zafar, M., Khan, I., Shabbir, K., and Khan, G.M. (2023). Nano Biomaterials Based Strategies for Enhanced Brain Targeting in the Treatment of Neurodegenerative Diseases: An up-to-Date Perspective. J. Nanobiotechnol., 21.","DOI":"10.1186\/s12951-023-02250-1"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Shabani, L., Abbasi, M., Azarnew, Z., Amani, A.M., and Vaez, A. (2023). Neuro-Nanotechnology: Diagnostic and Therapeutic Nano-Based Strategies in Applied Neuroscience. Biomed. Eng. Online, 22.","DOI":"10.1186\/s12938-022-01062-y"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Zhu, F.-D., Hu, Y.-J., Yu, L., Zhou, X.-G., Wu, J.-M., Tang, Y., Qin, D.-L., Fan, Q.-Z., and Wu, A.-G. (2021). Nanoparticles: A Hope for the Treatment of Inflammation in CNS. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.683935"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/s11671-024-03979-w","article-title":"Theranostics: A Multifaceted Approach Utilizing Nano-Biomaterials","volume":"19","author":"Yasir","year":"2024","journal-title":"Discov. Nano"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1038\/nature02265","article-title":"Therapeutic Approaches to Protein-Misfolding Diseases","volume":"426","author":"Cohen","year":"2003","journal-title":"Nature"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1002\/cbic.200900666","article-title":"Strategies for the Inhibition of Protein Aggregation in Human Diseases","volume":"11","author":"Bartolini","year":"2010","journal-title":"ChemBioChem"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1111\/j.1755-5949.2010.00177.x","article-title":"The Role of Tau in Alzheimer\u2019s Disease and Related Disorders","volume":"17","author":"Medeiros","year":"2011","journal-title":"CNS Neurosci. Ther."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1186\/s12974-023-02853-3","article-title":"Tau and Neuroinflammation in Alzheimer\u2019s Disease: Interplay Mechanisms and Clinical Translation","volume":"20","author":"Chen","year":"2023","journal-title":"J. Neuroinflamm."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.neulet.2019.04.022","article-title":"The Complexity of Tau in Alzheimer\u2019s Disease","volume":"705","author":"Naseri","year":"2019","journal-title":"Neurosci. Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1007\/s00018-019-03349-1","article-title":"Mechanisms of Secretion and Spreading of Pathological Tau Protein","volume":"77","author":"Brunello","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1038\/s41435-020-00113-5","article-title":"Tau at the Interface between Neurodegeneration and Neuroinflammation","volume":"21","author":"Didonna","year":"2020","journal-title":"Genes Immun."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4582","DOI":"10.1021\/acs.jpcb.5b00175","article-title":"Tau Assembly: The Dominant Role of PHF6 (VQIVYK) in Microtubule Binding Region Repeat R3","volume":"119","author":"Ganguly","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"e36584","DOI":"10.7554\/eLife.36584","article-title":"Inert and Seed-Competent Tau Monomers Suggest Structural Origins of Aggregation","volume":"7","author":"Mirbaha","year":"2018","journal-title":"eLife"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1007\/s00018-020-03681-x","article-title":"The Structure and Phase of Tau: From Monomer to Amyloid Filament","volume":"78","author":"Zeng","year":"2021","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature10154","article-title":"Structure-Based Design of Non-Natural Amino-Acid Inhibitors of Amyloid Fibril Formation","volume":"475","author":"Sievers","year":"2011","journal-title":"Nature"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Dammers, C., Yolcu, D., Kukuk, L., Willbold, D., Pickhardt, M., Mandelkow, E., Horn, A.H.C., Sticht, H., Malhis, M.N., and Will, N. (2016). Selection and Characterization of Tau Binding \u1d05-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0167432"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"23328","DOI":"10.1021\/acsami.1c00257","article-title":"Tau-Targeted Multifunctional Nanoinhibitor for Alzheimer\u2019s Disease","volume":"13","author":"Zhu","year":"2021","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"101388","DOI":"10.1016\/j.nantod.2022.101388","article-title":"Engineering a Pathological Tau-Targeted Nanochaperone for Selective and Synergetic Inhibition of Tau Pathology in Alzheimer\u2019s Disease","volume":"43","author":"Xu","year":"2022","journal-title":"Nano Today"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"eadl2991","DOI":"10.1126\/sciadv.adl2991","article-title":"D-Peptide-Magnetic Nanoparticles Fragment Tau Fibrils and Rescue Behavioral Deficits in a Mouse Model of Alzheimer\u2019s Disease","volume":"10","author":"Hou","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Qiao, L., Shen, Y., Li, G., Lv, G., and Li, C. (2023). Hypochlorous Acid-Activated UCNPs-LMB\/VQIVYK Multifunctional Nanosystem for Alzheimer\u2019s Disease Treatment. J. Funct. Biomater., 14.","DOI":"10.3390\/jfb14040207"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"12833","DOI":"10.1021\/acsomega.9b01411","article-title":"Protein-Capped Metal Nanoparticles Inhibit Tau Aggregation in Alzheimer\u2019s Disease","volume":"4","author":"Sonawane","year":"2019","journal-title":"ACS Omega"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1906861","DOI":"10.1002\/smll.201906861","article-title":"Self-Therapeutic Nanoparticle That Alters Tau Protein and Ameliorates Tauopathy Toward a Functional Nanomedicine to Tackle Alzheimer\u2019s","volume":"16","author":"Vimal","year":"2020","journal-title":"Small"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"30347","DOI":"10.1021\/acsomega.2c03616","article-title":"Inhibition Of Tau Protein Aggregation By a Chaperone-like \u03b2-Boswellic Acid Conjugated To Gold Nanoparticles","volume":"7","author":"Gharb","year":"2022","journal-title":"ACS Omega"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5263","DOI":"10.1021\/acsnano.0c10690","article-title":"A Tauopathy-Homing and Autophagy-Activating Nanoassembly for Specific Clearance of Pathogenic Tau in Alzheimer\u2019s Disease","volume":"15","author":"Sun","year":"2021","journal-title":"ACS Nano"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Paul, P.S., Patel, T., Cho, J.-Y., Yarahmady, A., Khalili, A., Semenchenko, V., Wille, H., Kulka, M., Mok, S.-A., and Kar, S. (2024). Native PLGA Nanoparticles Attenuate A\u03b2-Seed Induced Tau Aggregation under in Vitro Conditions: Potential Implication in Alzheimer\u2019s Disease Pathology. Sci. Rep., 14.","DOI":"10.1038\/s41598-023-50465-x"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4083","DOI":"10.1021\/acs.bioconjchem.8b00697","article-title":"Harnessing Lysosomal PH through PLGA Nanoemulsion as a Treatment of Lysosomal-Related Neurodegenerative Diseases","volume":"29","author":"Soria","year":"2018","journal-title":"Bioconjug Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1080\/15548627.2015.1136769","article-title":"Nanoparticles Restore Lysosomal Acidification Defects: Implications for Parkinson and Other Lysosomal-Related Diseases","volume":"12","author":"Bourdenx","year":"2016","journal-title":"Autophagy"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3390\/biophysica1020011","article-title":"Amyloid-Mediated Mechanisms of Membrane Disruption","volume":"1","author":"Sciacca","year":"2021","journal-title":"Biophysica"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"10005","DOI":"10.1080\/07391102.2021.1939163","article-title":"Modeling Structural Interconversion in Alzheimers\u2019 Amyloid Beta Peptide with Classical and Intrinsically Disordered Protein Force Fields","volume":"40","author":"Wu","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1038\/aps.2017.28","article-title":"Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development","volume":"38","author":"Chen","year":"2017","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1134\/S002689332104004X","article-title":"Beta Amyloid, Tau Protein, and Neuroinflammation: An Attempt to Integrate Different Hypotheses of Alzheimer\u2019s Disease Pathogenesis","volume":"55","author":"Garbuz","year":"2021","journal-title":"Mol. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"20230048","DOI":"10.1002\/EXP.20230048","article-title":"The Dissolution, Reassembly and Further Clearance of Amyloid-\u03b2 Fibrils by Tailor-Designed Dissociable Nanosystem for Alzheimer\u2019s Disease Therapy","volume":"4","author":"Feng","year":"2024","journal-title":"Exploration"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5650","DOI":"10.1021\/acsami.5b00915","article-title":"Design of LVFFARK and LVFFARK-Functionalized Nanoparticles for Inhibiting Amyloid \u03b2-Protein Fibrillation and Cytotoxicity","volume":"7","author":"Xiong","year":"2015","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1804","DOI":"10.1021\/acs.langmuir.9b03612","article-title":"LVFFARK-PEG-Stabilized Black Phosphorus Nanosheets Potently Inhibit Amyloid-\u03b2 Fibrillogenesis","volume":"36","author":"Yang","year":"2020","journal-title":"Langmuir"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.nano.2016.10.006","article-title":"Retro-Inverso Peptide Inhibitor Nanoparticles as Potent Inhibitors of Aggregation of the Alzheimer\u2019s A\u03b2 Peptide","volume":"13","author":"Gregori","year":"2017","journal-title":"Nanomedicine"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.neulet.2016.12.073","article-title":"HIV-1 Tat Disrupts Blood-Brain Barrier Integrity and Increases Phagocytic Perivascular Macrophages and Microglia in the Dorsal Striatum of Transgenic Mice","volume":"640","author":"Leibrand","year":"2017","journal-title":"Neurosci. Lett."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.jcis.2024.05.193","article-title":"Serum Albumin-Embedding Copper Nanoclusters Inhibit Alzheimer\u2019s \u03b2-Amyloid Fibrillogenesis and Neuroinflammation","volume":"672","author":"Liu","year":"2024","journal-title":"J. Colloid. Interface Sci."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3780","DOI":"10.1038\/s41467-019-11762-0","article-title":"Inhibition of Amyloid Beta Toxicity in Zebrafish with a Chaperone-Gold Nanoparticle Dual Strategy","volume":"10","author":"Javed","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.1021\/acs.chemmater.1c01947","article-title":"Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles","volume":"33","author":"Andrikopoulos","year":"2021","journal-title":"Chem. Mater."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/j.nano.2017.12.006","article-title":"Antibody-Functionalized Polymer Nanoparticle Leading to Memory Recovery in Alzheimer\u2019s Disease-like Transgenic Mouse Model","volume":"14","author":"Carradori","year":"2018","journal-title":"Nanomedicine"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"6646","DOI":"10.7150\/thno.76574","article-title":"Dual-Targeted Magnetic Mesoporous Silica Nanoparticles Reduce Brain Amyloid-\u03b2 Burden via Depolymerization and Intestinal Metabolism","volume":"12","author":"Liu","year":"2022","journal-title":"Theranostics"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"4184","DOI":"10.1002\/anie.201007067","article-title":"Polyoxometalates as Inhibitors of the Aggregation of Amyloid \u03b2 Peptides Associated with Alzheimer\u2019s Disease","volume":"50","author":"Geng","year":"2011","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"3455","DOI":"10.1002\/smll.201202612","article-title":"Self-Assembled Peptide\u2013Polyoxometalate Hybrid Nanospheres: Two in One Enhances Targeted Inhibition of Amyloid \u03b2-Peptide Aggregation Associated with Alzheimer\u2019s Disease","volume":"9","author":"Li","year":"2013","journal-title":"Small"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1007\/s12274-016-1000-6","article-title":"Polyoxometalate-Based Nanozyme: Design of a Multifunctional Enzyme for Multi-Faceted Treatment of Alzheimer\u2019s Disease","volume":"9","author":"Gao","year":"2016","journal-title":"Nano Res."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.biomaterials.2016.05.005","article-title":"Ceria\/POMs Hybrid Nanoparticles as a Mimicking Metallopeptidase for Treatment of Neurotoxicity of Amyloid-\u03b2 Peptide","volume":"98","author":"Guan","year":"2016","journal-title":"Biomaterials"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"26721","DOI":"10.1021\/acsami.1c04163","article-title":"Polyoxometalates as Effective Nano-Inhibitors of Amyloid Aggregation of Pro-Inflammatory S100A9 Protein Involved in Neurodegenerative Diseases","volume":"13","author":"Chaudhary","year":"2021","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"nwae226","DOI":"10.1093\/nsr\/nwae226","article-title":"Polyoxometalates: Metallodrug Agents for Combating Amyloid Aggregation","volume":"11","author":"Ma","year":"2024","journal-title":"Natl. Sci. Rev."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"8985","DOI":"10.1002\/anie.201400735","article-title":"Maintenance of Amyloid \u03b2 Peptide Homeostasis by Artificial Chaperones Based on Mixed-Shell Polymeric Micelles","volume":"53","author":"Huang","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1021\/acsmacrolett.8b00495","article-title":"Self-Assembly Molecular Chaperone to Concurrently Inhibit the Production and Aggregation of Amyloid \u03b2 Peptide Associated with Alzheimer\u2019s Disease","volume":"7","author":"Huang","year":"2018","journal-title":"ACS Macro Lett."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1901844","DOI":"10.1002\/advs.201901844","article-title":"Heat Shock Protein Inspired Nanochaperones Restore Amyloid-\u03b2 Homeostasis for Preventative Therapy of Alzheimer\u2019s Disease","volume":"6","author":"Yang","year":"2019","journal-title":"Adv. Sci."},{"key":"ref_74","first-page":"4491","article-title":"Mimosine Functionalized Gold Nanoparticles (Mimo-AuNPs) Suppress \u03b2-Amyloid Aggregation and Neuronal Toxicity","volume":"6","author":"Anand","year":"2021","journal-title":"Bioact. Mater."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2401208","DOI":"10.1002\/adfm.202401208","article-title":"A Peptide-Polyphenol Coated Polypyrrole Nanoparticle for Synergetic Attenuation of Aggregation and Cytotoxicity of Amyloid-\u03b2 Fibrils","volume":"34","author":"Zhang","year":"2024","journal-title":"Adv. Funct. Mater."},{"key":"ref_76","first-page":"506","article-title":"Significance of Native PLGA Nanoparticles in the Treatment of Alzheimer\u2019s Disease Pathology","volume":"17","author":"Anand","year":"2022","journal-title":"Bioact. Mater."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"4032","DOI":"10.1016\/j.apsb.2021.04.022","article-title":"A Nanocleaner Specifically Penetrates the Blood\u2013brain Barrier at Lesions to Clean Toxic Proteins and Regulate Inflammation in Alzheimer\u2019s Disease","volume":"11","author":"Lei","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1038\/s41467-018-04255-z","article-title":"A Self-Destructive Nanosweeper That Captures and Clears Amyloid \u03b2-Peptides","volume":"9","author":"Luo","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Gao, V., Briano, J.A., Komer, L.E., and Burr\u00e9, J. (2023). Functional and Pathological Effects of \u03b1-Synuclein on Synaptic SNARE Complexes. J. Mol. Biol., 435.","DOI":"10.1016\/j.jmb.2022.167714"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"22680","DOI":"10.1074\/jbc.M101181200","article-title":"Ca2+ Binding to \u03b1-Synuclein Regulates Ligand Binding and Oligomerization","volume":"276","author":"Nielsen","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Fan, T.-S., Liu, S.C.-H., and Wu, R.-M. (2021). Alpha-Synuclein and Cognitive Decline in Parkinson Disease. Life, 11.","DOI":"10.3390\/life11111239"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Mori, A., Imai, Y., and Hattori, N. (2020). Lipids: Key Players That Modulate \u03b1-Synuclein Toxicity and Neurodegeneration in Parkinson\u2019s Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21093301"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Br\u00e1s, I.C., and Outeiro, T.F. (2021). Alpha-Synuclein: Mechanisms of Release and Pathology Progression in Synucleinopathies. Cells, 10.","DOI":"10.3390\/cells10020375"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., and de Bernard, M. (2013). Triggering of Inflammasome by Aggregated \u03b1\u2013Synuclein, an Inflammatory Response in Synucleinopathies. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055375"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1002\/ana.25557","article-title":"Increased Immune Activation by Pathologic \u03b1-Synuclein in Parkinson\u2019s Disease","volume":"86","author":"Grozdanov","year":"2019","journal-title":"Ann. Neurol."},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Gharb, M., Mozafari, F., Arghavani, P., Saboury, A.A., and Riazi, G. (2025). Anti-Fibrillation Effect of Gold Nanoparticles Conjugated with Boswellic Acid on \u03b1-Synuclein. Res. Sq.","DOI":"10.21203\/rs.3.rs-5383385\/v1"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"7231","DOI":"10.1021\/acs.langmuir.2c03259","article-title":"Naringenin-Functionalized Gold Nanoparticles and Their Role in \u03b1-Synuclein Stabilization","volume":"39","author":"Maity","year":"2023","journal-title":"Langmuir"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"85312","DOI":"10.1039\/C6RA08502D","article-title":"Gallic Acid Loaded onto Polyethylenimine-Coated Human Serum Albumin Nanoparticles (PEI-HSA-GA NPs) Stabilizes \u03b1-Synuclein in the Unfolded Conformation and Inhibits Aggregation","volume":"6","author":"Morshedi","year":"2016","journal-title":"RSC Adv."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"3797","DOI":"10.1007\/s10570-024-05827-7","article-title":"Adsorption of Alpha-Synuclein and Inhibition of Fibril Formation by Nanocellulose and Gold-Coated-Nanocellulose","volume":"31","author":"Keikha","year":"2024","journal-title":"Cellulose"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.ijbiomac.2020.01.269","article-title":"Interaction with Zinc Oxide Nanoparticle Kinetically Traps \u03b1-Synuclein Fibrillation into off-Pathway Non-Toxic Intermediates","volume":"150","author":"Asthana","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"6989","DOI":"10.2147\/IJN.S220380","article-title":"Cerium Oxide NPs Mitigate the Amyloid Formation of \u03b1-Synuclein and Associated Cytotoxicity","volume":"14","author":"Zand","year":"2019","journal-title":"Int. J. Nanomed."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"e21789","DOI":"10.1016\/j.heliyon.2023.e21789","article-title":"Cerium Oxide Nanoparticles Modulating the Parkinson\u2019s Disease Conditions: From the Alpha Synuclein Structural Point of View and Antioxidant Properties of Cerium Oxide Nanoparticles","volume":"10","author":"Yao","year":"2024","journal-title":"Heliyon"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Mirzaei-Behbahani, B., Meratan, A.A., Moosakhani, B., Mohammad-Zaheri, M., Mousavi-Jarrahi, Z., Nikfarjam, N., Shahsavani, M.B., and Saboury, A.A. (2024). Efficient Inhibition of Amyloid Fibrillation and Cytotoxicity of \u03b1-Synuclein and Human Insulin Using Biosynthesized Silver Nanoparticles Decorated by Green Tea Polyphenols. Sci. Rep., 14.","DOI":"10.1038\/s41598-024-54464-4"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3168","DOI":"10.1021\/acschemneuro.2c00465","article-title":"Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of \u03b1-Synuclein","volume":"13","author":"Rafiei","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"19450","DOI":"10.1039\/D0NR05003B","article-title":"Graphene Oxide Sheets and Quantum Dots Inhibit \u03b1-Synuclein Amyloid Formation by Different Mechanisms","volume":"12","author":"Ghaeidamini","year":"2020","journal-title":"Nanoscale"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1038\/s41565-018-0179-y","article-title":"Graphene Quantum Dots Prevent \u03b1-Synucleinopathy in Parkinson\u2019s Disease","volume":"13","author":"Kim","year":"2018","journal-title":"Nat. Nanotechnol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3243","DOI":"10.1021\/acsnano.8b08983","article-title":"Mechanistic Understanding of the Interactions between Nano-Objects with Different Surface Properties and \u03b1-Synuclein","volume":"13","author":"Hosseini","year":"2019","journal-title":"ACS Nano"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1186\/s13024-023-00675-8","article-title":"Peptide-Based Approaches to Directly Target Alpha-Synuclein in Parkinson\u2019s Disease","volume":"18","author":"Allen","year":"2023","journal-title":"Mol. Neurodegener."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"117452","DOI":"10.1016\/j.ejmech.2025.117452","article-title":"Rationally Designed Peptides Inhibit the Formation of \u03b1-Synuclein Fibrils and Oligomers","volume":"289","author":"Ali","year":"2025","journal-title":"Eur. J. Med. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"11982","DOI":"10.1523\/JNEUROSCI.3158-09.2009","article-title":"CD14 and Toll-Like Receptors 2 and 4 Are Required for Fibrillar A\u03b2-Stimulated Microglial Activation","volume":"29","author":"Savage","year":"2009","journal-title":"J. Neurosci."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.4049\/jimmunol.2100035","article-title":"Microglial NLRP3 Inflammasome Activation upon TLR2 and TLR5 Ligation by Distinct \u03b1-Synuclein Assemblies","volume":"207","author":"Scheiblich","year":"2021","journal-title":"J. Immunol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13024-023-00651-2","article-title":"Misfolded Protein Oligomers: Mechanisms of Formation, Cytotoxic Effects, and Pharmacological Approaches against Protein Misfolding Diseases","volume":"19","author":"Rinauro","year":"2024","journal-title":"Mol. Neurodegener."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1038\/s41467-021-21937-3","article-title":"The Release of Toxic Oligomers from \u03b1-Synuclein Fibrils Induces Dysfunction in Neuronal Cells","volume":"12","author":"Cascella","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"5512","DOI":"10.1038\/s41467-022-33252-6","article-title":"Small Soluble \u03b1-Synuclein Aggregates Are the Toxic Species in Parkinson\u2019s Disease","volume":"13","author":"Emin","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1038\/s41531-021-00195-6","article-title":"Potent Inhibitors of Toxic Alpha-Synuclein Identified via Cellular Time-Resolved FRET Biosensors","volume":"7","author":"Braun","year":"2021","journal-title":"npj Park. Dis."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Lo, C.H. (2021). Recent Advances in Cellular Biosensor Technology to Investigate Tau Oligomerization. Bioeng. Transl. Med., 6.","DOI":"10.1002\/btm2.10231"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1016\/j.jalz.2019.06.4954","article-title":"Targeting the Ensemble of Heterogeneous Tau Oligomers in Cells: A Novel Small Molecule Screening Platform for Tauopathies","volume":"15","author":"Lo","year":"2019","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Yuan, X., Yang, Y., Xia, D., Meng, L., He, M., Liu, C., and Zhang, Z. (2022). Silica Nanoparticles Promote \u03b1-Synuclein Aggregation and Parkinson\u2019s Disease Pathology. Front. Neurosci., 15.","DOI":"10.3389\/fnins.2021.807988"},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Jiang, P., Gan, M., Yen, S.-H., and Dickson, D.W. (2021). Nanoparticles With Affinity for \u03b1-Synuclein Sequester \u03b1-Synuclein to Form Toxic Aggregates in Neurons With Endolysosomal Impairment. Front. Mol. Neurosci., 14.","DOI":"10.3389\/fnmol.2021.738535"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1038\/s41580-024-00757-5","article-title":"Mechanisms of Autophagy\u2013Lysosome Dysfunction in Neurodegenerative Diseases","volume":"25","author":"Nixon","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/s41573-019-0036-1","article-title":"Lysosomes as a Therapeutic Target","volume":"18","author":"Bonam","year":"2019","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1186\/s12974-025-03410-w","article-title":"Lysosomal Acidification Impairment in Astrocyte-Mediated Neuroinflammation","volume":"22","author":"Zeng","year":"2025","journal-title":"J. Neuroinflamm."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1186\/s12974-023-02866-y","article-title":"Lysosomal Acidification Dysfunction in Microglia: An Emerging Pathogenic Mechanism of Neuroinflammation and Neurodegeneration","volume":"20","author":"Quick","year":"2023","journal-title":"J. Neuroinflamm."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.4103\/1673-5374.390979","article-title":"Autolysosomal Acidification Impairment as a Mediator for TNFR1 Induced Neuronal Necroptosis in Alzheimer\u2019s Disease","volume":"19","author":"Asimakidou","year":"2024","journal-title":"Neural Regen. Res."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.biomaterials.2019.05.002","article-title":"Nanomaterial Designing Strategies Related to Cell Lysosome and Their Biomedical Applications: A Review","volume":"211","author":"Rathore","year":"2019","journal-title":"Biomaterials"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1021\/acsomega.1c04771","article-title":"Lysosome-Targeting Strategy Using Polypeptides and Chimeric Molecules","volume":"7","author":"Mondal","year":"2022","journal-title":"ACS Omega"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"2573","DOI":"10.1038\/s41467-023-38165-6","article-title":"Restoration of Lysosomal Acidification Rescues Autophagy and Metabolic Dysfunction in Non-Alcoholic Fatty Liver Disease","volume":"14","author":"Zeng","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"15452","DOI":"10.1021\/acsnano.3c09206","article-title":"Acidic Nanoparticles Restore Lysosomal Acidification and Rescue Metabolic Dysfunction in Pancreatic \u03b2-Cells under Lipotoxic Conditions","volume":"18","author":"Lo","year":"2024","journal-title":"ACS Nano"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Cunha, A., Gaubert, A., Verget, J., Thiolat, M.-L., Barth\u00e9l\u00e9my, P., Latxague, L., and Dehay, B. (2022). Trehalose-Based Nucleolipids as Nanocarriers for Autophagy Modulation: An In Vitro Study. Pharmaceutics, 14.","DOI":"10.3390\/pharmaceutics14040857"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"e13584","DOI":"10.1111\/acel.13584","article-title":"Acidic Nanoparticles Protect against \u03b1-Synuclein-Induced Neurodegeneration through the Restoration of Lysosomal Function","volume":"21","author":"Arotcarena","year":"2022","journal-title":"Aging Cell"},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Brouillard, M., Barth\u00e9l\u00e9my, P., Dehay, B., Crauste-Manciet, S., and Desvergnes, V. (2021). Nucleolipid Acid-Based Nanocarriers Restore Neuronal Lysosomal Acidification Defects. Front. Chem., 9.","DOI":"10.3389\/fchem.2021.736554"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Lo, C.H., Ren, M., Loi, G.W.Z., Saipuljumri, E.N., Indajang, J., Lim, K.L., and Zeng, J. (2024). Lysosome-Acidifying Nanoparticles Rescue A30P \u03b1-Synuclein Induced Neuronal Death in Cellular and Drosophila Models of Parkinsons Disease. bioRxiv.","DOI":"10.1101\/2024.04.19.590288"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/s41573-021-00371-6","article-title":"PROTAC Targeted Protein Degraders: The Past Is Prologue","volume":"21","author":"Langley","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1016\/j.chembiol.2024.08.010","article-title":"New Therapies on the Horizon: Targeted Protein Degradation in Neuroscience","volume":"31","author":"Gregory","year":"2024","journal-title":"Cell Chem. Biol."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Zhou, Q., Wang, W., and Deng, C. (2025). Advancements in Proteolysis Targeting Chimeras for Targeted Therapeutic Strategies in Alzheimer\u2019s Disease. Mol. Neurobiol.","DOI":"10.1007\/s12035-025-04838-0"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/s13024-023-00630-7","article-title":"Targeted Degradation of \u237a-Synuclein Aggregates in Parkinson\u2019s Disease Using the AUTOTAC Technology","volume":"18","author":"Lee","year":"2023","journal-title":"Mol. Neurodegener."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"e00499","DOI":"10.1016\/j.neurot.2024.e00499","article-title":"Targeted Protein Degradation with Bifunctional Molecules as a Novel Therapeutic Modality for Alzheimer\u2019s Disease & Beyond","volume":"22","author":"Sandhof","year":"2024","journal-title":"Neurotherapeutics"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"23939","DOI":"10.1021\/jacs.3c05199","article-title":"Autophagy Receptor-Inspired Antibody-Fusion Proteins for Targeted Intracellular Degradation","volume":"145","author":"Jiang","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"2400149","DOI":"10.1002\/adhm.202400149","article-title":"Systemic Administration of Neurotransmitter-Derived Lipidoids-PROTACs-DNA Nanocomplex Promotes Tau Clearance and Cognitive Recovery for Alzheimer\u2019s Disease Therapy","volume":"13","author":"Gong","year":"2024","journal-title":"Adv. Healthc. Mater."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Moreira, R., N\u00f3brega, C., de Almeida, L.P., and Mendon\u00e7a, L. (2024). Brain-Targeted Drug Delivery\u2014Nanovesicles Directed to Specific Brain Cells by Brain-Targeting Ligands. J. Nanobiotechnol., 22.","DOI":"10.1186\/s12951-024-02511-7"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Zia, S., Islam Aqib, A., Muneer, A., Fatima, M., Atta, K., Kausar, T., Zaheer, C.-N.F., Ahmad, I., Saeed, M., and Shafique, A. (2023). Insights into Nanoparticles-Induced Neurotoxicity and Cope up Strategies. Front. Neurosci., 17.","DOI":"10.3389\/fnins.2023.1127460"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"e327","DOI":"10.1002\/mco2.327","article-title":"Nanoparticles-Induced Potential Toxicity on Human Health: Applications, Toxicity Mechanisms, and Evaluation Models","volume":"4","author":"Xuan","year":"2023","journal-title":"MedComm"}],"container-title":["Nanomaterials"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-4991\/15\/10\/704\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:29:32Z","timestamp":1760030972000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-4991\/15\/10\/704"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5,8]]},"references-count":132,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2025,5]]}},"alternative-id":["nano15100704"],"URL":"https:\/\/doi.org\/10.3390\/nano15100704","relation":{},"ISSN":["2079-4991"],"issn-type":[{"value":"2079-4991","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,5,8]]}}}