Recent Developments of Hybrid Fluorescence Techniques: Advances in Amyloid Detection Methods

Lee, C.C.; Nayak, A.; Sethuraman, A.; Belfort, G.; McRae, G.J. A three-stage kinetic model of amyloid fibrillation. Biophys. J., 2007, 92(10), 3448-3458.
[http://dx.doi.org/10.1529/biophysj.106.098608] [PMID: 17325005]

Siddiqi, M.K.; Alam, P.; Chaturvedi, S.K.; Shahein, Y.E.; Khan, R.H. Mechanisms of protein aggregation and inhibition. Front. Biosci., 2017, 9(1), 1-20.
[PMID: 27814585]

Sulatsky, M.I.; Stepanenko, O.V.; Stepanenko, O.V.; Mikhailova, E.V.; Kuznetsova, I.M.; Turoverov, K.K.; Sulatskaya, A.I. Amyloid fibrils degradation: the pathway to recovery or aggravation of the disease? Front. Mol. Biosci., 2023, 10, 1208059.
[http://dx.doi.org/10.3389/fmolb.2023.1208059] [PMID: 37377863]

Makin, O.S.; Atkins, E.; Sikorski, P.; Johansson, J.; Serpell, L.C. Molecular basis for amyloid fibril formation and stability. Proc. Natl. Acad. Sci. USA, 2005, 102(2), 315-320.
[http://dx.doi.org/10.1073/pnas.0406847102] [PMID: 15630094]

Rambaran, R.N.; Serpell, L.C. Amyloid fibrils. Prion, 2008, 2(3), 112-117.
[http://dx.doi.org/10.4161/pri.2.3.7488] [PMID: 19158505]

Lee, J.C. Diagnosis of Alzheimer’s disease utilizing amyloid and tau as fluid biomarker. Exp. Mol. Med., 2019, 51, 1-10.
[http://dx.doi.org/10.1038/s12276-019-0299-y]

Castiglione, V.; Franzini, M.; Aimo, A.; Carecci, A.; Lombardi, C.M.; Passino, C.; Rapezzi, C.; Emdin, M.; Vergaro, G. Use of biomarkers to diagnose and manage cardiac amyloidosis. Eur. J. Heart Fail., 2021, 23(2), 217-230.
[http://dx.doi.org/10.1002/ejhf.2113] [PMID: 33527656]

Zheng, X.; Xu, Z.; Li, H.; Fu, H. A sensitive probe for amyloid fibril detection with strong fluorescence and early response. RSC Advances, 2018, 8(29), 15870-15875.
[http://dx.doi.org/10.1039/C8RA00751A] [PMID: 35542196]

Cliff, I. Stains and Indraneel Ghosh, When conjugated polymers meet amyloid fibrils. ASC Chem. Biol., 2007, 2(8), 525-528.

Ma, S.; Chen, G.; Xu, J.; Liu, Y.; Li, G.; Chen, T.; Li, Y.; James, T.D. Current strategies for the development of fluorescence-based molecular probes for visualizing the enzymes and proteins associated with Alzheimer’s disease. Coord. Chem. Rev., 2021, 427(213553), 213553.
[http://dx.doi.org/10.1016/j.ccr.2020.213553]

Ren, W.; Li, L.; Zhang, J.; Vaas, M.; Klohs, J.; Ripoll, J.; Wolf, M.; Ni, R.; Rudin, M. Non-invasive visualization of amyloid-beta deposits in Alzheimer amyloidosis mice using magnetic resonance imaging and fluorescence molecular tomography. Biomed. Opt. Express, 2022, 13(7), 3809-3822.
[http://dx.doi.org/10.1364/BOE.458290] [PMID: 35991935]

Zhou, J. Fluorescent diagnostic probes in neurodegenerative disease. Adv. Mater., 2020, 2001945, 1-43.

Schouw, HM Targeted optical fluorescence imaging: a meta-narrative review and future perspectives. Eur. J. Nucl. Med. Mol. Imaging., 2021, 48(13), 4272-4292.

Das, A.; Dutta, T.; Gadhe, L.; Koner, A.L.; Saraogi, I. Biocompatible fluorescent probe for the selective detection of amyloid fibrils. Anal. Chem., 2020, 92(15), 10336-10341.
[http://dx.doi.org/10.1021/acs.analchem.0c00379] [PMID: 32635722]

Diaz-Garcia , M.E.; Laino, R.B. Fluorescence Overview. Encyclo. Analyt. Sci., 2019, 3(3), 309-319.

dos Santos Rodrigues, F.H. Applications of fluorescence spectroscopy in protein conformational changes and intermolecular contacts. BBA Advances, 2023, 3, 1-13.

Bose, Aswathy Fluorescence spectroscopy and its applications: A Review. Int. J. Adv. Pharm. Anal., 2018, 8(1), 1-8.

Sharma, B.K. Instrumental methods of chemical analysis, 25^th ed; Krishna Prakashan Media: Meerut, India, 2005.

Kakkar, Saloni Progress in fluorescence biosensing and food safety towards point-of-detection (PoD) system. Biosensors., 2023, 13(2), 249.

Jung, H.S.; Verwilst, P.; Kim, W.Y.; Kim, J.S. Fluorescent and colorimetric sensors for the detection of humidity or water content. Chem. Soc. Rev., 2016, 45(5), 1242-1256.
[http://dx.doi.org/10.1039/C5CS00494B] [PMID: 26766615]

Zhang, X.; Hu, Y.; Yang, X.; Tang, Y.; Han, S.; Kang, A.; Deng, H.; Chi, Y.; Zhu, D.; Lu, Y. Förster resonance energy transfer (FRET)-based biosensors for biological applications. Biosens. Bioelectron., 2019, 138, 111314.
[http://dx.doi.org/10.1016/j.bios.2019.05.019]

Challa, P.K.; Peter, Q.; Wright, M.A.; Zhang, Y.; Saar, K.L.; Carozza, J.A.; Benesch, J.L.P.; Knowles, T.P.J. Real-Time Intrinsic fluorescence visualization and sizing of proteins and protein complexes in microfluidic devices. Anal. Chem., 2018, 90(6), 3849-3855.
[http://dx.doi.org/10.1021/acs.analchem.7b04523] [PMID: 29451779]

Bekard, I.B.; Dunstan, D.E. Tyrosine autofluorescence as a measure of bovine insulin fibrillation. Biophys. J., 2009, 97(9), 2521-2531.
[http://dx.doi.org/10.1016/j.bpj.2009.07.064] [PMID: 19883595]

Zhuang, X.; Ha, T.; Kim, H.D.; Centner, T.; Labeit, S.; Chu, S. Fluorescence quenching: A tool for single-molecule protein-folding study. Proc. Natl. Acad. Sci. USA, 2000, 97(26), 14241-14244.
[http://dx.doi.org/10.1073/pnas.97.26.14241] [PMID: 11121030]

Lakowicz, J.R. Principles of Fluorescence Spectroscopy; Springer: New York, NY, 2006.

Marcelo, H. Gehlen, The centenary of the Stern-Volmer equation of fluorescence quenching: From the single line plot to the SV quenching map. J. Photochem. Photobiol. Photochem. Rev., 2020, 42, 1-14.

Kang, J.; Lemaire, H.G.; Unterbeck, A.; Salbaum, J.M.; Masters, C.L.; Grzeschik,, K.H.; Multhaup, G.; Beyreuther, K.; Hill, B.M The precursor of Alzheimer’s disease amyloid A4 protein resembles a cell-surface receptor. Nature., 1987, 325(6106), 733-736.

Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Böddrich, A.; Purfürst, B.; Benilova, I.; Korsak, M.; Gallo, G.; Rizzo, D.; Gonnelli, L.; Fragai, M.; De Strooper, B.; Wanker, E.E.; Luchinat, C. Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils. Chem. Commun. (Camb.), 2020, 56(62), 8830-8833.
[http://dx.doi.org/10.1039/D0CC02463E] [PMID: 32749391]

Greenberg, B.D.; Bencen, G.H.; Seilhamer, J.J.; Lewicki, J.A.; Fiddes, J.C. Nucleotide sequence of the gene encoding human atrial natriuretic factor precursor. Nature, 1984, 312(5995), 656-658.
[http://dx.doi.org/10.1038/312656a0] [PMID: 6095119]

Gibbs, R.A.; Weinstock, G.M.; Metzker, M.L.; Muzny, D.M.; Sodergren, E.J.; Scherer, S.; Scott, G.; Steffen, D.; Worley, K.C.; Burch, P.E.; Okwuonu, G.; Hines, S.; Lewis, L.; DeRamo, C.; Delgado, O.; Dugan-Rocha, S.; Miner, G.; Morgan, M.; Hawes, A.; Gill, R.; Holt, C.R.A.; Adams, M.D.; Amanatides, P.G.; Baden-Tillson, H.; Barnstead, M.; Chin, S.; Evans, C.A.; Ferriera, S.; Fosler, C.; Glodek, A.; Gu, Z.; Jennings, D.; Kraft, C.L.; Nguyen, T.; Pfannkoch, C.M.; Sitter, C.; Sutton, G.G.; Venter, J.C.; Woodage, T.; Smith, D.; Lee, H-M.; Gustafson, E.; Cahill, P.; Kana, A.; Doucette-Stamm, L.; Weinstock, K.; Fechtel, K.; Weiss, R.B.; Dunn, D.M.; Green, E.D.; Blakesley, R.W.; Bouffard, G.G.; de Jong, P.J.; Osoegawa, K.; Zhu, B.; Marra, M.; Schein, J.; Bosdet, I.; Fjell, C.; Jones, S.; Krzywinski, M.; Mathewson, C.; Siddiqui, A.; Wye, N.; McPherson, J.; Zhao, S.; Fraser, C.M.; Shetty, J.; Shatsman, S.; Geer, K.; Chen, Y.; Abramzon, S.; Nierman, W.C.; Gibbs, R.A.; Weinstock, G.M.; Havlak, P.H.; Chen, R.; James Durbin, K.; Simons, R.; Ren, Y.; Song, X-Z.; Li, B.; Liu, Y.; Qin, X.; Cawley, S.; Weinstock, G.M.; Worley, K.C.; Cooney, A.J.; Gibbs, R.A.; D’Souza, L.M.; Martin, K.; Qian Wu, J.; Gonzalez-Garay, M.L.; Jackson, A.R.; Kalafus, K.J.; McLeod, M.P.; Milosavljevic, A.; Virk, D.; Volkov, A.; Wheeler, D.A.; Zhang, Z.; Bailey, J.A.; Eichler, E.E.; Tuzun, E.; Birney, E.; Mongin, E.; Ureta-Vidal, A.; Woodwark, C.; Zdobnov, E.; Bork, P.; Suyama, M.; Torrents, D.; Alexandersson, M.; Trask, B.J.; Young, J.M.; Smith, D.; Huang, H.; Fechtel, K.; Wang, H.; Xing, H.; Weinstock, K.; Daniels, S.; Gietzen, D.; Schmidt, J.; Stevens, K.; Vitt, U.; Wingrove, J.; Camara, F.; Mar Albà, M.; Abril, J.F.; Guigo, R.; Smit, A.; Dubchak, I.; Rubin, E.M.; Couronne, O.; Poliakov, A.; Hübner, N.; Ganten, D.; Goesele, C.; Hummel, O.; Kreitler, T.; Lee, Y-A.; Monti, J.; Schulz, H.; Zimdahl, H.; Himmelbauer, H.; Lehrach, H.; Jacob, H.J.; Bromberg, S.; Gullings-Handley, J.; Jensen-Seaman, M.I.; Kwitek, A.E.; Lazar, J.; Pasko, D.; Tonellato, P.J.; Twigger, S.; Ponting, C.P.; Duarte, J.M.; Rice, S.; Goodstadt, L.; Beatson, S.A.; Emes, R.D.; Winter, E.E.; Webber, C.; Brandt, P.; Nyakatura, G.; Adetobi, M.; Chiaromonte, F.; Elnitski, L.; Eswara, P.; Hardison, R.C.; Hou, M.; Kolbe, D.; Makova, K.; Miller, W.; Nekrutenko, A.; Riemer, C.; Schwartz, S.; Taylor, J.; Yang, S.; Zhang, Y.; Lindpaintner, K.; Andrews, T.D.; Caccamo, M.; Clamp, M.; Clarke, L.; Curwen, V.; Durbin, R.; Eyras, E.; Searle, S.M.; Cooper, G.M.; Batzoglou, S.; Brudno, M.; Sidow, A.; Stone, E.A.; Craig Venter, J.; Payseur, B.A.; Bourque, G.; López-Otín, C.; Puente, X.S.; Chakrabarti, K.; Chatterji, S.; Dewey, C.; Pachter, L.; Bray, N.; Yap, V.B.; Caspi, A.; Tesler, G.; Pevzner, P.A.; Haussler, D.; Roskin, K.M.; Baertsch, R.; Clawson, H.; Furey, T.S.; Hinrichs, A.S.; Karolchik, D.; Kent, W.J.; Rosenbloom, K.R.; Trumbower, H.; Weirauch, M.; Cooper, D.N.; Stenson, P.D.; Ma, B.; Brent, M.; Arumugam, M.; Shteynberg, D.; Copley, R.R.; Taylor, M.S.; Riethman, H.; Mudunuri, U.; Peterson, J.; Guyer, M.; Felsenfeld, A.; Old, S.; Mockrin, S.; Collins, F. Genome sequence of the Brown Norway rat yields insights into mammalian evolution. Nature, 2004, 428(6982), 493-521.
[http://dx.doi.org/10.1038/nature02426] [PMID: 15057822]

Strausberg, R.L.; Feingold, E.A.; Grouse, L.H.; Derge, J.G.; Klausner, R.D.; Collins, F.S.; Wagner, L.; Shenmen, C.M.; Schuler, G.D.; Altschul, S.F.; Zeeberg, B.; Buetow, K.H.; Schaefer, C.F.; Bhat, N.K.; Hopkins, R.F.; Jordan, H.; Moore, T.; Max, S.I.; Wang, J.; Hsieh, F.; Diatchenko, L.; Marusina, K.; Farmer, A.A.; Rubin, G.M.; Hong, L.; Stapleton, M.; Soares, M.B.; Bonaldo, M.F.; Casavant, T.L.; Scheetz, T.E.; Brownstein, M.J.; Usdin, T.B.; Toshiyuki, S.; Carninci, P.; Prange, C.; Raha, S.S.; Loquellano, N.A.; Peters, G.J.; Abramson, R.D.; Mullahy, S.J.; Bosak, S.A.; McEwan, P.J.; McKernan, K.J.; Malek, J.A.; Gunaratne, P.H.; Richards, S.; Worley, K.C.; Hale, S.; Garcia, A.M.; Gay, L.J.; Hulyk, S.W.; Villalon, D.K.; Muzny, D.M.; Sodergren, E.J.; Lu, X.; Gibbs, R.A.; Fahey, J.; Helton, E.; Ketteman, M.; Madan, A.; Rodrigues, S.; Sanchez, A.; Whiting, M.; Madan, A.; Young, A.C.; Shevchenko, Y.; Bouffard, G.G.; Blakesley, R.W.; Touchman, J.W.; Green, E.D.; Dickson, M.C.; Rodriguez, A.C.; Grimwood, J.; Schmutz, J.; Myers, R.M.; Butterfield, Y.S.; Krzywinski, M.I.; Skalska, U.; Smailus, D.E.; Schnerch, A.; Schein, J.E.; Jones, S.J.; Marra, M.A. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. USA, 2002, 99(26), 16899-16903.
[http://dx.doi.org/10.1073/pnas.242603899] [PMID: 12477932]

Otelea, M.R. Prion protein gene (PRNP) polymorphism at the codon 185 in Braila County local sheep breed in Romania. Rom. Biotechnol. Lett., 2011, 16(4), 6419-6429.

Solomon, A.; Weiss, D.T.; Murphy, C. Primary amyloidosis associated with a novel heavy-chain fragment (AH amyloidosis). Am. J. Hematol., 1994, 45(2), 171-176.
[http://dx.doi.org/10.1002/ajh.2830450214] [PMID: 8141123]

Castoano, E.M.; Prelli, F.; Pras, M. J. Biol. Chem., 1995, 270(29), 17610-17615.
[http://dx.doi.org/10.1074/jbc.270.29.17610] [PMID: 7615568]

Mita, S.; Maeda, S.; Shimada, K.; Araki, S. Cloning and sequence analysis of cDNA for human prealbumin. Biochem. Biophys. Res. Commun., 1984, 124(2), 558-564.
[http://dx.doi.org/10.1016/0006-291X(84)91590-0] [PMID: 6093805]

Gustavsson, A.; Jahr, H.; Tobiassen, R.; Jacobson, D.R.; Sletten, K.; Westermark, P. Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis. Lab. Invest., 1995, 73(5), 703-708.
[PMID: 7474944]

Güssow, D.; Rein, R.; Ginjaar, I.; Hochstenbach, F.; Seemann, G.; Kottman, A.; Ploegh, H.L. The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit. J. Immunol., 1987, 139(9), 3132-3138.
[http://dx.doi.org/10.4049/jimmunol.139.9.3132] [PMID: 3312414]

Bellotti, V.; Stoppini, M.; Mangione, P.; Sunde, M.; Robinson, C.; Asti, L.; Brancaccio, D.; Ferri, G. β 2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem., 1998, 258(1), 61-67.
[http://dx.doi.org/10.1046/j.1432-1327.1998.2580061.x] [PMID: 9851692]

Matsumoto, T.; Nakamura, A.M.; Takahashi, K.G. Cloning of cDNAs and hybridization analysis of lysozymes from two oyster species, Crassostrea gigas and Ostrea edulis. Comp. Biochem. Physiol. B Biochem. Mol. Biol., 2006, 145(3-4), 325-330.
[http://dx.doi.org/10.1016/j.cbpb.2006.08.003]

Pepys, M.B.; Hawkins, P.N.; Booth, D.R.; Vigushin, D.M.; Tennent, G.A.; Soutar, A.K.; Totty, N.; Nguyen, O.; Blake, C.C.F.; Terry, C.J.; Feest, T.G.; Zalin, A.M.; Hsuan, J.J. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature, 1993, 362(6420), 553-557.
[http://dx.doi.org/10.1038/362553a0] [PMID: 8464497]

Nishi, M.; Chan, S.J.; Nagamatsu, S.; Bell, G.I.; Steiner, D.F. Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone. Proc. Natl. Acad. Sci. USA, 1989, 86(15), 5738-5742.
[http://dx.doi.org/10.1073/pnas.86.15.5738] [PMID: 2668946]

Christmanson, L.; Rorsman, F.; Stenman, G.; Westermark, P.; Betsholtz, C. The human islet amyloid polypeptide (IAPP) gene. FEBS Lett., 1990, 267(1), 160-166.
[http://dx.doi.org/10.1016/0014-5793(90)80314-9] [PMID: 2365085]

Ghisaidoobe, A.; Chung, S. Intrinsic tryptophan fluorescence in the detection and analysis of proteins: A focus on Förster resonance energy transfer techniques. Int. J. Mol. Sci., 2014, 15(12), 22518-22538.
[http://dx.doi.org/10.3390/ijms151222518] [PMID: 25490136]

Toprakcioglu, Z.; Challa, P.; Xu, C.; Knowles, T.P.J. Label-free analysis of protein aggregation and phase behavior. ACS Nano, 2019, 13(12), 13940-13948.
[http://dx.doi.org/10.1021/acsnano.9b05552] [PMID: 31738513]

Chakraborty, H.; Chattopadhyay, A. Sensing tryptophan microenvironment of amyloid protein utilizing wavelength-selective fluorescence approach. J. Fluoresc., 2017, 27(6), 1995-2000.
[http://dx.doi.org/10.1007/s10895-017-2138-7] [PMID: 28687983]

Aran Terol, P.; Kumita, J.R.; Hook, S.C.; Dobson, C.M.; Esbjörner, E.K. Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide. Biochem. Biophys. Res. Commun., 2015, 468(4), 696-701.
[http://dx.doi.org/10.1016/j.bbrc.2015.11.018] [PMID: 26551456]

Fiona, T.S. Structure-specific intrinsic fluorescence of protein amyloids used to study their kinetics of aggregation. Bio-nanoimaging; Academic Press, 2014.

Tikhonova, T.N.; Rovnyagina, N.R.; Zherebker, A.Y.; Sluchanko, N.N.; Rubekina, A.A.; Orekhov, A.S.; Nikolaev, E.N.; Fadeev, V.V.; Uversky, V.N.; Shirshin, E.A. Dissection of the deep-blue autofluorescence changes accompanying amyloid fibrillation. Arch. Biochem. Biophys., 2018, 651, 13-20.
[http://dx.doi.org/10.1016/j.abb.2018.05.019] [PMID: 29803394]

Sirangelo, I.; Borriello, M.; Irace, G.; Iannuzzi, C. Intrinsic blue-green fluorescence in amyloyd fibrils. AIMS Biophys., 2018, 5(2), 155-165.
[http://dx.doi.org/10.3934/biophy.2018.2.155]

Pinotsi, D.; Buell, A.K.; Dobson, C.M.; Kaminski, G.S. label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence. Chem. Bio. Chem., 2013, 14, 846-850.

Del Mercato, L.L.; Pompa, P.P.; Maruccio, G.; Torre, A.D.; Sabella, S.; Tamburro, A.M.; Cingolani, R.; Rinaldi, R. Charge transport and intrinsic fluorescence in amyloid-like fibrils. Proc. Natl. Acad. Sci. USA, 2007, 104(46), 18019-18024.
[http://dx.doi.org/10.1073/pnas.0702843104] [PMID: 17984067]

Groenning, M. Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status. J. Chem. Biol., 2010, 3(1), 1-18.
[http://dx.doi.org/10.1007/s12154-009-0027-5] [PMID: 19693614]

Apter, B. Fluorescence phenomena in amyloid and amyloidogenic bionanostructures. Crystals, 2020, 10(8), 668.
[http://dx.doi.org/10.3390/cryst10080668]

Sulatskaya, A.I.; Maskevich, A.A.; Kuznetsova, I.M.; Uversky, V.N.; Turoverov, K.K. Fluorescence quantum yield of thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils. PLoS One, 2010, 5(10), e15385.
[http://dx.doi.org/10.1371/journal.pone.0015385] [PMID: 21048945]

Biancalana, M.; Koide, S. Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim. Biophys. Acta. Proteins Proteomics, 2010, 1804(7), 1405-1412.
[http://dx.doi.org/10.1016/j.bbapap.2010.04.001] [PMID: 20399286]

Volkova, K.D.; Kovalska, V.B.; Balanda, A.O.; Vermeij, R.J.; Subramaniam, V.; Slominskii, Y.L.; Yarmoluk, S.M. Cyanine dye–protein interactions: Looking for fluorescent probes for amyloid structures. J. Biochem. Biophys. Methods, 2007, 70(5), 727-733.
[http://dx.doi.org/10.1016/j.jbbm.2007.03.008] [PMID: 17467807]

Needham, L.M.; Weber, J.; Varela, J.A.; Fyfe, J.W.B.; Do, D.T.; Xu, C.K.; Tutton, L.; Cliffe, R.; Keenlyside, B.; Klenerman, D.; Dobson, C.M.; Hunter, C.A.; Müller, K.H.; O’Holleran, K.; Bohndiek, S.E.; Snaddon, T.N.; Lee, S.F. ThX – a next-generation probe for the early detection of amyloid aggregates. Chem. Sci. (Camb.), 2020, 11(18), 4578-4583.
[http://dx.doi.org/10.1039/C9SC04730A] [PMID: 34122915]

Sulatsky, M.I.; Sulatskaya, A.I.; Povarova, O.I.; Antifeeva, I.A.; Kuznetsova, I.M.; Turoverov, K.K. Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils. Prion, 2020, 14(1), 67-75.
[http://dx.doi.org/10.1080/19336896.2020.1720487] [PMID: 32008441]

Wolfe, L.S.; Calabrese, M.F.; Nath, A.; Blaho, D.V.; Miranker, A.D.; Xiong, Y. Protein-induced photophysical changes to the amyloid indicator dye thioflavin T. Proc. Natl. Acad. Sci. USA, 2010, 107(39), 16863-16868.
[http://dx.doi.org/10.1073/pnas.1002867107] [PMID: 20826442]

Klunk, W.E.; Wang, Y.; Huang, G.; Debnath, M.L.; Holt, D.P.; Mathis, C.A. Uncharged thioflavin-T derivatives bind to amyloid-β protein with high affinity and readily enter the brain. Life Sci., 2001, 69(13), 1471-1484.
[http://dx.doi.org/10.1016/S0024-3205(01)01232-2] [PMID: 11554609]

Buxbaum, J.N.; Linke, R.P. A molecular history of the amyloidoses. J. Mol. Biol., 2012, 421(2-3), 142-159.
[http://dx.doi.org/10.1016/j.jmb.2012.01.024] [PMID: 22321796]

Sunde, M.; Blake, C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem., 1997, 50, 123-159.
[http://dx.doi.org/10.1016/S0065-3233(08)60320-4] [PMID: 9338080]

Yang, Y.; Cui, M. Radiolabeled bioactive benzoheterocycles for imaging β-amyloid plaques in Alzheimer’s disease. Eur. J. Med. Chem., 2014, 87, 703-721.
[http://dx.doi.org/10.1016/j.ejmech.2014.10.012] [PMID: 25305715]

Gade Malmos, K.; Blancas-Mejia, L.M.; Weber, B.; Buchner, J.; Ramirez-Alvarado, M.; Naiki, H.; Otzen, D. ThT 101: A primer on the use of thioflavin T to investigate amyloid formation. Amyloid, 2017, 24(1), 1-16.
[http://dx.doi.org/10.1080/13506129.2017.1304905] [PMID: 28393556]

Sulatskaya, A.I.; Sulatsky, M.I.; Antifeeva, I.A.; Kuznetsova, I.M.; Turoverov, K.K. Structural analogue of Thioflavin T, DMASEBT, as a tool for amyloid study. Anal. Chem., 2019, 91(4), 3131-3140.
[http://dx.doi.org/10.1021/acs.analchem.8b05737] [PMID: 30673267]

Lavysh, A.V.; Sulatskaya, A.I.; Lugovskii, A.A.; Voropay, E.S.; Kuznetsova, I.M.; Turoverov, K.K.; Maskevich, A.A. Photophysical properties of Trans-2-[4-(dimethylamino)styryl]-3-ethyl-1,3-benzothiazolium perchlorate, a new structural analog of Thioflavin T. J. Appl. Spectrosc., 2014, 81(2), 205-213.
[http://dx.doi.org/10.1007/s10812-014-9911-z]

Klunk Imaging amyloid in AD with PIB. Ann. Neurol., 2004, 55(3), 1-14.
[PMID: 14991808]

Watanabe, H.; Ono, M.; Ariyoshi, T.; Katayanagi, R.; Saji, H. Novel benzothiazole derivatives as fluorescent probes for detection of β-amyloid and ὰ-synuclein aggregates. ACS Chem. Neurosci., 2017, 8(8), 1656-1662.
[http://dx.doi.org/10.1021/acschemneuro.6b00450] [PMID: 28467708]

Freire, S.; De Araujo, M.H.; Al-Soufi, W.; Novo, M. Photophysical study of Thioflavin T as fluorescence marker of amyloid fibrils. Dyes Pigments, 2014, 110, 97-105.
[http://dx.doi.org/10.1016/j.dyepig.2014.05.004]

Mathis, C.A.; Wang, Y.; Holt, D.P.; Huang, G.F.; Debnath, M.L.; Klunk, W.E. Synthesis and evaluation of 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents. J. Med. Chem., 2003, 46(13), 2740-2754.
[http://dx.doi.org/10.1021/jm030026b] [PMID: 12801237]

Qin, L. Julian Vastl and Jianmin Gao, Hightly sensitive amyloid detection enabled by thioflavin T dimers. Mol. Biosyst., 2010, 6, 1791-1795.
[http://dx.doi.org/10.1039/c005255h] [PMID: 20614050]

Ono, M.; Hayashi, S.; Kimura, H.; Kawashima, H.; Nakayama, M.; Saji, H. Push–pull benzothiazole derivatives as probes for detecting β-amyloid plaques in Alzheimer’s brains. Bioorg. Med. Chem., 2009, 17(19), 7002-7007.
[http://dx.doi.org/10.1016/j.bmc.2009.08.032] [PMID: 19740669]

Kovalska, V.; Chernii, S.; Losytskyy, M.; Tretyakova, I.; Dovbii, Y.; Gorski, A.; Chernii, V.; Czerwieniec, R.; Yarmoluk, S. Design of functionalized β-ketoenole derivatives as efficient fluorescent dyes for detection of amyloid fibrils. New J. Chem., 2018, 42(16), 13308-13318.
[http://dx.doi.org/10.1039/C8NJ01020J]

Si, G.; Zhou, S.; Xu, G.; Wang, J.; Wu, B.; Zhou, S. A curcumin-based NIR fluorescence probe for detection of amyloid-beta (Aβ) plaques in Alzheimer’s disease. Dyes Pigments, 2019, 163, 509-515.
[http://dx.doi.org/10.1016/j.dyepig.2018.12.003]

Marzano, N.R.; Wray, K.M.; Johnston, C.L.; Paudel, B.P.; Hong, Y.; van Oijen, A.; Ecroyd, H. An ὰ-Cyanostilbene derivative for the enhanced detection and imaging of amyloid fibril aggregates. ACS Chem. Neurosci., 2020, 11(24), 4191-4202.
[http://dx.doi.org/10.1021/acschemneuro.0c00478] [PMID: 33226775]

Shrishti, P. Basic Orange 21: A molecular rotor probe for fluorescence turn-on sensing of amyloid fibrils. J. Mol. Liq., 2020, 303(112618), 1-11.

Teoh, C.L.; Su, D.; Sahu, S.; Yun, S.W.; Drummond, E.; Prelli, F.; Lim, S.; Cho, S.; Ham, S.; Wisniewski, T.; Chang, Y.T. A chemical fluorescent probe for the detection of Aβ oligomers. J. Am. Chem. Soc., 2015, 137(42), 13503-13509.
[http://dx.doi.org/10.1021/jacs.5b06190] [PMID: 26218347]

Cao, K.J.; Kim, J.H.; Kroeger, H.; Gaffney, P.M.; Lin, J.H.; Sigurdson, C.J.; Yang, J. ARCAM-1 facilitates fluorescence detection of amyloid-containing deposits in the retina. Transl. Vis. Sci. Technol., 2021, 10(7), 5.
[http://dx.doi.org/10.1167/tvst.10.7.5] [PMID: 34096989]

Pradhan, N.; Jana, D.; Ghorai, B.K.; Jana, N.R. Detection and monitoring of amyloid fibrillation using a fluorescence “Switch-On” Probe. ACS Appl. Mater. Interfaces, 2015, 7(46), 25813-25820.
[http://dx.doi.org/10.1021/acsami.5b07751] [PMID: 26540091]

Li, L.; Luo, W.C.; Jiang, M.; Yu, X.; Xu, L. Turn-on fluorescence probing of amyloid fibrils by the proto-berberine alkaloids and the study of their interactions. Int. J. Biol. Macromol., 2023, 231, 123319.
[http://dx.doi.org/10.1016/j.ijbiomac.2023.123319] [PMID: 36682666]

Carlos, W.B Small molecules fluorescent probes for the detection of amyloid self-assembly in vitro and in vivo. Curr. Protein Pept. Sci., 2011, 11, 206-220.

Oyarzún, M.P.; Tapia-Arellano, A.; Cabrera, P.; Jara-Guajardo, P.; Kogan, M.J. Plasmonic nanoparticles as optical sensing probes for the detection of Alzheimer’s disease. Sensors (Basel), 2021, 21(6), 2067.
[http://dx.doi.org/10.3390/s21062067] [PMID: 33809416]

Sun, L.; Liu, D.; Fu, D.; Yue, T.; Scharre, D.; Zhang, L. Fluorescent peptide nanoparticles to detect amyloid-beta aggregation in cerebrospinal fluid and serum for Alzheimer’s disease diagnosis and progression monitoring. Chem. Eng. J., 2021, 405, 126733.
[http://dx.doi.org/10.1016/j.cej.2020.126733]

Xu, S.C.S.; LoRicco, J.G.; Bishop, A.C.; James, N.A.; Huynh, W.H.; McCallum, S.A.; Roan, N.R.; Makhatadze, G.I. Sequence-independent recognition of the amyloid structural motif by GFP protein family. Proc. Natl. Acad. Sci. USA, 2020, 117(36), 22122-22127.
[http://dx.doi.org/10.1073/pnas.2001457117] [PMID: 32839332]

Usui, K.; Mie, M.; Andou, T.; Mihara, H.; Kobatake, E. Fluorescent and luminescent fusion proteins for analyses of amyloid beta peptide aggregation. J. Pept. Sci., 2017, 23(7-8), 659-665.
[http://dx.doi.org/10.1002/psc.3003] [PMID: 28378376]

Takahashi, T.; Mihara, H. FRET detection of amyloid β-peptide oligomerization using a fluorescent protein probe presenting a pseudo-amyloid structure. Chem. Commun. (Camb.), 2012, 48(10), 1568-1570.
[http://dx.doi.org/10.1039/C1CC14552E] [PMID: 21909572]

Morfin, J.F.; Lacerda, S.; Geraldes, C.F.G.C.; Tóth, É. Metal complexes for the visualisation of amyloid peptides. Sensors & Diagnostics, 2022, 1(4), 627-647.
[http://dx.doi.org/10.1039/D2SD00026A]

Chia, Y.Y.; Tay, M.G. An insight into fluorescent transition metal complexes. Dalton Trans., 2014, 43(35), 13159-13168.
[http://dx.doi.org/10.1039/C4DT01098A] [PMID: 25032996]

Hayne, D.J.; Lim, S.; Donnelly, P.S. Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer’s disease. Chem. Soc. Rev., 2014, 43(19), 6701-6715.
[http://dx.doi.org/10.1039/C4CS00026A] [PMID: 24671229]

Yu, H.; Zhao, W.; Xie, M.; Li, X.; Sun, M.; He, J.; Wang, L.; Yu, L. Real-time monitoring of self-aggregation of β-amyloid by a fluorescent probe based on Ruthenium complex. Anal. Chem., 2020, 92(4), 2953-2960.
[http://dx.doi.org/10.1021/acs.analchem.9b03566] [PMID: 31941275]

Herland, A.; Nilsson, K.P.R.; Olsson, J.D.M.; Hammarström, P.; Konradsson, P.; Inganäs, O. Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH. J. Am. Chem. Soc., 2005, 127(7), 2317-2323.
[http://dx.doi.org/10.1021/ja045835e] [PMID: 15713111]

Herrmann, U.S.; Schütz, A.K.; Shirani, H.; Huang , D.; Saban, D.; Nuvolone, M.; Li, B.; Ballmer, B.; Åslund, A.K.; Mason, J.J.; Rushing, E.; Budka, H.; Nyström, S.; Hammarström, P.; Böckmann, A.; Caflisch, A.; Meier, B.H.; Nilsson, K.P.; Hornemann, S.; Aguzzi., A. Structure-based drug design identifies polythiophenes as antiprion compounds. Sci. Translat. Med., 2015, 299, ra123.

Kieninger, B.; Gioeva, Z.; Krüger, S.; Westermark, G.T.; Friedrich, R.P.; FÄndrich, M.; Röcken, C. PTAA and B10: new approaches to amyloid detection in tissue—evaluation of amyloid detection in tissue with a conjugated polyelectrolyte and a fibril-specific antibody fragment. Amyloid, 2011, 18(2), 47-52.
[http://dx.doi.org/10.3109/13506129.2011.560623] [PMID: 21401323]

Åslund, A.; Sigurdson, C.J.; Klingstedt, T.; Grathwohl, S.; Bolmont, T.; Dickstein, D.L.; Glimsdal, E.; Prokop, S.; Lindgren, M.; Konradsson, P.; Holtzman, D.M.; Hof, P.R.; Heppner, F.L.; Gandy, S.; Jucker, M.; Aguzzi, A.; Hammarström, P.; Nilsson, K.P.R. Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. ACS Chem. Biol., 2009, 4(8), 673-684.
[http://dx.doi.org/10.1021/cb900112v] [PMID: 19624097]

Nilsson, K.P.R. Conjugated polyelectrolytes- Conformation-sensitive optical probes for staining and characterization of amyloid deposits. Chembiochem., 2006, 797, 1096-1104.

Hawe, A.; Sutter, M.; Jiskoot, W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res., 2008, 25(7), 1487-1499.
[http://dx.doi.org/10.1007/s11095-007-9516-9] [PMID: 18172579]

Galbán, J.; Andreu, Y.; Sierra, J.F.; De Marcos, S.; Castillo, J.R. Intrinsic fluorescence of enzymes and fluorescence of chemically modified enzymes for analytical purposes: A review. Luminescence, 2001, 16(2), 199-210.
[http://dx.doi.org/10.1002/bio.633] [PMID: 11312548]

Hellmann, N.; Schneider, D. Hands on: Using tryptophan fluorescence spectroscopy to study protein structure. Methods Mol. Biol., 2019, 1958, 379-401.
[http://dx.doi.org/10.1007/978-1-4939-9161-7_20] [PMID: 30945230]

Ruiz-Arias, Á.; Jurado, R.; Fueyo-González, F.; Herranz, R.; Gálvez, N.; González-Vera, J.A.; Orte, A. A FRET pair for quantitative and superresolution imaging of amyloid fibril formation. Sens. Actuators. B. Chem., 2022, 350, 130882.
[http://dx.doi.org/10.1016/j.snb.2021.130882]

Espinar-Barranco, L.; Paredes, J.M.; Orte, A.; Crovetto, L.; Garcia-Fernandez, E. A solvatofluorochromic dye as a fluorescent lifetime-based probe of β-amyloid aggregation. Dyes Pigments, 2022, 202, 110274.
[http://dx.doi.org/10.1016/j.dyepig.2022.110274]

Zhou, Y.; Hua, J.; Ding, D.; Tang, Y. Interrogating amyloid aggregation with aggregation-induced emission fluorescence probes. Biomaterials, 2022, 286, 121605.
[http://dx.doi.org/10.1016/j.biomaterials.2022.121605] [PMID: 35653878]

Alexander, P.D. Photobleaching of organic fluorophores: quantitative characterization, mechanisms, protection. Methods Appl. Fluoresc., 2020, 8, 1-26.

Wan, J.; Zhang, X.; Zhang, K.; Su, Z. Biological nanoscale fluorescent probes: From structure and performance to bioimaging. Rev. Anal. Chem., 2020, 39(1), 209-221.
[http://dx.doi.org/10.1515/revac-2020-0119]

Smith, A.M.; Mancini, M.C.; Nie, S. Second window for in vivo imaging. Nat. Nanotechnol., 2009, 4(11), 710-711.
[http://dx.doi.org/10.1038/nnano.2009.326] [PMID: 19898521]

Yang, Y.; Yu, Y.; Chen, H.; Meng, X.; Ma, W.; Yu, M.; Li, Z.; Li, C.; Liu, H.; Zhang, X.; Xiao, H.; Yu, Z. Illuminating platinum transportation while maximizing therapeutic efficacy by gold nanoclusters via simultaneous near-infrared-I/II imaging and glutathione scavenging. ACS Nano, 2020, 14(10), 13536-13547.
[http://dx.doi.org/10.1021/acsnano.0c05541] [PMID: 32924505]

Tokuraku, K.; Marquardt, M.; Ikezu, T. Real-time imaging and quantification of amyloid-β peptide aggregates by novel quantum-dot nanoprobes. PLoS One, 2009, 4(12), e8492.
[http://dx.doi.org/10.1371/journal.pone.0008492] [PMID: 20041162]

Barbalinardo, M.; Antosova, A.; Gambucci, M.; Bednarikova, Z.; Albonetti, C.; Valle, F.; Sassi, P.; Latterini, L.; Gazova, Z.; Bystrenova, E. Effect of metallic nanoparticles on amyloid fibrils and their influence to neural cell toxicity. Nano Res., 2020, 13(4), 1081-1089.
[http://dx.doi.org/10.1007/s12274-020-2748-2]

Zhao, J.; Xu, N.; Yang, X.; Ling, G.; Zhang, P. The roles of gold nanoparticles in the detection of amyloid-β peptide for Alzheimer’s disease. Colloid Interface Sci. Commun., 2022, 46, 100579.
[http://dx.doi.org/10.1016/j.colcom.2021.100579]

Chakraborty, A.; Mohapatra, S.S.; Barik, S.; Roy, I.; Gupta, B.; Biswas, A. Impact of nanoparticles on amyloid β-induced Alzheimer’s disease, tuberculosis, leprosy and cancer: A systematic review. Biosci. Rep., 2023, 43(2), BSR20220324.
[http://dx.doi.org/10.1042/BSR20220324] [PMID: 36630532]

Tsay, J.M.; Michalet, X. New light on quantum dot cytotoxicity. Chem. Biol., 2005, 12(11), 1159-1161.
[http://dx.doi.org/10.1016/j.chembiol.2005.11.002] [PMID: 16298294]

Crivat, G.; Taraska, J.W. Imaging proteins inside cells with fluorescent tags. Trends Biotechnol., 2012, 30(1), 8-16.
[http://dx.doi.org/10.1016/j.tibtech.2011.08.002] [PMID: 21924508]

Prajapati, K.P.; Ansari, M.; Yadav, D.K.; Mittal, S.; Anand, B.G.; Kar, K. A robust yet simple method to generate fluorescent amyloid nanofibers. J. Mater. Chem. B., 2023, 11(36), 8765-8774.
[http://dx.doi.org/10.1039/D3TB01203D] [PMID: 37661927]

Xu, R.; Wu, Q.; Xing, C.; Wang, H.; Xu, W.; Meng, X.; Hou, H. A novel water-stable luminescent metal complex exhibiting high sensitive and selective detection to Fe³⁺ and Al³⁺. Polyhedron, 2021, 197(197), 115056.
[http://dx.doi.org/10.1016/j.poly.2021.115056]

Nilsson, K.P.R.; Ikenberg, K.; Åslund, A.; Fransson, S.; Konradsson, P.; Röcken, C.; Moch, H.; Aguzzi, A. Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy. Am. J. Pathol., 2010, 176(2), 563-574.
[http://dx.doi.org/10.2353/ajpath.2010.080797] [PMID: 20035056]

Thomas, S.W., III; Joly, G.D.; Swager, T.M. Chemical sensors based on amplifying fluorescent conjugated polymers. Chem. Rev., 2007, 107(4), 1339-1386.
[http://dx.doi.org/10.1021/cr0501339] [PMID: 17385926]

Sigurdson, C.J.; Nilsson, K.P.R.; Hornemann, S.; Manco, G.; Polymenidou, M.; Schwarz, P.; Leclerc, M.; Hammarström, P.; Wüthrich, K.; Aguzzi, A. Prion strain discrimination using luminescent conjugated polymers. Nat. Methods, 2007, 4(12), 1023-1030.
[http://dx.doi.org/10.1038/nmeth1131] [PMID: 18026110]

Jara-Guajardo, P.; Cabrera, P.; Celis, F.; Soler, M.; Berlanga, I.; Parra-Muñoz, N.; Acosta, G.; Albericio, F.; Guzman, F.; Campos, M.; Alvarez, A.; Morales-Zavala, F.; Kogan, M.J. Gold nanoparticles mediate improved detection of β-amyloid aggregates by fluorescence. Nanomaterials (Basel), 2020, 10(4), 690.
[http://dx.doi.org/10.3390/nano10040690] [PMID: 32268543]

Molecular rotors: fluorescent sensors for microviscosity and conformation of biomolecules. Angew. Chem. Int. Ed., 2024, 63(6), 1-711.

Gence, L. Conjugated polymer and hybrid polymer metal single nanowires: Correlated characterization and device integration. Nanowires Science and Technology; Intechopen, 2010.

Xia, N.; Zhou, B.; Huang, N.; Jiang, M.; Zhang, J.; Liu, L. Visual and fluorescent assays for selective detection of beta-amyloid oligomers based on the inner filter effect of gold nanoparticles on the fluorescence of CdTe quantum dots. Biosens. Bioelectron., 2016, 85, 625-632.
[http://dx.doi.org/10.1016/j.bios.2016.05.066] [PMID: 27240009]

Gorbenko, G.; Trusova, V.; Deligeorgiev, T.; Gadjev, N.; Mizuguchi, C.; Saito, H. Two-step FRET as a tool for probing the amyloid state of proteins. J. Mol. Liq., 2019, 294(111675), 111675.
[http://dx.doi.org/10.1016/j.molliq.2019.111675]

Nair, R.V.; Padmanabhan, P.; Gulyás, B.; Matham, M.V. Fluorescence Resonance Energy Transfer (FRET)-Based ThT free sensing of Beta-Amyloid fibrillation by Carbon dot-Ag composites. Plasmonics, 2021, 16(3), 863-872.
[http://dx.doi.org/10.1007/s11468-020-01338-w]

Hamd-Ghadareh, S.; Salimi, A.; Parsa, S.; Mowla, S.J. Development of three-dimensional semi-solid hydrogel matrices for ratiometric fluorescence sensing of Amyloid β peptide and imaging in SH-SY5 cells: Improvement of point of care diagnosis of Alzheimer’s disease biomarker. Biosens. Bioelectron., 2022, 199(113895), 113895.
[http://dx.doi.org/10.1016/j.bios.2021.113895] [PMID: 34968953]

Birch, D.J.S. Fluorescence detections and directions. Meas. Sci. Technol., 2011, 22(5), 052002.
[http://dx.doi.org/10.1088/0957-0233/22/5/052002]

Rolinski, O.J.; Amaro, M.; Birch, D.J.S. Early detection of amyloid aggregation using intrinsic fluorescence. Biosens. Bioelectron., 2010, 25(10), 2249-2252.
[http://dx.doi.org/10.1016/j.bios.2010.03.005]

Nath, P.; Mahtaba, K.R.; Ray, A. Fluorescence-based portable assays for detection of biological and chemical analytes. Sensors, 2023, 23(11), 1-22.
[http://dx.doi.org/10.3390/s23115053]

Young-Ho Shin, M. Teresa Gutierrez-Wing, and Jin-Woo Choi, Review- Recent progress in portable fluorescence sensors. J. Electrochem. Soc., 2021, 168, 1-18.

Strianese, M.; Staiano, M.; Ruggiero, G.; Labella, T.; Pellecchia, C.; D’Auria, S. Fluorescence-Based Biosensors. Methods Mol. Biol., 2012, 875, 193-216.
[http://dx.doi.org/10.1007/978-1-61779-806-1_9] [PMID: 22573441]

Lohcharoenkal, W.; Abbas, Z.; Rojanasakul, Y. Advances in nanotechnology-based biosensing of immunoregulatory cytokines. Biosensors (Basel), 2021, 11(10), 364.
[http://dx.doi.org/10.3390/bios11100364] [PMID: 34677320]

Damborský, P.; Švitel, J.; Katrlík, J. Optical biosensors. Essays Biochem., 2016, 60(1), 91-100.
[http://dx.doi.org/10.1042/EBC20150010] [PMID: 27365039]

Jamerlan, A.; Soo, S.; Hulme, J. Advances in amyloid beta oligomer detection applications in Alzheimer’s disease. Trends Analyt Chem., 2020, 129, 115919.

Li, F.; Stewart, C.; Yang, S.; Shi, F.; Cui, W.; Zhang, S.; Wang, H.; Huang, H.; Chen, M.; Han, J. Optical sensor array for the early diagnosis of Alzheimer’s Disease. Front Chem., 2022, 10, 874864.
[http://dx.doi.org/10.3389/fchem.2022.874864] [PMID: 35444997]

Bunz, U.H. Poly(paraphenyleneethynylene and Poly(aryleneethynylene)s. Handbook of conducting polymers; CRC Press., 2007.

Mehrotra, Parikha Biosensors and their applications- A review. JOBCR-202, 2016, 6(2), 153-159.

Dominguez, M.H. Optical biosensors and their applications for the detection of water pollutants. Biosensors., 2023, 13(3), 370.

Ishigaki, Y.; Tanaka, H.; Akama, H.; Ogara, T.; Uwai, K.; Tokuraku, K. A microliter-scale high-throughput screening system with quantum-dot nanoprobes for amyloid-β aggregation inhibitors. PLoS One, 2013, 8(8), e72992.
[http://dx.doi.org/10.1371/journal.pone.0072992] [PMID: 23991168]

Sasaki, R.; Tainaka, R.; Ando, Y.; Hashi, Y.; Deepak, H.V.; Suga, Y.; Murai, Y.; Anetai, M.; Monde, K.; Ohta, K.; Ito, I.; Kikuchi, H.; Oshima, Y.; Endo, Y.; Nakao, H.; Sakono, M.; Uwai, K.; Tokuraku, K. An automated microliter-scale high-throughput screening system (MSHTS) for real-time monitoring of protein aggregation using quantum-dot nanoprobes. Sci. Rep., 2019, 9(1), 2587.
[http://dx.doi.org/10.1038/s41598-019-38958-0] [PMID: 30796247]

Akhtar, N.; Metkar, S.K.; Girigoswami, A.; Girigoswami, K. ZnO nanoflower based sensitive nano-biosensor for amyloid detection. Mater. Sci. Eng. C, 2017, 78, 960-968.
[http://dx.doi.org/10.1016/j.msec.2017.04.118] [PMID: 28576073]

Dong, J.; Fujita, R.; Zako, T.; Ueda, H. Construction of Quenchbodies to detect and image amyloid β oligomers. Anal. Biochem., 2018, 550, 61-67.
[http://dx.doi.org/10.1016/j.ab.2018.04.016] [PMID: 29678763]

Chen, W.; Gao, G.; Jin, Y.; Deng, C. A facile biosensor for Aβ₄₀O based on fluorescence quenching of prussian blue nanoparticles. Talanta, 2020, 216(120930), 120930.
[http://dx.doi.org/10.1016/j.talanta.2020.120930] [PMID: 32456942]

Xing, Z.W. Driving force to detect Alzheimer’s disease biomarkers: application of a thioflavine T@Er-MOF ratiometric fluorescent sensor for smart detection of presenilin 1, amyloid β-protein and acetylcholine. Analyst (Lond.), 2020, 145(4646), 1-18.