{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T04:52:32Z","timestamp":1771908752548,"version":"3.50.1"},"reference-count":191,"publisher":"Begell House","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Crit Rev Ther Drug Carrier Syst"],"published-print":{"date-parts":[[2024]]},"abstract":"<p>Amyloidosis is the major cause of many neurodegenerative diseases, such as, Alzheimer's and Parkinson's where the misfolding and deposition of a previously functional protein make it inept for carrying out its function. The genesis of amyloid fibril formation and the strategies to inhibit it have been studied extensively, although some parts of this puzzle still remain unfathomable to date. Many classes of molecules have been explored as potential drugs &lt;i&gt;in vitro&lt;\/i&gt;, but their inability to work &lt;i&gt;in vivo&lt;\/i&gt; by crossing the blood-brain-barrier has made them an inadequate treatment option. In this regard, nanoparticles (NPs) have turned out to be an exciting alternative because they could overcome many drawbacks of previously studied molecules and provide advantages, such as, greater bioavailability of molecules and target-specific delivery of drugs. In this paper, we present an overview on several coated NPs which have shown promising efficiency in inhibiting fibril formation. A hundred and thirty papers published in the past two decades have been comprehensively reviewed, which majorly encompass NPs comprising different materials like gold, silver, iron-oxide, poly(lactic-co-glycolic acid), polymeric NP, etc., which are coated with various molecules of predominantly natural origin, such as different types of amino acids, peptides, curcumin, drugs, catechin, etc. We hope that this review will shed light on the advancement of symbiotic amalgamation of NPs with molecules from natural sources and will inspire further research on the tremendous therapeutic potential of these combinations for many amyloid-related diseases.\n<\/p>","DOI":"10.1615\/critrevtherdrugcarriersyst.2023046209","type":"journal-article","created":{"date-parts":[[2023,6,30]],"date-time":"2023-06-30T17:23:06Z","timestamp":1688145786000},"page":"85-119","source":"Crossref","is-referenced-by-count":5,"title":["Targeting Amyloids with Coated Nanoparticles: A Review on Potential Combinations of Nanoparticles and Bio-Compatible Coatings"],"prefix":"10.1615","volume":"41","author":[{"given":"Oshin D.","family":"Warerkar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niyati H.","family":"Mudliar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Munira M.","family":"Momin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prabhat K.","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"613","reference":[{"key":"2","doi-asserted-by":"crossref","unstructured":"Selkoe DJ. Folding proteins in fatal ways. Nature. 2003;426:900-4.","DOI":"10.1038\/nature02264"},{"key":"3","doi-asserted-by":"crossref","unstructured":"Jana NR, Nukina N. Recent advances in understanding the pathogenesis of polyglutamine diseases: Involvement of molecular chaperones and ubiquitin-proteasome pathway. J Chem Neuroanat. 2003;26(2):95-101.","DOI":"10.1016\/S0891-0618(03)00029-2"},{"key":"4","doi-asserted-by":"crossref","unstructured":"Rambaran RN, Serpell LC. Amyloid fibrils: Abnormal protein assembly. Prion. 2008;2(3):112-7.","DOI":"10.4161\/pri.2.3.7488"},{"key":"5","doi-asserted-by":"crossref","unstructured":"Querfurth HW, LaFerla FM. Alzheimer's disease. N Engl J Med. 2010;362(4):329-44.","DOI":"10.1056\/NEJMra0909142"},{"key":"6","doi-asserted-by":"crossref","unstructured":"Paulson HL, Perez MK, Trottier Y, Trojanowski JQ, Subramony SH, Das SS, Vig P, Mandel JL, Fischbeck KH, Pittman RN. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron. 1997;19(2):333-44.","DOI":"10.1016\/S0896-6273(00)80943-5"},{"key":"7","doi-asserted-by":"crossref","unstructured":"Skovronsky DM, Lee VM-Y, Trojanowski JQ. Neurodegenerative diseases: New concepts of pathogenesis and their therapeutic implications. Annu Rev Pathol. 2006;1:151-70.","DOI":"10.1146\/annurev.pathol.1.110304.100113"},{"key":"8","doi-asserted-by":"crossref","unstructured":"Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med. 2004;10:S10-7.","DOI":"10.1038\/nm1066"},{"key":"9","doi-asserted-by":"crossref","unstructured":"Blokhuis AM, Groen EJN, Koppers M, van den Berg LH, Pasterkamp RJ. Aggregation in amyotrophic lateral sclerosis. Acta Neuropathol. 2013;125(6):777-94.","DOI":"10.1007\/s00401-013-1125-6"},{"key":"10","doi-asserted-by":"crossref","unstructured":"Aguzzi A, Calella AM. Prions: Protein aggregation and infectious diseases. Physiol Rev. 2009;89(4):1105-52.","DOI":"10.1152\/physrev.00006.2009"},{"key":"11","doi-asserted-by":"crossref","unstructured":"Moreau KL, King JA. Protein misfolding and aggregation in cataract disease and prospects for prevention. Trends Mol Med. 2012;18(5):273\u201382.","DOI":"10.1016\/j.molmed.2012.03.005"},{"key":"12","doi-asserted-by":"crossref","unstructured":"Marzban L, Park K, Verchere CB. Islet amyloid polypeptide and type 2 diabetes. Exp Gerontol. 2003;38(4):347-51.","DOI":"10.1016\/S0531-5565(03)00004-4"},{"key":"13","doi-asserted-by":"crossref","unstructured":"Selkoe DJ. Amyloid beta protein precursor and the pathogenesis of Alzheimer's disease cell. 1989;58: 611-2.","DOI":"10.1016\/0092-8674(89)90093-7"},{"key":"14","doi-asserted-by":"crossref","unstructured":"Sisodia SS, Price DL. Role of the beta-amyloid protein in Alzheimer's disease. FASEB J. 1995;9(5):366-70.","DOI":"10.1096\/fasebj.9.5.7896005"},{"key":"15","doi-asserted-by":"crossref","unstructured":"Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006;75:333-6.","DOI":"10.1146\/annurev.biochem.75.101304.123901"},{"key":"16","doi-asserted-by":"crossref","unstructured":"Sakono M, Zako T. Amyloid oligomers: Formation and toxicity of AB oligomers. FEBS J. 2010;277(6):1348-58.","DOI":"10.1111\/j.1742-4658.2010.07568.x"},{"key":"17","doi-asserted-by":"crossref","unstructured":"Kocahan S, Dogan Z. Mechanisms of Alzheimer's disease pathogenesis and prevention: The brain, neural pathology, N-methyl-D-aspartate receptors, tau protein and other risk factors. Clin Psychopharmacol Neurosci. 2017;15(1):1-8.","DOI":"10.9758\/cpn.2017.15.1.1"},{"key":"18","doi-asserted-by":"crossref","unstructured":"Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science. 2002;297(5590):353-6.","DOI":"10.1126\/science.1072994"},{"key":"19","doi-asserted-by":"crossref","unstructured":"Barage SH, Sonawane KD. Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease. Neuropeptides. 2015;52:1-18.","DOI":"10.1016\/j.npep.2015.06.008"},{"key":"20","doi-asserted-by":"crossref","unstructured":"Manno M, Craparo EF, Martorana V, Bulone D, San Biagio PL. Kinetics of insulin aggregation: Disentanglement of amyloid fibrillation from large-size cluster formation. Biophys J. 2006;90(12):4585-91.","DOI":"10.1529\/biophysj.105.077636"},{"key":"21","doi-asserted-by":"crossref","unstructured":"Malik R, Roy I. Probing the mechanism of insulin aggregation during agitation. Int J Pharm. 2011;413(1-2):73-80.","DOI":"10.1016\/j.ijpharm.2011.04.024"},{"key":"22","doi-asserted-by":"crossref","unstructured":"Surveswaran S, Cai Y-Z, Corke H, Sun M. Systematic evaluation of natural phenolic antioxidants from 133 Indian medicinal plants. Food Chem. 2007;102(3):938-53.","DOI":"10.1016\/j.foodchem.2006.06.033"},{"key":"23","doi-asserted-by":"crossref","unstructured":"Hsieh S, Chang C-W, Chou H-H. Gold nanoparticles as amyloid-like fibrillogenesis inhibitors. Colloids Surf B Biointerfaces. 2013;112:525-9.","DOI":"10.1016\/j.colsurfb.2013.08.029"},{"key":"24","doi-asserted-by":"crossref","unstructured":"Patil SD, Rhodes DG, Burgess DJ. DNA-based therapeutics and DNA delivery systems: A comprehensive review. AAPS J. 2005;7:E61-77.","DOI":"10.1208\/aapsj070109"},{"key":"25","doi-asserted-by":"crossref","unstructured":"El-Sayed IH, Huang X, El-Sayed MA. Surface plasmon resonance scattering and absorption of anti-EGFR antibody conjugated gold nanoparticles in cancer diagnostics: Applications in oral cancer. Nano Lett. 2005;5(5):829-34.","DOI":"10.1021\/nl050074e"},{"key":"26","doi-asserted-by":"crossref","unstructured":"Tiwari PM, Vig K, Dennis VA, Singh SR. Functionalized gold nanoparticles and their biomedical applications. Nanomaterials. 2011;1(1):31-63.","DOI":"10.3390\/nano1010031"},{"key":"27","doi-asserted-by":"crossref","unstructured":"Torchilin VP. Multifunctional nanocarriers. Adv Drug Deliv Rev. 2006;58(14):1532-55.","DOI":"10.1016\/j.addr.2006.09.009"},{"key":"28","doi-asserted-by":"crossref","unstructured":"El-Sayed IH, Huang X, El-Sayed MA. Selective laser photo-thermal therapy of epithelial carcinoma using anti-EGFR antibody conjugated gold nanoparticles. Cancer Lett. 2006;239(1):129-35.","DOI":"10.1016\/j.canlet.2005.07.035"},{"key":"29","doi-asserted-by":"crossref","unstructured":"Zhuang Z-P, Kung M-P, Hou C, Skovronsky DM, Gur TL, Pl\u00f6ssl K, Trojanowski JQ, Lee VM-Y, Kung HF. Radioiodinated styrylbenzenes and thioflavins as probes for amyloid aggregates. J Med Chem. 2011;44(12):1905-14.","DOI":"10.1021\/jm010045q"},{"key":"30","doi-asserted-by":"crossref","unstructured":"Kanwar JR, Sun X, Punj V, Sriramoju B, Mohan RR, Zhou S-F, Chauhan A, Kanwar RK. Nanoparticles in the treatment and diagnosis of neurological disorders: Untamed dragon with fire power to heal. Nanomedicine. 2012;8(4):399-414.","DOI":"10.1016\/j.nano.2011.08.006"},{"key":"31","doi-asserted-by":"crossref","unstructured":"Jain A, Jain A, Gulbake A, Shilpi S, Hurkat P, Jain SK. Peptide and protein delivery using new drug delivery systems. Crit Rev Ther Drug Carrier Syst. 2013;30(4):293-329.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.2013006955"},{"key":"32","unstructured":"Kumar HK, Venkatesh N, Bhowmik H, Kuila A. Metallic nanoparticle: A review. Biomed J Sci Tech Res. 2018;4(2)3765-75."},{"key":"33","doi-asserted-by":"crossref","unstructured":"Mody V, Siwale R, Singh A, Mody H. Introduction to metallic nanoparticles. J Pharm Bioallied Sci. 2010;2(4):282-9.","DOI":"10.4103\/0975-7406.72127"},{"key":"34","doi-asserted-by":"crossref","unstructured":"Smith QR. A review of blood-brain barrier transport techniques. Methods Mol Med. 2003;89:193-208.","DOI":"10.1385\/1-59259-419-0:193"},{"key":"35","doi-asserted-by":"crossref","unstructured":"Yoo SI, Yang M, Brender JR, Subramanian V, Sun K, Joo NE, Jeong S-H, Ramamoorthy A, Kotov NA. Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: Functional similarities with proteins. Angew Chem. 2011;50(22):5110-5.","DOI":"10.1002\/anie.201007824"},{"key":"36","doi-asserted-by":"crossref","unstructured":"Agyare EK, Curran GL, Ramakrishnan M, Yu CC, Poduslo JF, Kandimalla KK. Development of a smart nano-vehicle to target cerebrovascular amyloid deposits and brain parenchymal plaques observed in Alzheimer's disease and cerebral amyloid angiopathy. Pharm Res. 2008;25(11):2674-84.","DOI":"10.1007\/s11095-008-9688-y"},{"key":"37","doi-asserted-by":"crossref","unstructured":"Cabaleiro-Lago C, Quinlan-Pluck F, Lynch I, Lindman S, Minogue AM, Thulin E, Walsh DM, Dawson KA, Linse S. Inhibition of amyloid beta protein fibrillation by polymeric nanoparticles. J Am Chem Soc. 2008;130(46):15437-43.","DOI":"10.1021\/ja8041806"},{"key":"38","doi-asserted-by":"crossref","unstructured":"Porat Y, Abramowitz A, Gazit E. Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des. 2005;67(1):27-37.","DOI":"10.1111\/j.1747-0285.2005.00318.x"},{"key":"39","doi-asserted-by":"crossref","unstructured":"Xie H, Peng J, Liu C, Fang X, Duan H, Zou Y, Yang Y, Wang C. Aromatic-interaction-mediated inhibition of B-amyloid assembly structures and cytotoxicity. J Pept Sci. 2017;23:679-84.","DOI":"10.1002\/psc.3011"},{"key":"40","doi-asserted-by":"crossref","unstructured":"Lee C-C, Nayak A, Sethuraman A, Belfort G, McRae GJ. A three-stage kinetic model of amyloid fibrillation. Biophys J. 2007;92(10):3448-58.","DOI":"10.1529\/biophysj.106.098608"},{"key":"41","doi-asserted-by":"crossref","unstructured":"Gazit E. A possible role for \u03c0-stacking in the self-assembly of amyloid fibrils. FASEB J. 2002;16(1):77-83.","DOI":"10.1096\/fj.01-0442hyp"},{"key":"42","doi-asserted-by":"crossref","unstructured":"Liu H, Xie B, Dong X, Zhang L, Wang Y, Liu F, Sun Y. Negatively charged hydrophobic nanoparticles inhibit amyloid B-protein fibrillation: The presence of an optimal charge density. React Funct Polym. 2016;103(C):108-16.","DOI":"10.1016\/j.reactfunctpolym.2016.04.003"},{"key":"43","doi-asserted-by":"crossref","unstructured":"Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry. 2001;40(20):6036-46.","DOI":"10.1021\/bi002555c"},{"key":"44","doi-asserted-by":"crossref","unstructured":"Xiao L, Zhao D, Chan W, Choi M, Li H. Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots. Biomaterials. 2010;31(1):91-8.","DOI":"10.1016\/j.biomaterials.2009.09.014"},{"key":"45","doi-asserted-by":"crossref","unstructured":"Benelli G, Lukehart CM. Special issue: Applications of green-synthesized nanoparticles in pharmacology, parasitology and entomology. J Clust Sci. 2017;28(1):1-2.","DOI":"10.1007\/s10876-017-1165-5"},{"key":"46","doi-asserted-by":"crossref","unstructured":"Zaman M, Ahmad E, Qadeer A, Rabbani G, Khan R. Nanoparticles in relation to peptide and protein aggregation. Int J Nanomedicine. 2014;9(1):899-912.","DOI":"10.2147\/IJN.S54171"},{"key":"47","doi-asserted-by":"crossref","unstructured":"Wang H, Gao XD, Zhou GC, Cai L, Yao WB. In vitro and in vivo antioxidant activity of aqueous extract from Choerospondias axillaris fruit. Food Chem. 2008;106(3):888-95.","DOI":"10.1016\/j.foodchem.2007.05.068"},{"key":"48","doi-asserted-by":"crossref","unstructured":"Kogan MJ, Bastus NG, Amigo R, Grillo-Bosch D, Araya E, Turiel A, Labarta A, Giralt E, Puntes VF. Nanoparticle-mediated local and remote manipulation of protein aggregation. Nano Letters. 2005;6(1):110-5.","DOI":"10.1021\/nl0516862"},{"key":"49","doi-asserted-by":"crossref","unstructured":"Jana NR, Earhart C, Ying JY. Synthesis of water-soluble and functionalized nanoparticles by silica coating. Chem Mater. 2007;19(21):5074-82.","DOI":"10.1021\/cm071368z"},{"key":"50","doi-asserted-by":"crossref","unstructured":"Lohse SE, Murphy CJ. Applications of colloidal inorganic nanoparticles: From medicine to energy. J Am Chem Soc. 2012;134(38):15607-20.","DOI":"10.1021\/ja307589n"},{"key":"51","doi-asserted-by":"crossref","unstructured":"Alharbi KK, Al-sheikh YA. Role and implications of nanodiagnostics in the changing trends of clinical diagnosis. Saudi J Biol Sci. 2014;21(2):109-17.","DOI":"10.1016\/j.sjbs.2013.11.001"},{"key":"52","doi-asserted-by":"crossref","unstructured":"Seo JM, Kim EB, Hyun MS, Kim BB, Park TJ. Self-assembly of biogenic gold nanoparticles and their use to enhance drug delivery into cells. Colloids Surf B Biointerfaces. 2015;135:27-34.","DOI":"10.1016\/j.colsurfb.2015.07.022"},{"key":"53","doi-asserted-by":"crossref","unstructured":"Sherwani MA, Tufail S, Khan AA, Owais M. Gold nanoparticle-photosensitizer conjugate based photodynamic inactivation of biofilm producing cells: Potential for treatment of C. albicans infection in BALB\/c mice. PLoS One. 2015;10(7):e0131684.","DOI":"10.1371\/journal.pone.0131684"},{"key":"54","doi-asserted-by":"crossref","unstructured":"Saha A, Pawar VM, Jayaraman S. Characterisation of polyphenols in terminalia arjuna bark extract. Indian J Pharm Sci. 2012;74(4):339-47.","DOI":"10.4103\/0250-474X.107067"},{"key":"55","doi-asserted-by":"crossref","unstructured":"Chen Y-S, Hung Y-C, Liau I, Huang GS. Assessment of the in vivo toxicity of gold nanoparticles. Nanoscale Res Lett. 2009;4(8):858.","DOI":"10.1007\/s11671-009-9334-6"},{"key":"56","doi-asserted-by":"crossref","unstructured":"Lewinski N, Colvin V, Drezek R. Cytotoxicity of nanoparticles. Small. 2008;4(1):26-49.","DOI":"10.1002\/smll.200700595"},{"key":"57","doi-asserted-by":"crossref","unstructured":"Sani A, Cao C, Cui D. Toxicity of gold nanoparticles (AuNPs): A review. Biochem Biophys Rep. 2021;26:100991.","DOI":"10.1016\/j.bbrep.2021.100991"},{"key":"58","doi-asserted-by":"crossref","unstructured":"Yang Y, Qin Z, Zeng W, Yang T, Cao Y, Mei C, Kuang Y. Toxicity assessment of nanoparticles in various systems and organs. Nanotechnol Rev. 2017;6(3):279-89.","DOI":"10.1515\/ntrev-2016-0047"},{"key":"59","doi-asserted-by":"crossref","unstructured":"Amini A, Kamali M, Amini B, Najafi A. Enhanced antibacterial activity of imipenem immobilized on surface of spherical and rod gold nanoparticles. J Phys D Appl Phys. 2019;52(6):065401.","DOI":"10.1088\/1361-6463\/aaef4d"},{"key":"60","doi-asserted-by":"crossref","unstructured":"Singh R, Patil S, Singh N, Gupta S. Dual functionality nanobioconjugates targeting intracellular bacteria in cancer cells with enhanced antimicrobial activity. Sci Rep. 2017;7(1):5792.","DOI":"10.1038\/s41598-017-06014-4"},{"key":"61","doi-asserted-by":"crossref","unstructured":"Dhamecha D, Jalalpure S, Jadhav K, Sajjan D. Green synthesis of gold nanoparticles using Pterocarpus marsupium: Characterization and biocompatibility studies. Part Sci Technol. 2016;34(2):156-64.","DOI":"10.1080\/02726351.2015.1054972"},{"key":"62","doi-asserted-by":"crossref","unstructured":"Suganthy N, Sri Ramkumar V, Pugazhendhi A, Benelli G, Archunan G. Biogenic synthesis of gold nanoparticles from Terminalia arjuna bark extract: Assessment of safety aspects and neuroprotective potential via antioxidant, anticholinesterase, and antiamyloidogenic effects. Environ Sci Pollut Res. 2017;25(11):10418-33.","DOI":"10.1007\/s11356-017-9789-4"},{"key":"63","doi-asserted-by":"crossref","unstructured":"Tavanti F, Pedone A, Menziani MC. Competitive binding of proteins to gold nanoparticles disclosed by molecular dynamics simulations. J Phys Chem C. 2015;119(38):22172-80.","DOI":"10.1021\/acs.jpcc.5b05796"},{"key":"64","doi-asserted-by":"crossref","unstructured":"Stevanovic M, Uskokovic D. Poly(lactide-co-glycolide)-based micro and nanoparticles for the controlled drug delivery of vitamins. Curr Nanosci. 2009;5(1):1-14.","DOI":"10.2174\/157341309787314566"},{"key":"65","doi-asserted-by":"crossref","unstructured":"Zhao L, Xin Y, Li Y, Yang X, Luo L, Meng F. Ultraeffective inhibition of amyloid fibril assembly by nanobody-gold nanoparticle conjugates. Bioconjug Chem. 2019;30(1):29-33.","DOI":"10.1021\/acs.bioconjchem.8b00797"},{"key":"66","doi-asserted-by":"crossref","unstructured":"Gorgani L, Mohammadi M, Najafpour GD, Nikzad M. Piperine-The bioactive compound of black pepper: from isolation to medicinal formulations. Compr Rev Food Sci Food Saf. 2017;16(1):124-40.","DOI":"10.1111\/1541-4337.12246"},{"key":"67","doi-asserted-by":"crossref","unstructured":"Derosa G, Maffioli P, Sahebkar A. Piperine and its role in chronic diseases. In: Gupta SC, Prasad S, Aggarwal BB, editors. Anti-inflammatory nutraceuticals and chronic diseases. Cham: Springer International Publishing; 2016. p. 173-84.","DOI":"10.1007\/978-3-319-41334-1_8"},{"key":"68","doi-asserted-by":"crossref","unstructured":"Meghwal M, Goswami TK. Piper nigrum and piperine: An update. Phytother Res. 2013;27(8):1121-30.","DOI":"10.1002\/ptr.4972"},{"key":"69","doi-asserted-by":"crossref","unstructured":"Singletary K. Black pepper: Overview of health benefits. Nutr Today. 2010;45(1):43-7.","DOI":"10.1097\/NT.0b013e3181cb4539"},{"key":"70","doi-asserted-by":"crossref","unstructured":"Anand BG, Shekhawat DS, Dubey K, Kar K. Uniform, polycrystalline, and thermostable piperinecoated gold nanoparticles to target insulin fibril assembly. ACS Biomater Sci Eng. 2017;3(6):1136-45.","DOI":"10.1021\/acsbiomaterials.7b00030"},{"key":"71","doi-asserted-by":"crossref","unstructured":"Mishra NK, Deepak RNVK, Sankararamakrishnan R, Verma S. Controlling in vitro insulin amyloidosis with stable peptide conjugates: A combined experimental and computational study. J Phys Chem B. 2015;119(50):15395-406.","DOI":"10.1021\/acs.jpcb.5b08215"},{"key":"72","doi-asserted-by":"crossref","unstructured":"Gao N, Sun H, Dong K, Ren J, Duan T, Xu C, Qu X. Transition-metal-substituted polyoxometalate derivatives as functional anti-amyloid agents for Alzheimer's disease. Nat Commun. 2014;5(1):3422.","DOI":"10.1038\/ncomms4422"},{"key":"73","doi-asserted-by":"crossref","unstructured":"Zhang W, Christofferson AJ, Besford QA, Richardson JJ, Guo J, Ju Y, Kempe K, Yarovsky I, Caruso F. Metal-dependent inhibition of amyloid fibril formation: Synergistic effects of cobalt\u2013tannic acid networks. Nanoscale. 2019;11(4):1921-8.","DOI":"10.1039\/C8NR09221D"},{"key":"74","doi-asserted-by":"crossref","unstructured":"Meesaragandla B, Karanth S, Janke U, Delcea M. Biopolymer-coated gold nanoparticles inhibit human insulin amyloid fibrillation. Sci Rep. 2020;10(1):7862.","DOI":"10.1038\/s41598-020-64010-7"},{"key":"75","doi-asserted-by":"crossref","unstructured":"Desai KG. Chitosan nanoparticles prepared by ionotropic gelation: An overview of recent advances. Crit Rev Ther Drug Carrier Syst. 2016;33(2):107-58.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.2016014850"},{"key":"76","doi-asserted-by":"crossref","unstructured":"Maher P. The effects of stress and aging on glutathione metabolism. Ageing Res Rev. 2005;4(2):288-314.","DOI":"10.1016\/j.arr.2005.02.005"},{"key":"77","doi-asserted-by":"crossref","unstructured":"Antosova A, Gazova Z, Fedunova D, Valusova E, Bystrenova E, Valle F, Daxnerova Z, Biscarini F, Antalik M. Anti-amyloidogenic activity of glutathione-covered gold nanoparticles. Mater Sci Eng C. 2012;32(8):2529-35.","DOI":"10.1016\/j.msec.2012.07.036"},{"key":"78","doi-asserted-by":"crossref","unstructured":"Zhang X-D, Wu D, Shen X, Liu P-X, Fan F-Y, Fan S-J. In vivo renal clearance, biodistribution, toxicity of gold nanoclusters. Biomaterials. 2012;33(18):4628-38.","DOI":"10.1016\/j.biomaterials.2012.03.020"},{"key":"79","doi-asserted-by":"crossref","unstructured":"Dubey K, Anand BG, Badhwar R, Bagler G, Navya PN, Daima HK, Kar K. Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin. J Amino Acids. 2015;47(12): 2551-60.","DOI":"10.1007\/s00726-015-2046-6"},{"key":"80","doi-asserted-by":"crossref","unstructured":"Maruyama T, Fujimoto Y, Maekawa T. Synthesis of gold nanoparticles using various amino acids. J Colloid Interface Sci. 2015;447:254-7.","DOI":"10.1016\/j.jcis.2014.12.046"},{"key":"81","doi-asserted-by":"crossref","unstructured":"Karmakar S, Sarkar N, Pandey LM. Proline functionalized gold nanoparticles modulates lysozyme fibrillation. Colloids Surf B Biointerfaces. 2019;174(1):401-8.","DOI":"10.1016\/j.colsurfb.2018.11.032"},{"key":"82","doi-asserted-by":"crossref","unstructured":"Li SC, Goto NK, Williams KA, Deber CM. Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment. Proc Natl Acad Sci U S A. 1996;93(13):6676-81.","DOI":"10.1073\/pnas.93.13.6676"},{"key":"83","doi-asserted-by":"crossref","unstructured":"Samuel D, Ganesh G, Yang P-W, Chang M-M, Wang S-L, Hwang K-C, Yu C, Jayaraman G, Kumar TKS, Trivedi VD, Chang D-K. Proline inhibits aggregation during protein refolding. Protein Sci. 2000;9(2):344-52.","DOI":"10.1110\/ps.9.2.344"},{"key":"84","doi-asserted-by":"crossref","unstructured":"Palmal S, Jana NR, Jana NR. Inhibition of amyloid fibril growth by nanoparticle coated with histidine-based polymer. J Phys Chem C. 2014;118(37):21630-8.","DOI":"10.1021\/jp505613g"},{"key":"85","doi-asserted-by":"crossref","unstructured":"Saha A, Basiruddin SK, Sarkar R, Pradhan N, Jana NR. Functionalized plasmonic-fluorescent nanoparticles for imaging and detection. J Phys Chem C. 2009;113(43):18492-8.","DOI":"10.1021\/jp904791h"},{"key":"86","doi-asserted-by":"crossref","unstructured":"Hao S, Li X, Han A, Yang Y, Fang G, Liu J, Wang S. CLVFFA-functionalized gold nanoclusters inhibit AB40 fibrillation, fibrils' prolongation, and mature fibrils' disaggregation. ACS Chem Neurosci. 2019;10(11):4633-42.","DOI":"10.1021\/acschemneuro.9b00469"},{"key":"87","doi-asserted-by":"crossref","unstructured":"Agrachev M, Ruzzi M, Venzo A, Maran F. Nuclear and electron magnetic resonance spectroscopies of atomically precise gold nanoclusters. Acc Chem Res. 2018;52(1):44-52.","DOI":"10.1021\/acs.accounts.8b00495"},{"key":"88","doi-asserted-by":"crossref","unstructured":"Luo Z, Yuan X, Yu Y, Zhang Q, Leong DT, Lee JY, Xie J. From aggregation-induced emission of Au(I)-thiolate complexes to ultrabright Au(0)@Au(I)-thiolate core-shell nanoclusters. J Am Chem Soc. 2012;134(40):16662-70.","DOI":"10.1021\/ja306199p"},{"key":"89","doi-asserted-by":"crossref","unstructured":"Chakraborty P, Nag A, Chakraborty A, Pradeep T. Approaching materials with atomic precision using supramolecular cluster assemblies. Acc Chem Res. 2018;52(1):2-11.","DOI":"10.1021\/acs.accounts.8b00369"},{"key":"90","doi-asserted-by":"crossref","unstructured":"Hesari M, Ding Z. A grand avenue to Au nanocluster electrochemiluminescence. Acc Chem Res. 2017;50(2):218-30.","DOI":"10.1021\/acs.accounts.6b00441"},{"key":"91","doi-asserted-by":"crossref","unstructured":"Kwak K, Lee D. Electrochemistry of atomically precise metal nanoclusters. Acc Chem Res. 2018;52(1):12-22.","DOI":"10.1021\/acs.accounts.8b00379"},{"key":"92","doi-asserted-by":"crossref","unstructured":"Wang S, Li Q, Kang X, Zhu M. Customizing the structure, composition, and properties of alloy nanoclusters by metal exchange. Acc Chem Res. 2018;51(11):2784-92.","DOI":"10.1021\/acs.accounts.8b00327"},{"key":"93","doi-asserted-by":"crossref","unstructured":"Yan J, Teo BK, Zheng N. Surface chemistry of atomically precise coinage-metal nanoclusters: From structural control to surface reactivity and catalysis. Acc Chem Res. 2018;51(12):3084-93.","DOI":"10.1021\/acs.accounts.8b00371"},{"key":"94","doi-asserted-by":"crossref","unstructured":"Qian H, Zhu M, Wu Z, Jin R. Quantum sized gold nanoclusters with atomic precision. Acc Chem Res. 2012;45(9):1470-9.","DOI":"10.1021\/ar200331z"},{"key":"95","doi-asserted-by":"crossref","unstructured":"Yang Y, Han A, Li R, Fang G, Liu J, Wang S. Synthesis of highly fluorescent gold nanoclusters and their use in sensitive analysis of metal ions. Analyst. 2017;142(23):4486-93.","DOI":"10.1039\/C7AN01348E"},{"key":"96","doi-asserted-by":"crossref","unstructured":"Gao G, Chen R, He M, Li J, Li J, Wang L, Sun T. Gold nanoclusters for Parkinson's disease treatment. Biomater. 2019;194:36-46.","DOI":"10.1016\/j.biomaterials.2018.12.013"},{"key":"97","doi-asserted-by":"crossref","unstructured":"Zhang E, Fu A. A new strategy for specific imaging of neural cells based on peptide-conjugated gold nanoclusters. Int J Nanomedicine. 2015;10:2115-24.","DOI":"10.2147\/IJN.S78554"},{"key":"98","doi-asserted-by":"crossref","unstructured":"Herbig ME, Weller KM, Merkle HP. Reviewing biophysical and cell biological methodologies in cell-penetrating peptide (CPP) research. Crit Rev Ther Drug Carrier Syst. 2007;24(3):203-55.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.v24.i3.10"},{"key":"99","doi-asserted-by":"crossref","unstructured":"Esatbeyoglu T, Huebbe P, Ernst IMA, Chin D, Wagner AE, Rimbach G. Curcumin-from molecule to biological function. Angew Chem, Int Ed Engl. 2012;51(22):5308-32.","DOI":"10.1002\/anie.201107724"},{"key":"100","doi-asserted-by":"crossref","unstructured":"Goel A, Kunnumakkara AB, Aggarwal BB. Curcumin as 'Curcumin': From kitchen to clinic. Biochem Pharmacol. 2008;75(4):787-809.","DOI":"10.1016\/j.bcp.2007.08.016"},{"key":"101","doi-asserted-by":"crossref","unstructured":"Cartiera MS, Ferreira EC, Caputo C, Egan ME, Caplan MJ, Saltzman WM. Partial correction of cystic fibrosis defects with PLGA nanoparticles encapsulating curcumin. Mol Pharm. 2010;7(1):86-93.","DOI":"10.1021\/mp900138a"},{"key":"102","doi-asserted-by":"crossref","unstructured":"Ringman MJ, Frautschy AS, Cole MG, Masterman LD, Cummings LJ. A potential role of the curry spice curcumin in alzheimers disease. Curr Alzheimer Res. 2005;2(2):131-6.","DOI":"10.2174\/1567205053585882"},{"key":"103","doi-asserted-by":"crossref","unstructured":"Park S-Y, Kim H-S, Cho E-K, Kwon B-Y, Phark S, Hwang K-W, Sul D. Curcumin protected PC12 cells against beta-amyloid-induced toxicity through the inhibition of oxidative damage and tau hyperphosphorylation. Food Chem Toxicol. 2008;46(8):2881-7.","DOI":"10.1016\/j.fct.2008.05.030"},{"key":"104","doi-asserted-by":"crossref","unstructured":"Lim GP, Chu T, Yang F, Beech W, Frautschy SA, Cole GM. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci. 2001;21(21):8370.","DOI":"10.1523\/JNEUROSCI.21-21-08370.2001"},{"key":"105","doi-asserted-by":"crossref","unstructured":"Mishra S, Palanivelu K. The effect of curcumin (turmeric) on Alzheimer's disease: An overview. Ann Indian Acad Neurol. 2008;11(1):13-9.","DOI":"10.4103\/0972-2327.40220"},{"key":"106","doi-asserted-by":"crossref","unstructured":"Frautschy SA, Hu W, Kim P, Miller SA, Chu T, Harris-White ME, Cole GM. Phenolic anti-inflammatory antioxidant reversal of AB-induced cognitive deficits and neuropathology. Neurobiol Aging. 2001;22(6):993-1005.","DOI":"10.1016\/S0197-4580(01)00300-1"},{"key":"107","doi-asserted-by":"crossref","unstructured":"Ono K, Hasegawa K, Naiki H, Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's B-amyloid fibrils in vitro. J NeurosciRes. 2004;75(6):742-50.","DOI":"10.1002\/jnr.20025"},{"key":"108","doi-asserted-by":"crossref","unstructured":"Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen PP, Kayed R, Glabe CG, Frautschy SA, Cole GM. Curcumin inhibits formation of amyloid B oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem. 2005;280(7):5892-901.","DOI":"10.1074\/jbc.M404751200"},{"key":"109","doi-asserted-by":"crossref","unstructured":"Dikshit P, Goswami A, Mishra A, Nukina N, Jana NR. Curcumin enhances the polyglutamine-expanded truncated N-terminal huntingtin-induced cell death by promoting proteasomal malfunction. Biochem Biophys Res Commun. 2006;342(4):1323-8.","DOI":"10.1016\/j.bbrc.2006.02.104"},{"key":"110","doi-asserted-by":"crossref","unstructured":"Garcia-Alloza M, Borrelli LA, Rozkalne A, Hyman BT, Bacskai BJ. Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model. J Neurochem. 2007;102(4):1095-104.","DOI":"10.1111\/j.1471-4159.2007.04613.x"},{"key":"111","doi-asserted-by":"crossref","unstructured":"Shi W, Dolai S, Rizk S, Hussain A, Tariq H, Averick S, L'Amoreaux W, El Idrissi A, Banerjee P, Raja K. Synthesis of monofunctional curcumin derivatives, clicked curcumin dimer, and a PAMAM dendrimer curcumin conjugate for therapeutic applications. Org Lett. 2007;9(26):5461-4.","DOI":"10.1021\/ol702370m"},{"key":"112","doi-asserted-by":"crossref","unstructured":"Wang SSS, Liu K-N, Lee W-H. Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme. Biophys Chem. 2009;144(1):78-87.","DOI":"10.1016\/j.bpc.2009.06.010"},{"key":"113","doi-asserted-by":"crossref","unstructured":"Ran C, Xu X, Raymond SB, Ferrara BJ, Neal K, Bacskai BJ, Medarova Z, Moore A. Design, synthesis, and testing of difluoroboron-derivatized curcumins as near-infrared probes for in vivo detection of amyloid-B deposits. J Am Chem Soc. 2009;131(42):15257-61.","DOI":"10.1021\/ja9047043"},{"key":"114","doi-asserted-by":"crossref","unstructured":"Sharma S, Ying Z, Gomez-Pinilla F. A pyrazole curcumin derivative restores membrane homeostasis disrupted after brain trauma. Exp Neurol. 2010;226(1):191-9.","DOI":"10.1016\/j.expneurol.2010.08.027"},{"key":"115","doi-asserted-by":"crossref","unstructured":"Dolai S, Shi W, Corbo C, Sun C, Averick S, Obeysekera D, Farid M, Alonso A, Banerjee P, Raja K. 'Clicked' sugar-curcumin conjugate: Modulator of amyloid-\u03b2 and tau peptide aggregation at ultralow concentrations. ACS Chem Neurosci. 2011;2(12):694-9.","DOI":"10.1021\/cn200088r"},{"key":"116","doi-asserted-by":"crossref","unstructured":"Taylor M, Moore S, Mourtas S, Niarakis A, Re F, Zona C, Ferla BL, Nicotra F, Masserini M, Antimisiaris SG, Gregori M, Allsop D. Effect of curcumin-associated and lipid ligand-functionalized nanoliposomes on aggregation of the Alzheimer's AB peptide. Nanomedicine. 2011;7(5):541-50.","DOI":"10.1016\/j.nano.2011.06.015"},{"key":"117","doi-asserted-by":"crossref","unstructured":"Liu K, Guo TL, Chojnacki J, Lee H-G, Wang X, Siedlak SL, Rao W, Zhu X, Zhang S. Bivalent ligand containing curcumin and cholesterol as a fluorescence probe for AB plaques in Alzheimer's disease. ACS Chem Neurosci. 2012;3(2):141-6.","DOI":"10.1021\/cn200122j"},{"key":"118","doi-asserted-by":"crossref","unstructured":"Mathew A, Fukuda T, Nagaoka Y, Hasumura T, Morimoto H, Yoshida Y, Maekawa T, Venugopal K, Kumar DS. Curcumin loaded-PLGA nanoparticles conjugated with Tet-1 peptide for potential use in Alzheimer's disease. PLoS One. 2012;7(3):e32616.","DOI":"10.1371\/journal.pone.0032616"},{"key":"119","doi-asserted-by":"crossref","unstructured":"Anand P, Kunnumakkara AB, Newman RA, Aggarwal BB. Bioavailability of curcumin: Problems and promises. Mol Pharm. 2007;4(6):807-18.","DOI":"10.1021\/mp700113r"},{"key":"120","doi-asserted-by":"crossref","unstructured":"Palmal S, Maity AR, Singh BK, Basu S, Jana NR, Jana NR. Inhibition of amyloid fibril growth and dissolution of amyloid fibrils by curcumin-gold nanoparticles. Chem Eur J. 2014;20(20):6184-91.","DOI":"10.1002\/chem.201400079"},{"key":"121","doi-asserted-by":"crossref","unstructured":"Pryor NE, Moss MA, Hestekin CN. Unraveling the early events of amyloid-B protein (AB) aggregation: Techniques for the determination of AB aggregate size. Int J Mol Sci. 2012;13(3):3038-72.","DOI":"10.3390\/ijms13033038"},{"key":"122","doi-asserted-by":"crossref","unstructured":"Krutyakov YA, Kudrinskiy AA, Olenin AY, Lisichkin GV. Synthesis and properties of silver nanoparticles: Advances and prospects. Russ Chem Rev. 2008;77(3):233-57.","DOI":"10.1070\/RC2008v077n03ABEH003751"},{"key":"123","doi-asserted-by":"crossref","unstructured":"Wang M, Kakinen A, Pilkington EH, Davis TP, Ke PC. Differential effects of silver and iron oxide nanoparticles on IAPP amyloid aggregation. Biomater Sci. 2017;5(3):485-93.","DOI":"10.1039\/C6BM00764C"},{"key":"124","doi-asserted-by":"crossref","unstructured":"Geitner NK, Bhattacharya P, Steele M, Chen R, Ladner DA, Ke PC. Understanding dendritic polymer-hydrocarbon interactions for oil dispersion. RSC Adv. 2012;2(25):9371-5.","DOI":"10.1039\/c2ra21602g"},{"key":"125","doi-asserted-by":"crossref","unstructured":"Gladytz A, Abel B, Risselada HJ. Gold-induced fibril growth: The mechanism of surface-facilitated amyloid aggregation. Angew Chem Int Ed. 2016;55(37):11242-6.","DOI":"10.1002\/anie.201605151"},{"key":"126","doi-asserted-by":"crossref","unstructured":"Antosova A, Bednarikova Z, Koneracka M, Antal I, Marek J, Kubovcikova M, Zavisova V, Jurikova A, Gazova Z. Amino acid functionalized superparamagnetic nanoparticles inhibit lysozyme amyloid fibrillization. Chem Eur J. 2019;25(31):7501-14.","DOI":"10.1002\/chem.201806262"},{"key":"127","doi-asserted-by":"crossref","unstructured":"Cai J, Dao P, Chen H, Yan L, Li YL, Zhang W, Li L, Du Z, Dong C-Z, Meunier B. Ultrasmall superparamagnetic iron oxide nanoparticles-bound NIR dyes: Novel theranostic agents for Alzheimer's disease. Dyes Pigm. 2020;173:107968.","DOI":"10.1016\/j.dyepig.2019.107968"},{"key":"128","doi-asserted-by":"crossref","unstructured":"Dao P, Ye F, Liu Y, Du ZY, Zhang K, Dong CZ, Meunier B, Chen H. Development of phenothiazine-based theranostic compounds that act both as inhibitors of B-amyloid aggregation and as imaging probes for amyloid plaques in Alzheimer's disease. ACS Chem Neurosci. 2017;8(4):798-806.","DOI":"10.1021\/acschemneuro.6b00380"},{"key":"129","doi-asserted-by":"crossref","unstructured":"Shukla R, Nune SK, Chanda N, Katti K, Mekapothula S, Kulkarni RR, Welshons WV, Kannan R, Katti KV. Soybeans as a phytochemical reservoir for the production and stabilization of biocompatible gold nanoparticles. Small. 2008;4(9):1425-36.","DOI":"10.1002\/smll.200800525"},{"key":"130","doi-asserted-by":"crossref","unstructured":"Costa JP, Ferreira PB, De Sousa DP, Jordan J, Freitas RM. Anticonvulsant effect of phytol in a pilocarpine model in mice. Neurosci Lett. 2012;523(2):115-8.","DOI":"10.1016\/j.neulet.2012.06.055"},{"key":"131","doi-asserted-by":"crossref","unstructured":"Chang H-J, Kim HJ, Chun HS. Quantitative structure-activity relationship (QSAR) for neuroprotective activity of terpenoids. Life Sci. 2007;80(9):835-41.","DOI":"10.1016\/j.lfs.2006.11.009"},{"key":"132","doi-asserted-by":"crossref","unstructured":"Sathya S, Manogari BG, Thamaraiselvi K, Vaidevi S, Ruckmani K, Devi KP. Phytol loaded PLGA nanoparticles ameliorate scopolamine-induced cognitive dysfunction by attenuating cholinesterase activity, oxidative stress and apoptosis in Wistar rat. Nutr Neurosci. 2020;25(3):485-501.","DOI":"10.1080\/1028415X.2020.1764290"},{"key":"133","doi-asserted-by":"crossref","unstructured":"Araya E, Olmedo I, Bastus NG, Guerrero S, Puntes VF, Giralt E, Kogan MJ. Gold nanoparticles and microwave irradiation inhibit beta-amyloid amyloidogenesis. Nanoscale Res Lett. 2008;3(11): 435-43.","DOI":"10.1007\/s11671-008-9178-5"},{"key":"134","doi-asserted-by":"crossref","unstructured":"Sahni JK, Doggui S, Ali J, Baboota S, Dao L, Ramassamy C. Neurotherapeutic applications of nanoparticles in Alzheimer's disease. J Control Release. 2011;152(2):208-31.","DOI":"10.1016\/j.jconrel.2010.11.033"},{"key":"135","doi-asserted-by":"crossref","unstructured":"Balasubramanian I, Hariharan S, Kumar MNVR. PLGA nanoparticles in drug delivery: The state of the art. Crit Rev Ther Drug Carrier Syst. 2004;21:387-422.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.v21.i5.20"},{"key":"136","doi-asserted-by":"crossref","unstructured":"Schwendeman S. Recent advances in the stabilization of proteins encapsulated in injectable PLGA delivery systems. Crit Rev Ther Drug Carrier Syst. 2002;19:73-98.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.v19.i1.20"},{"key":"137","doi-asserted-by":"crossref","unstructured":"Jain A, Jain SK. PEGylation: An approach for drug delivery. A review. Crit Rev Ther Drug Carrier Syst. 2008;25(5):403-47.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.v25.i5.10"},{"key":"138","doi-asserted-by":"crossref","unstructured":"Xiong N, Dong X-Y, Zheng J, Liu F-F, Sun Y. Design of LVFFARK and LVFFARK-functionalized nanoparticles for inhibiting amyloid B-protein fibrillation and cytotoxicity. ACS Appl Mater Interfaces. 2015;7(10):5650-62.","DOI":"10.1021\/acsami.5b00915"},{"key":"139","doi-asserted-by":"crossref","unstructured":"Shive MS, Anderson JM. Biodegradation and biocompatibility of PLA and PLGA microspheres. Adv Drug Deliv Rev. 1997;28(1):5-24.","DOI":"10.1016\/S0169-409X(97)00048-3"},{"key":"140","doi-asserted-by":"crossref","unstructured":"Baysal I, Ucar G, Gultekinoglu M, Ulubayram K, Yabanoglu-Ciftci S. Donepezil loaded PLGA-b-PEG nanoparticles: Their ability to induce destabilization of amyloid fibrils and to cross blood brain barrier in vitro. J Neural Transm. 2017;124(1):33-45.","DOI":"10.1007\/s00702-016-1527-4"},{"key":"141","doi-asserted-by":"crossref","unstructured":"Rogers SL, Friedhoff LT. Long-term efficacy and safety of donepezil in the treatment of Alzheimer's disease: An interim analysis of the results of a US multicentre open label extension study. Eur Neuropsychopharmacol. 1998;8(1):67-75.","DOI":"10.1016\/S0924-977X(97)00079-5"},{"key":"142","doi-asserted-by":"crossref","unstructured":"Herrmann N, Chau SA, Kircanski I, Lanct\u00f4t KL. Current and emerging drug treatment options for Alzheimer's disease. Drugs. 2012;71(15):2031-65.","DOI":"10.2165\/11595870-000000000-00000"},{"key":"143","doi-asserted-by":"crossref","unstructured":"Bala I, Hariharan S, Kumar MNVR. PLGA nanoparticles in drug delivery: The state of the art. Crit Rev Ther Drug Carrier Syst. 2004;21(5):387-422.","DOI":"10.1615\/CritRevTherDrugCarrierSyst.v21.i5.20"},{"key":"144","doi-asserted-by":"crossref","unstructured":"Badilescu S, Packirisamy M. Microfluidics-nano-integration for synthesis and sensing. Polymers. 2012;4(2):1278\u2013310. doi: 10.3390\/polym4021278.","DOI":"10.3390\/polym4021278"},{"key":"145","doi-asserted-by":"crossref","unstructured":"Baysal I, Yabanoglu-Ciftci S, Tunc-Sarisozen Y, Ulubayram K, Ucar G. Interaction of selegiline-loaded PLGA-b-PEG nanoparticles with beta-amyloid fibrils. J Neural Transm. 2013;120(6):903-10.","DOI":"10.1007\/s00702-013-0992-2"},{"key":"146","doi-asserted-by":"crossref","unstructured":"Liu JK, Teng Q, Garrity-Moses M, Federici T, Tanase D, Imperiale MJ, Boulis NM. A novel peptide defined through phage display for therapeutic protein and vector neuronal targeting. Neurobiol Dis. 2005;19(3):407-18.","DOI":"10.1016\/j.nbd.2005.01.022"},{"key":"147","doi-asserted-by":"crossref","unstructured":"Zhongju Y, Lin W, Yiliang L, Xiao L. Efficient modulation of beta-amyloid peptide fibrillation with polymer nanoparticles revealed by super-resolution optical microscopy. Anal Chem. 2019;91(13):8582-90.","DOI":"10.1021\/acs.analchem.9b01877"},{"key":"148","doi-asserted-by":"crossref","unstructured":"Shoval H, Lichtenberg D, Gazit E. The molecular mechanisms of the anti-amyloid effects of phenols. Amyloid. 2007;14(1):73-87.","DOI":"10.1080\/13506120601116674"},{"key":"149","doi-asserted-by":"crossref","unstructured":"Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA. (-)-epigallocatechin-3-gallate (EGCG) maintains k-casein in its pre-fibrillar state without redirecting its aggregation pathway. J Mol Biol. 2009;392(3):689-700.","DOI":"10.1016\/j.jmb.2009.07.031"},{"key":"150","doi-asserted-by":"crossref","unstructured":"Bertoncini CW, Fernandez CO, Griesinger C, Jovin TM, Zweckstetter M. Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation. J Biol Chem. 2005;280(35):30649-52.","DOI":"10.1074\/jbc.C500288200"},{"key":"151","doi-asserted-by":"crossref","unstructured":"Gregori M, Taylor M, Salvati E, Re F, Mancini S, Balducci C, Forloni G, Zambelli V, Sesana S, Michael M, Michail C, Tinker-Mill C, Kolosov O, Sherer M, Harris S, Fullwood NJ, Masserini M, Allsop D. Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer's AB peptide. Nanomedicine. 2017;13(2):723-32.","DOI":"10.1016\/j.nano.2016.10.006"},{"key":"152","doi-asserted-by":"crossref","unstructured":"Austen BM, Paleologou KE, Ali SAE, Qureshi MM, Allsop D, El-Agnaf OMA. Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's B-amyloid peptide. Biochemistry. 2008;47(7):1984-92.","DOI":"10.1021\/bi701415b"},{"key":"153","doi-asserted-by":"crossref","unstructured":"Parthsarathy V, McClean PL, H\u00f6lscher C, Taylor M, Tinker C, Jones G, Kolosov O, Salvati E, Gregori M, Masserini M, Allsop D. A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe\/PS1\u0394E9 mouse model of Alzheimer's disease. PLoS One. 2013;8(1):e54769.","DOI":"10.1371\/journal.pone.0054769"},{"key":"154","doi-asserted-by":"crossref","unstructured":"Taylor M, Moore S, Mayes J, Parkin E, Beeg M, Canovi M, Gobbi M, Mann DMA, Allsop D. Development of a proteolytically stable retro-inverso peptide inhibitor of B-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. Biochemistry. 2010;49(15):3261-72.","DOI":"10.1021\/bi100144m"},{"key":"155","doi-asserted-by":"crossref","unstructured":"Chafekar SM, Malda H, Merkx M, Meijer EW, Viertl D, Lashuel HA, Baas F, Scheper W. Branched KLVFF tetramers strongly potentiate inhibition of B-amyloid aggregation. Chembiochem. 2007;8(15):1857-64.","DOI":"10.1002\/cbic.200700338"},{"key":"156","doi-asserted-by":"crossref","unstructured":"Liu Y, Sun J, Gong Y, Zhou H, Chen X, Zhu X, Zhao Y, Wen Y, Qin X, Liu J. Peptide-modified mo polyoxometalate nanoparticles suppress Zn2+-induced A\u03b2 aggregation. ChemNanoMat. 2019;5(7): 897-910.","DOI":"10.1002\/cnma.201900057"},{"key":"157","doi-asserted-by":"crossref","unstructured":"Pithadia AS, Lim MH. Metal-associated amyloid-B species in Alzheimer's disease. Curr Opin Chem Biol. 2012;16(1):67-73.","DOI":"10.1016\/j.cbpa.2012.01.016"},{"key":"158","doi-asserted-by":"crossref","unstructured":"Cherny RA, Legg JT, McLean CA, Fairlie DP, Huang X, Atwood CS, Beyreuther K, Tanzi RE, Masters CL, Bush AI. Aqueous dissolution of Alzheimer's disease AB amyloid deposits by biometal depletion. J Biol Chem. 1999;274(33):23223-8.","DOI":"10.1074\/jbc.274.33.23223"},{"key":"159","doi-asserted-by":"crossref","unstructured":"Choi J-S, Braymer Joseph J, Nanga Ravi PR, Ramamoorthy A, Lim Mi H. Design of small molecules that target metal-AB species and regulate metal-induced A\u03b2 aggregation and neurotoxicity. Proc Natl Acad Sci U S A. 2010;107(51):21990-5.","DOI":"10.1073\/pnas.1006091107"},{"key":"160","doi-asserted-by":"crossref","unstructured":"House E, Collingwood J, Khan A, Korchazkina O, Berthon G, Exley C. Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of A\u03b242 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease. J Alzheimers Dis. 2004;6:291-301.","DOI":"10.3233\/JAD-2004-6310"},{"key":"161","doi-asserted-by":"crossref","unstructured":"Sears ME. Chelation: Harnessing and enhancing heavy metal detoxification-A review. Sci World J. 2013;2013:219840.","DOI":"10.1155\/2013\/219840"},{"key":"162","doi-asserted-by":"crossref","unstructured":"Cherny RA, Atwood CS, Xilinas ME, Gray DN, Jones WD, McLean CA, Barnham KJ, Volitakis I, Fraser FW, Kim Y-S, Huang X, Goldstein LE, Moir RD, Lim JT, Beyreuther K, Zheng H, Tanzi RE, Masters CL, Bush AI. Treatment with a copper-zinc chelator markedly and rapidly inhibits B-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 2001;30(3):665-76.","DOI":"10.1016\/S0896-6273(01)00317-8"},{"key":"163","doi-asserted-by":"crossref","unstructured":"Liu H, Dong X, Liu F, Zheng J, Sun Y. Iminodiacetic acid-conjugated nanoparticles as a bifunctional modulator against Zn2+-mediated amyloid B-protein aggregation and cytotoxicity. J Colloid Interface Sci. 2017;505:973-82.","DOI":"10.1016\/j.jcis.2017.06.093"},{"key":"164","doi-asserted-by":"crossref","unstructured":"Xie B, Li X, Dong X-Y, Sun Y. Insight into the inhibition effect of acidulated serum albumin on amyloid B-protein fibrillogenesis and cytotoxicity. Langmuir. 2014;30(32):9789-96.","DOI":"10.1021\/la5025197"},{"key":"165","doi-asserted-by":"crossref","unstructured":"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 B-peptide aggregation associated with Alzheimer's disease. Small. 2013;9(20):3455-61.","DOI":"10.1002\/smll.201202612"},{"key":"166","doi-asserted-by":"crossref","unstructured":"Yu H, Li M, Liu G, Geng J, Wang J, Ren J, Zhao C, Qu X. Metallosupramolecular complex targeting an a\/B discordant stretch of amyloid B peptide. Chem Sci. 2012;3(11):3145-53.","DOI":"10.1039\/c2sc20372c"},{"key":"167","doi-asserted-by":"crossref","unstructured":"Liu L, Xu K, Wang H, Jeremy Tan PK, Fan W, Venkatraman SS, Li L, Yang Y-Y. Self-assembled cationic peptide nanoparticles as an efficient antimicrobial agent. Nat Nanotechnol. 2009;4(7):457-63.","DOI":"10.1038\/nnano.2009.153"},{"key":"168","doi-asserted-by":"crossref","unstructured":"Gao N, Sun H, Dong K, Ren J, Qu X. Gold-nanoparticle-based multifunctional amyloid-B inhibitor against Alzheimer's disease. Chem Eur J. 2015;21(2):829-35.","DOI":"10.1002\/chem.201404562"},{"key":"169","doi-asserted-by":"crossref","unstructured":"Geng J, Li M, Ren J, Wang E, Qu X. Polyoxometalates as inhibitors of the aggregation of amyloid B peptides associated with Alzheimer's disease. Angew Chem Int Ed Engl. 2011;50(18):4184-8.","DOI":"10.1002\/anie.201007067"},{"key":"170","doi-asserted-by":"crossref","unstructured":"Soto C, Sigurdsson EM, Morelli L, Asok Kumar R, Castano EM, Frangione B. B-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat Med. 1998;4(7):822-6.","DOI":"10.1038\/nm0798-822"},{"key":"171","doi-asserted-by":"crossref","unstructured":"Li M, Xu C, Ren J, Wang E, Qu X. Photodegradation of B-sheet amyloid fibrils associated with Alzheimer's disease by using polyoxometalates as photocatalysts. Chem Commun. 2013;49(97):11394-6.","DOI":"10.1039\/c3cc46772d"},{"key":"172","doi-asserted-by":"crossref","unstructured":"Kepp KP. Bioinorganic chemistry of Alzheimer's disease. Chem Rev. 2012;112(10):5193-239.","DOI":"10.1021\/cr300009x"},{"key":"173","doi-asserted-by":"crossref","unstructured":"Wang X, Wang X, Guo Z. Metal-involved theranostics: An emerging strategy for fighting Alzheimer's disease. Coord Chem Rev. 2018;362:72-84.","DOI":"10.1016\/j.ccr.2018.03.010"},{"key":"174","doi-asserted-by":"crossref","unstructured":"Sen S, Konar S, Pathak A, Dasgupta S, DasGupta S. Effect of functionalized magnetic MnFe2O4 nanoparticles on fibrillation of human serum albumin. J Phys Chem B. 2014;118(40):11667-76.","DOI":"10.1021\/jp507902y"},{"key":"175","doi-asserted-by":"crossref","unstructured":"Bellova A, Bystrenova E, Koneracka M, Kopcansky P, Valle F, Tomasovicova N, Timko M, Bagelova J, Biscarini F, Gazova Z. Effect of Fe(3)O(4) magnetic nanoparticles on lysozyme amyloid aggregation. Nanotechnology. 2010;21(6):065103.","DOI":"10.1088\/0957-4484\/21\/6\/065103"},{"key":"176","doi-asserted-by":"crossref","unstructured":"Cabaleiro-Lago C, Lynch I, Dawson KA, Linse S. Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles. Langmuir. 2009;26(5):3453-61.","DOI":"10.1021\/la902980d"},{"key":"177","doi-asserted-by":"crossref","unstructured":"Wang J, Zhang Z, Zhang H, Li C, Chen M, Liu L, Dong M. Enhanced photoresponsive graphene oxide-modified g-C3N4 for disassembly of amyloid \u03b2 fibrils. ACS Appl Mater Interfaces. 2018;11(1):96-103.","DOI":"10.1021\/acsami.8b10343"},{"key":"178","doi-asserted-by":"crossref","unstructured":"Yan H, Yang H. TiO2\u2013g-C3N4 composite materials for photocatalytic H2 evolution under visible light irradiation. J Alloys Compd. 2011;509(4):L26-9.","DOI":"10.1016\/j.jallcom.2010.09.201"},{"key":"179","doi-asserted-by":"crossref","unstructured":"Susumu K, Oh E, Delehanty JB, Blanco-Canosa JB, Johnson BJ, Jain V, Hervey WJ, Algar WR, Boeneman K, Dawson PE, Medintz IL. Multifunctional compact zwitterionic ligands for preparing robust biocompatible semiconductor quantum dots and gold nanoparticles. J Am Chem Soc. 2011;133(24):9480-96.","DOI":"10.1021\/ja201919s"},{"key":"180","doi-asserted-by":"crossref","unstructured":"Nune SK, Chanda N, Shukla R, Katti K, Kulkarni RR, Thilakavathy S, Mekapothula S, Kannan R, Katti KV. Green nanotechnology from tea: Phytochemicals in tea as building blocks for production of biocompatible gold nanoparticles. J Mater Chem. 2009;19(19):2912-20.","DOI":"10.1039\/b822015h"},{"key":"181","doi-asserted-by":"crossref","unstructured":"Wang J, Feng Y, Tian X, Li C, Liu L. Disassembling and degradation of amyloid protein aggregates based on gold nanoparticle-modified g-C3N4. Colloids Surf B Biointerfaces. 2020;192:111051.","DOI":"10.1016\/j.colsurfb.2020.111051"},{"key":"182","doi-asserted-by":"crossref","unstructured":"Bleeke T, Zhang H, Madamanchi N, Patterson C, Faber JE. Catecholamine-induced vascular wall growth is dependent on generation of reactive oxygen species. Circ Res. 2004;94(1):37-45.","DOI":"10.1161\/01.RES.0000109412.80157.7D"},{"key":"183","doi-asserted-by":"crossref","unstructured":"Zhang J, Zhou X, Yu Q, Yang L, Sun D, Zhou Y, Liu J. Epigallocatechin-3-gallate (EGCG)-stabilized selenium nanoparticles coated with Tet-1 peptide to reduce amyloid-B aggregation and cytotoxicity. ACS Appl Mater Interfaces. 2014;6(11):8475-87.","DOI":"10.1021\/am501341u"},{"key":"184","doi-asserted-by":"crossref","unstructured":"Yang L, Chen Q, Liu Y, Zhang J, Sun D, Zhou Y, Liu J. Se\/Ru nanoparticles as inhibitors of metalinduced AB aggregation in Alzheimer's disease. J Mater Chem B. 2014;2(14):1977-87.","DOI":"10.1039\/C3TB21586E"},{"key":"185","doi-asserted-by":"crossref","unstructured":"Gazit V, Ben-Abraham R, Coleman R, Weizman A, Katz Y. Cysteine-induced hypoglycemic brain damage: An alternative mechanism to excitotoxicity. J Amino Acids. 2004;26(2):163-8.","DOI":"10.1007\/s00726-003-0045-5"},{"key":"186","doi-asserted-by":"crossref","unstructured":"Zhou X, Sun J, Yin T, Le F, Yang L, Liu Y, Liu J. Enantiomers of cysteine-modified SeNPs (d\/lSeNPs) as inhibitors of metal-induced AB aggregation in Alzheimer's disease. J Mater Chem B. 2015;3(39):7764-74.","DOI":"10.1039\/C5TB00731C"},{"key":"187","doi-asserted-by":"crossref","unstructured":"Singh A, Kumar A, Verma RK, Shukla R. Silymarin encapsulated nanoliquid crystals for improved activity against beta amyloid induced cytotoxicity. Int J Biol Macromol. 2020;149:1198-206.","DOI":"10.1016\/j.ijbiomac.2020.02.041"},{"key":"188","doi-asserted-by":"crossref","unstructured":"Yin F, Liu J, Ji X, Wang Y, Zidichouski J, Zhang J. Silibinin: A novel inhibitor of AB aggregation. Neurochem Int. 2011;58(3):399-403.","DOI":"10.1016\/j.neuint.2010.12.017"},{"key":"189","doi-asserted-by":"crossref","unstructured":"Sciacca MFM, Romanucci V, Zarrelli A, Monaco I, Lolicato F, Spinella N, Galati C, Grasso G, D'Urso L, Romeo M, Diomede L, Salmona M, Bongiorno C, Di Fabio G, La Rosa C, Milardi D. Inhibition of AB amyloid growth and toxicity by silybins: The crucial role of stereochemistry. ACS Chem Neurosci. 2017;8(8):1767-78.","DOI":"10.1021\/acschemneuro.7b00110"},{"key":"190","doi-asserted-by":"crossref","unstructured":"Lu P, Mamiya T, Lu LL, Mouri A, Zou LB, Nagai T, Hiramatsu M, Ikejima T, Nabeshima T. Silibinin prevents amyloid B peptide-induced memory impairment and oxidative stress in mice. Br J Pharmacol. 2009;157(7):1270-7.","DOI":"10.1111\/j.1476-5381.2009.00295.x"},{"key":"191","doi-asserted-by":"crossref","unstructured":"Urandur S, Banala VT, Shukla RP, Mittapelly N, Pandey G, Kalleti N, Mitra K, Rath SK, Trivedi R, Ramarao P, Mishra PR. Anisamide-anchored lyotropic nano-liquid crystalline particles with AIE effect: A smart optical beacon for tumor imaging and therapy. ACS Appl Mater Interfaces. 2018;10(15):12960-74.","DOI":"10.1021\/acsami.7b19109"},{"key":"192","doi-asserted-by":"crossref","unstructured":"Liu H, Yu L, Dong X, Sun Y. Synergistic effects of negatively charged hydrophobic nanoparticles and (-)-epigallocatechin-3-gallate on inhibiting amyloid B-protein aggregation. J Colloid Interface Sci. 2017;491:305-12.","DOI":"10.1016\/j.jcis.2016.12.038"}],"container-title":["Critical Reviews\u2122 in Therapeutic Drug Carrier Systems"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.dl.begellhouse.com\/download\/article\/7f5e04807354142a\/CRT-46209.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,30]],"date-time":"2023-10-30T07:04:16Z","timestamp":1698649456000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.dl.begellhouse.com\/journals\/3667c4ae6e8fd136,0d18644164e01f6f,7f5e04807354142a.html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"references-count":191,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2024]]}},"URL":"https:\/\/doi.org\/10.1615\/critrevtherdrugcarriersyst.2023046209","relation":{},"ISSN":["0743-4863"],"issn-type":[{"value":"0743-4863","type":"print"}],"subject":[],"published":{"date-parts":[[2024]]}}}