Abstract
Protein accumulation is a biological process in which mis-folded proteins aggregate and clump together either intra- or extracellularly. The lack of reliable sensors and the complex nature of these peptide aggregate make it challenging to detect them in the early stages of formation/growth. Rapid advances and ongoing research in the field of nanomaterials can provide practical solutions for the early monitoring and detection of amyloid aggregation. This chapter focuses on using quantum dot multimodal probes for amyloid detection. The fluorescent probes enable the in vitro monitoring of insulin, human islet amyloid polypeptide (hIAPP), and amyloid (Aβ−42) (Aβ42) oligomers and monomers during the fibrillogenesis dynamic. Moreover, research has shown that the quantum dot probe demonstrates 10 times greater signals when it comes to real-time detection of amyloid intermediates and fibrils compared to the traditionally used thioflavin dye. A negative ΔG° (standard free energy change for the reaction) value(−36.21 kJ/mol) for quantum dot probes indicates spontaneous interaction of the probe with the peptides. Thermodynamic measurements show that these interactions involve hydrogen bonding as well as hydrophobic (in an aqueous solution, nonpolar materials tend to accumulate and omit molecules of water) surface interactions. These probes monitor the in vitro fibrillation kinetics of various amyloid proteins having high specificity and sensitivity compared to thioflavin dye, as well as the existence of a 19F center (unique spectral signature in proteins). These properties make quantum dots effective probes for nonradiative and noninvasive in vivo detection of amyloid plaques.
Similar content being viewed by others
References
Abedini A, Schmidt AM (2013) Mechanisms of islet amyloidosis toxicity in type 2 diabetes. FEBS Lett 587:1119–1127. https://doi.org/10.1016/j.febslet.2013.01.017
Aguzzi A, O’Connor T (2010) Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat Rev Drug Discov 9:237–248. https://doi.org/10.1038/nrd3050
Albert MS, DeKosky ST, Dickson D, Dubois B, Feldman HH, Fox NC, Gamst A, Holtzman DM, Jagust WJ, Petersen RC, Snyder PJ, Carrillo MC, Thies B, Phelps CH (2011) The diagnosis of mild cognitive impairment due to Alzheimer’s disease: recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease. Alzheimers Dement 7:270–279. https://doi.org/10.1016/j.jalz.2011.03.008
Auer S, Trovato A, Vendruscolo M (2009) A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation. PLoS Comput Biol 5:1000458–1000464. https://doi.org/10.1371/journal.pcbi.1000458
Ben Hmidene A, Hanaki M, Murakami K, Irie K, Isoda H, Shigemori H (2017) Inhibitory activities of antioxidant flavonoids from Tamarix gallica on amyloid aggregation related to Alzheimer’s and type 2 diabetes diseases. Biol Pharm Bull 40:238–241. https://doi.org/10.1248/bpb.b16-00801
Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea JE, Ruotolo BT, Robinson CV, Bowers MT (2009) Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer’s disease. Nat Chem 1:326–331. https://doi.org/10.1038/nchem.247
Bhaskar S, Tian F, Stoeger T, Kreyling W, de la Fuente JM, Grazú V, Borm P, Estrada G, Ntziachristos V, Razansky D (2010) Multifunctional Nanocarriers for diagnostics, drug delivery and targeted treatment across blood-brain barrier: perspectives on tracking and neuroimaging. Part Fibre Toxicol 7:3–27. https://doi.org/10.1186/1743-8977-7-3
Cairns NJ, Bigio EH, Mackenzie IR, Neumann M, Lee VM, Hatanpaa KJ, White CL 3rd, Schneider JA, Grinberg LT, Halliday G, Duyckaerts C, Lowe JS, Holm IE, Tolnay M, Okamoto K, Yokoo H, Murayama S, Woulfe J, Munoz DG, Dickson DW, Ince PG, Trojanowski JQ, Mann DM (2007) Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the consortium for frontotemporal lobar degeneration. Acta Neuropathol 114:5–22. https://doi.org/10.1007/s00401-007-0237-2
Celej MS, Jares-Erijman EA, Jovin TM (2008) Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein. Biophys J 94:4867–4879. https://doi.org/10.1529/biophysj.107.125211
Chatterjee S, Mudher A (2018) Alzheimer’s disease and type 2 diabetes: a critical assessment of the shared pathological traits. Front Neurosci 12:383. https://doi.org/10.3389/fnins.2018.00383
Courtney SM, Ungerleider LG, Keil K, Haxby JV (1997) Transient and sustained activity in a distributed neural system for human working memory. Nature 386:608–611. https://doi.org/10.1038/386608a0
Craft S (2005) Insulin resistance syndrome and Alzheimer’s disease: age- and obesity-related effects on memory, amyloid, and inflammation. Neurobiol Aging 26(Suppl 1):65–69. https://doi.org/10.1016/j.neurobiolaging.2005.08.021
Despa F, Decarli C (2013) Amylin: what might be its role in Alzheimer’s disease and how could this affect therapy? Expert Rev Proteomics 10:403–405. https://doi.org/10.1586/14789450.2013.841549
Eisenberg D, Jucker M (2012) The amyloid state of proteins in human diseases. Cell 148:1188–1203. https://doi.org/10.1016/j.cell.2012.02.022
Gilbert BJ (2014) The role of amyloid β in the pathogenesis of Alzheimer’s disease. Postgrad Med J 90:113–117. https://doi.org/10.1136/postgradmedj-2013-201515rep
Hawe A, Sutter M, Jiskoot W (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25:1487–1499. https://doi.org/10.1007/s11095-007-9516-9
Heneka MT, O’Banion MK (2007) Inflammatory processes in Alzheimer’s disease. J Neuroimmunol 184:69–91. https://doi.org/10.1016/j.jneuroim.2006.11.017
Hirosumi J, Tuncman G, Chang L, Görgün CZ, Uysal KT, Maeda K, Karin M, Hotamisligil GS (2002) A central role for JNK in obesity and insulin resistance. Nature 420:333–336. https://doi.org/10.1038/nature01137
Hötzer B, Medintz IL, Hildebrandt N (2012) Fluorescence in nanobiotechnology: sophisticated fluorophores for novel applications. Small 8:2297–2326. https://doi.org/10.1002/smll.201200109
Hu B, Dai F, Fan Z, Ma G, Tang Q, Zhang X (2015) Nanotheranostics: Congo red/Rutin-MNPs with enhanced magnetic resonance imaging and H2O2-responsive therapy of Alzheimer’s disease in APPswe/PS1dE9 transgenic mice. Adv Mater 27:5499–5505. https://doi.org/10.1002/adma.201502227
Husby G, Marhaug G, Sletten K (1982) Amyloid a in systemic amyloidosis associated with cancer. Cancer Res 42:1600–1603
Ittner LM, Gotz J (2011) Amyloid-beta and tau – a toxic pas de deux in Alzheimer’s disease. Nat Rev Neurosci 12:65–72. https://doi.org/10.1038/nrn2967
Jack L Jr, Boseman L, Vinicor F (2004) Aging Americans and diabetes. A public health and clinical response. Geriatrics 59:14–17
Jayaraman A, Pike CJ (2014) Alzheimer’s disease and type 2 diabetes: multiple mechanisms contribute to interactions. Curr Diab Rep 14:476. https://doi.org/10.1007/s11892-014-0476-2
Kahn SE, D’Alessio DA, Schwartz MW, Fujimoto WY, Ensinck JW, Taborsky GJ Jr, Porte D Jr (1990) Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells. Diabetes 39:634–638. https://doi.org/10.2337/diab.39.5.634
Kidachi E, Kurisu M, Hanaki M, Miyamae Y, Irie K, Murakami K (2016) Structure-activity relationship of phenylethanoid glycosides on the inhibition of amyloid β aggregation. Heterocycles 92:1976–1982. https://doi.org/10.3987/COM-16-13533
Kim JE, Lee M (2003) Fullerene inhibits beta-amyloid peptide aggregation. Biochem Biophys Res Commun 303:576–579. https://doi.org/10.1016/s0006-291x(03)00393-0
Kim H, Haluzik M, Gavrilova O, Yakar S, Portas J, Sun H, Pajvani UB, Scherer PE, LeRoith D (2004) Thiazolidinediones improve insulin sensitivity in adipose tissue and reduce the hyperlipidaemia without affecting the hyperglycaemia in a transgenic model of type 2 diabetes. Diabetologia 47:2215–2225. https://doi.org/10.1007/s00125-004-1581-6
Klajnert B, Cortijo-Arellano M, Bryszewska M, Cladera J (2006) Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer’s and prion diseases. Biochem Biophys Res Commun 339:577–582. https://doi.org/10.1016/j.bbrc.2005.11.053
Kodali R, Wetzel R (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 17:48–57. https://doi.org/10.1016/j.sbi.2007.01.007
Kurochkin IV, Goto S (1994) Alzheimer’s beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett 345:33–37. https://doi.org/10.1016/0014-5793(94)00387-4
Kyle KA, Bayed KD (1975) Amyloidosis: review OP 236 cases. Medicine 54:271–299. https://doi.org/10.1097/00005792-197507000-00001
Leuzy A, Heurling K, Ashton NJ, Schöll M, Zimmer ER (2018) In vivo detection of Alzheimer’s disease. Yale J Biol Med 91:291–300
Lin H, Bhatia R, Lal R (2001) Amyloid beta protein forms ion channels: implications for Alzheimer’s disease pathophysiology. FASEB J 15:2433–2444. https://doi.org/10.1096/fj.01-0377com
Lindgren M, Hammarström P (2010) Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states. FEBS J 277:1380–1388. https://doi.org/10.1111/j.1742-4658.2010.07571.x
Linse S (2019) Mechanism of amyloid protein aggregation and the role of inhibitors. Pure Appl Chem 91:211–229. https://doi.org/10.1515/pac-2018-1017
Linse S, Cabaleiro-Lago C, Xue WF, Lynch I, Lindman S, Thulin E, Radford SE, Dawson KA (2007) Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci U S A 104:8691–8696. https://doi.org/10.1073/pnas.0701250104
Liu Y, An S, Li J, Kuang Y, He X, Guo Y, Ma H, Zhang Y, Ji B, Jiang C (2016) Brain-targeted co-delivery of therapeutic gene and peptide by multifunctional nanoparticles in Alzheimer’s disease mice. Biomaterials 80:33–45. https://doi.org/10.1016/j.biomaterials.2015.11.060
Luca S, Yau WM, Leapman R, Tycko R (2007) Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46:13505–13522. https://doi.org/10.1021/bi701427q
Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K (1985) Amyloid plaque core protein in Alzheimer disease and down syndrome. Proc Natl Acad Sci U S A 82:4245–4249. https://doi.org/10.1073/pnas.82.12.4245
Milanski M, Degasperi G, Coope A, Morari J, Denis R, Cintra DE, Tsukumo DM, Anhe G, Amaral ME, Takahashi HK, Curi R, Oliveira HC, Carvalheira JB, Bordin S, Saad MJ, Velloso LA (2009) Saturated fatty acids produce an inflammatory response predominantly through the activation of TLR4 signaling in hypothalamus: implications for the pathogenesis of obesity. J Neurosci 29:359–370. https://doi.org/10.1523/jneurosci.2760-08.2009
Miller Y, Ma B, Nussinov R (2010) Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape. Chem Rev 110:4820–4838. https://doi.org/10.1021/cr900377t
Moraes L, Vasconcelos-dos-Santos A, Santana FC, Godoy MA, Rosado-de-Castro PH, Jasmin, Azevedo-Pereira RL, Cintra WM, Gasparetto EL, Santiago MF, Mendez-Otero R (2012) Neuroprotective effects and magnetic resonance imaging of mesenchymal stem cells labeled with SPION in a rat model of Huntington’s disease. Stem Cell Res 9:143–155. https://doi.org/10.1016/j.scr.2012.05.005
Mourtas S, Canovi M, Zona C, Aurilia D, Niarakis A, La Ferla B, Salmona M, Nicotra F, Gobbi M, Antimisiaris SG (2011) Curcumin-decorated nanoliposomes with very high affinity for amyloid-β1-42 peptide. Biomaterials 32:1635–1645. https://doi.org/10.1016/j.biomaterials.2010.10.027
Mudshinge SR, Deore AB, Patil S, Bhalgat CM (2011) Nanoparticles: emerging carriers for drug delivery. Saudi Pharm J 19:129–141. https://doi.org/10.1016/j.jsps.2011.04.001
Nguyen HD, Hall CK (2004) Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc Natl Acad Sci U S A 101:16180–16185. https://doi.org/10.1073/pnas.0407273101
Paradise J, Diliberto GM, Tisdale AW, Kokkoli E (2008) Exploring emerging nanobiotechnology drugs and medical devices. Food Drug Law J 63:407–420
Pardridge WM (2012) Drug transport across the blood-brain barrier. J Cereb Blood Flow Metab 32:1959–1972. https://doi.org/10.1038/jcbfm.2012.126
Patra JK, Das G, Fraceto LF, Campos EVR, Rodriguez-Torres MDP, Acosta-Torres LS, Diaz-Torres LA, Grillo R, Swamy MK, Sharma S, Habtemariam S, Shin H-S (2018) Nano based drug delivery systems: recent developments and future prospects. J Nanobiotechnol 16:71–104. https://doi.org/10.1186/s12951-018-0392-8
Pickut BA, Dierckx RA, Dobbeleir A, Audenaert K, Van Laere K, Vervaet A, De Deyn PP (1999) Validation of the cerebellum as a reference region for SPECT quantification in patients suffering from dementia of the Alzheimer type. Psychiatry Res 90:103–112. https://doi.org/10.1016/s0925-4927(99)00004-9
Prades R, Guerrero S, Araya E, Molina C, Salas E, Zurita E, Selva J, Egea G, López-Iglesias C, Teixidó M, Kogan MJ, Giralt E (2012) Delivery of gold nanoparticles to the brain by conjugation with a peptide that recognizes the transferrin receptor. Biomaterials 33:7194–7205. https://doi.org/10.1016/j.biomaterials.2012.06.063
Pradhan N, Jana D, Ghorai BK, Jana NR (2015) Detection and monitoring of amyloid fibrillation using a fluorescence “switch-on” probe. ACS Appl Mater Interfaces 7:25813–25820. https://doi.org/10.1021/acsami.5b07751
Querfurth HW, LaFerla FM (2010) Alzheimer’s disease. N Engl J Med 362:329–344. https://doi.org/10.1056/NEJMra0909142
Saiki M, Honda S, Kawasaki K, Zhou D, Kaito A, Konakahara T, Morii H (2005) Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. J Mol Biol 348:983–998. https://doi.org/10.1016/j.jmb.2005.03.022
Sebastião I, Candeias E, Santos MS, de Oliveira CR, Moreira PI, Duarte AI (2014) Insulin as a bridge between type 2 diabetes and Alzheimer disease – how anti-diabetics could be a solution for dementia. Front Endocrinol (Lausanne) 5:110. https://doi.org/10.3389/fendo.2014.00110
Selkoe DJ, Hardy J (2016) The amyloid hypothesis of Alzheimer’s disease at 25 years. EMBO Mol Med 8:595–608. https://doi.org/10.15252/emmm.201606210
Skaat H, Sorci M, Belfort G, Margel S (2009) Effect of maghemite nanoparticles on insulin amyloid fibril formation: selective labeling, kinetics, and fibril removal by a magnetic field. J Biomed Mater Res A 91:342–351. https://doi.org/10.1002/jbm.a.32232
Spranger J, Kroke A, Möhlig M, Hoffmann K, Bergmann MM, Ristow M, Boeing H, Pfeiffer AF (2003) Inflammatory cytokines and the risk to develop type 2 diabetes: results of the prospective population-based European Prospective Investigation into Cancer and Nutrition (EPIC)-Potsdam Study. Diabetes 52:812–817. https://doi.org/10.2337/diabetes.52.3.812
Stein LJ, Dorsa DM, Baskin DG, Figlewicz DP, Porte D Jr, Woods SC (1987) Reduced effect of experimental peripheral hyperinsulinemia to elevate cerebrospinal fluid insulin concentrations of obese Zucker rats. Endocrinology 121:1611–1615. https://doi.org/10.1210/endo-121-5-1611
Su F, Shu H, Ye Q, Wang Z, Xie C, Yuan B, Zhang Z, Bai F (2017) Brain insulin resistance deteriorates cognition by altering the topological features of brain networks. Neuroimage Clin 13:280–287. https://doi.org/10.1016/j.nicl.2016.12.009
Symmers WS (1956) Primary amyloidosis: a review. J Clin Pathol 9:187–211. https://doi.org/10.1136/jcp.9.3.187
Tiwari V, Solanki V, Tiwari M (2015) In-vivo and in-vitro techniques used to investigate Alzheimer’s disease. Front Life Sci 8:332–347. https://doi.org/10.1080/21553769.2015.1044129
Toyama BH, Weissman JS (2011) Amyloid structure: conformational diversity and consequences. Annu Rev Biochem 80:557–585. https://doi.org/10.1146/annurev-biochem-090908-120656
Turnell WG, Finch JT (1992) Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J Mol Biol 227:1205–1223. https://doi.org/10.1016/0022-2836(92)90532-o
Walker JM, Harrison FE (2015) Shared neuropathological characteristics of obesity, type 2 diabetes and Alzheimer’s disease: impacts on cognitive decline. Nutrients 7:7332–7357. https://doi.org/10.3390/nu7095341
Wang ST, Lin Y, Hsu CC, Amdursky N, Spicer CD, Stevens MM (2017) Probing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore. Talanta 173:44–50. https://doi.org/10.1016/j.talanta.2017.05.015
Webb EA, Hesseling AC, Schaaf HS, Gie RP, Lombard CJ, Spitaels A, Delport S, Marais BJ, Donald K, Hindmarsh P, Beyers N (2009) High prevalence of Mycobacterium tuberculosis infection and disease in children and adolescents with type 1 diabetes mellitus. Int J Tuberc Lung Dis 13(7):868–874
Westermark P, Wernstedt C, Wilander E, Hayden DW, O’Brien TD, Johnson KH (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci U S A 84:3881–3885. https://doi.org/10.1073/pnas.84.11.3881
Wynne K, Stanley S, McGowan B, Bloom S (2005) Appetite control. J Endocrinol 184:291–318. https://doi.org/10.1677/joe.1.05866
Xiao L, Zhao D, Chan WH, Choi MM, Li HW (2010) Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-L-cysteine capped quantum dots. Biomaterials 31:91–98. https://doi.org/10.1016/j.biomaterials.2009.09.014
Xu C, Webb WW (1996) Measurement of two-photon excitation cross sections of molecular fluorophores with data from 690 to 1050 nm. J Opt Soc Am B 13:481–491. https://doi.org/10.1364/JOSAB.13.000481
Yang T, Yang L, Zhang C, Wang Y, Ma X, Wang K, Luo J, Yao C, Wang X, Wang X (2016) A copper–amyloid-β targeted fluorescent chelator as a potential theranostic agent for Alzheimer’s disease. Inorg Chem Front 3:1572–1581. https://doi.org/10.1039/c6qi00268d
Yazaki M, Higuchi K (2014) Senile systemic amyloidosis. Brain Nerve 66:817–826
Yiannopoulou KG, Papageorgiou SG (2013) Current and future treatments for Alzheimer’s disease. Ther Adv Neurol Disord 6:19–33. https://doi.org/10.1177/1756285612461679
Yousaf M, Ahmad M, Bhatti IA, Nasir A, Hasan M, Jian X, Kalantar-Zadeh K, Mahmood N (2019) In vivo and in vitro monitoring of amyloid aggregation via BSA@FGQDs multimodal probe. ACS Sens 4:200–210. https://doi.org/10.1021/acssensors.8b01216
Zhang Y, Song W (2017) Islet amyloid polypeptide: another key molecule in Alzheimer’s pathogenesis? Prog Neurobiol 153:100–120. https://doi.org/10.1016/j.pneurobio.2017.03.001
Zhang D, Neumann O, Wang H, Yuwono VM, Barhoumi A, Perham M, Hartgerink JD, Wittung-Stafshede P, Halas NJ (2009) Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH. Nano Lett 9:666–671. https://doi.org/10.1021/nl803054h
Zhang M, Mao X, Yu Y, Wang CX, Yang YL, Wang C (2013) Nanomaterials for reducing amyloid cytotoxicity. Adv Mater 25:3780–3801. https://doi.org/10.1002/adma.201301210
Zhou Y, Peng Z, Seven ES, Leblanc RM (2018) Crossing the blood-brain barrier with nanoparticles. J Control Release 270:290–303. https://doi.org/10.1016/j.jconrel.2017.12.015
Ziegler SI (2005) Positron emission tomography: principles, technology, and recent developments. Nucl Phys A 752:679–687. https://doi.org/10.1016/j.nuclphysa.2005.02.067
Acknowledgments
The authors would like to acknowledge the Vice-Chancellor fellowship scheme at RMIT University and the School of Engineering for financial support and RMIT University for the RMIT Research Stipend Scholarship (RRSS).
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2023 Springer Nature Switzerland AG
About this entry
Cite this entry
Jeyachandran, T., Loomba, S., Khalid, A., Mahmood, N. (2023). Multifunctional Nanoprobes for the Surveillance of Amyloid Aggregation. In: Shanker, U., Hussain, C.M., Rani, M. (eds) Handbook of Green and Sustainable Nanotechnology. Springer, Cham. https://doi.org/10.1007/978-3-030-69023-6_105-1
Download citation
DOI: https://doi.org/10.1007/978-3-030-69023-6_105-1
Received:
Accepted:
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-69023-6
Online ISBN: 978-3-030-69023-6
eBook Packages: Springer Reference Chemistry and Mat. ScienceReference Module Physical and Materials ScienceReference Module Chemistry, Materials and Physics