Abstract
Experimental studies of amyloids encounter many challenges. There are many methods available for studying proteins, which can be applied to amyloids: from basic staining techniques, allowing visualization of fibers, to complex methods, e.g., AFM-IR used to their detailed biochemical and structural characterization in nanoscale. Which method is appropriate depends on the goal of an experiment: verification of aggregational properties of a peptide, distinguishing oligomers from mature fibers, or kinetic studies. Insolubility, rapid aggregation, and the need of using a high-purity peptide may be a limiting factor in studies involving amyloids. Moreover, the results obtained by various experimental methods often differ significantly, which may lead to misclassification of amyloid peptides. Due to ambiguity of experimental results, laborious and time-consuming analysis, bioinformatical methods become more widely used for amyloids.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Sušec T (2016) Historical review. Acta Clin Croat 55:675. https://doi.org/10.20471/acc.2016.55.01.25
Tanskanen M (2013) “Amyloid” — historical aspects. In: Amyloidosis. InTech, Rijeka
Yakupova EI, Bobyleva LG, Vikhlyantsev IM, Bobylev AG (2019) Congo Red and amyloids: history and relationship. Biosci Rep 39:BSR20181415. https://doi.org/10.1042/BSR20181415
Otzen D (2010) Functional amyloid: turning swords into plowshares. Prion 4:256–264. https://doi.org/10.4161/pri.4.4.13676
Hayden EY, Conovaloff JL, Mason A et al (2018) Preparation of pure populations of amyloid β-protein oligomers of defined size. In: Methods in molecular biology. Humana Press Inc., Totowa, NJ, pp 3–12
Erskine E, MacPhee CE, Stanley-Wall NR (2018) Functional amyloid and other protein fibers in the biofilm matrix. J Mol Biol 430:3642–3656. https://doi.org/10.1016/j.jmb.2018.07.026
Benson MD, Buxbaum JN, Eisenberg DS et al (2018) Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee. Amyloid 25:215–219. https://doi.org/10.1080/13506129.2018.1549825
Wolfe KJ, Cyr DM (2011) Amyloid in neurodegenerative diseases: friend or foe? Semin Cell Dev Biol 22:476–481
Magalingam KB, Radhakrishnan A, ** NS, Haleagrahara N (2018) Current concepts of neurodegenerative mechanisms in Alzheimer’s disease. Biomed Res Int 2018:3740461. https://doi.org/10.1155/2018/3740461
Dobson CM, Knowles TPJ, Vendruscolo M (2020) The amyloid phenomenon and its significance in biology and medicine. Cold Spring Harb Perspect Biol 12:a033878. https://doi.org/10.1101/cshperspect.a033878
Tennent GA (1999) Isolation and characterization of amyloid fibrils from tissue. Methods Enzymol 309:26–47. https://doi.org/10.1016/S0076-6879(99)09004-7
Rostagno A, Ghiso J (2009) Isolation and biochemical characterization of amyloid plaques and paired helical filaments. Curr Protoc Cell Biol 44:3.33.1–3.33.33. https://doi.org/10.1002/0471143030.cb0333s44
Stenstad T, Magnus JH, Syse K, Husby G (1993) On the association between amyloid fibrils and glycosaminoglycans; possible interactive role of Ca2+ and amyloid P-component. Clin Exp Immunol 94:189–195. https://doi.org/10.1111/j.1365-2249.1993.tb05999.x
Kaplan B, Yakar S, Balta Y et al (1997) Isolation and purification of two major serum amyloid A isotypes SAA1 and SAA2 from the acute phase plasma of mice. J Chromatogr B Biomed Appl 704:69–76. https://doi.org/10.1016/S0378-4347(97)00462-3
Behrens NE, Lipke PN, Pilling D et al (2019) Secretion of inflammatory cytokines. MBio 10:1–14
Cutler P (2003) Protein purification protocols. Humana Press, Totowa, NJ
Esparza TJ, Wildburger NC, Jiang H et al (2016) Soluble amyloid-beta aggregates from human Alzheimer’s disease brains. Sci Rep 6:1–16. https://doi.org/10.1038/srep38187
Chhetri G, Pandey T, Chinta R et al (2015) An improved method for high-level soluble expression and purification of recombinant amyloid-beta peptide for in vitro studies. Protein Expr Purif 114:71–76. https://doi.org/10.1016/j.pep.2015.05.015
Warner CJA, Dutta S, Foley AR, Raskatov JA (2017) A tailored HPLC purification protocol that yields high-purity amyloid beta 42 and amyloid beta 40 peptides, capable of oligomer formation. J Vis Exp 2017:4–9. https://doi.org/10.3791/55482
Danielsen HN, Hansen SH, Herbst FA et al (2017) Direct identification of functional amyloid proteins by label-free quantitative mass spectrometry. Biomolecules 7:1–9. https://doi.org/10.3390/biom7030058
Ahmed AB, Kajava AV (2013) Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence. FEBS Lett 587:1089–1095. https://doi.org/10.1016/j.febslet.2012.12.006
Chan WC, White PD (2000) Fmoc solid phase peptide synthesis : a practical approach. Oxford University Press, Oxford
Chiti F, Stefani M, Taddei N et al (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424:805–808. https://doi.org/10.1038/nature01891
Palmieri LC, Melo-Ferreira B, Braga CA et al (2013) Stepwise oligomerization of murine amylin and assembly of amyloid fibrils. Biophys Chem 180–181:135–144. https://doi.org/10.1016/j.bpc.2013.07.013
Pawar AP, DuBay KF, Zurdo J et al (2005) Prediction of “aggregation-prone” and “aggregation- susceptible” regions in proteins associated with neurodegenerative diseases. J Mol Biol 350:379–392. https://doi.org/10.1016/j.jmb.2005.04.016
Stawikowski M, Fields GB (2012) Introduction to peptide synthesis. Curr Protoc Protein Sci Chapter 18:Unit 18.1. https://doi.org/10.1002/0471140864.ps1801s69
Yang Y (2015) Side reactions in peptide synthesis. Elsevier Inc., Amsterdam
Tickler A, Clip**dale A, Wade J (2004) Amyloid-beta as a “difficult sequence” in solid phase peptide synthesis. Protein Pept Lett 11:377–384. https://doi.org/10.2174/0929866043406986
Tam JP, Lu YA (1995) Coupling difficulty associated with interchain clustering and phase transition in solid phase peptide synthesis. J Am Chem Soc 117:12058–12063. https://doi.org/10.1021/ja00154a004
Nakaie CR, Oliveira E, Vicente EF et al (2011) Solid-phase peptide synthesis in highly loaded conditions. Bioorg Chem 39:101–109. https://doi.org/10.1016/j.bioorg.2011.01.001
Breinbauer R (2009) The power of functional resins in organic synthesis. Edited by Judit Tulla-Puche and Fernando Albericio. Angew Chem Int Ed 48:3560–3561. https://doi.org/10.1002/anie.200900955
Bayer E (1991) Towards the chemical synthesis of proteins. Angew Chem Int Ed Eng 30:113–129. https://doi.org/10.1002/anie.199101133
Hyde C, Johnson T, Owen D et al (1994) Some “difficult sequences” made easy. A study of interchain association in solid-phase peptide synthesis. Int J Pept Protein Res 5:431–440
Stewart J, Klis W, Epton R (1990) Innovations and perspectives in solid phase synthesis. SPCC(UK) Ltd., Birmingham
Zhang L, Goldammer C, Henkel B et al (1994) Innovation perspectives in solid phase synthesis. Mayflower Worldwide, Birmingham
Behrendt R, White P, Offer J (2016) Advances in Fmoc solid-phase peptide synthesis. J Pept Sci 22:4–27. https://doi.org/10.1002/psc.2836
Erdélyi M, Gogoll A (2002) Rapid microwave-assisted solid phase peptide synthesis. Synthesis 11:1592–1596. https://doi.org/10.1055/s-2002-33348
Kasim JK, Kavianinia I, Harris PWR, Brimble MA (2019) Three decades of amyloid beta synthesis: challenges and advances. Front Chem 7:472. https://doi.org/10.3389/fchem.2019.00472
Miranda MTM, Liria CW, Remuzgo C (2011) Difficult peptides. In: Amino acids, peptides and proteins in organic chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, pp 549–569
Nilsson MR (2004) Techniques to study amyloid fibril formation in vitro. Methods 34:151–160. https://doi.org/10.1016/j.ymeth.2004.03.012
Shen CL, Murphy RM (1995) Solvent effects on self-assembly of beta-amyloid peptide. Biophys J 69:640–651. https://doi.org/10.1016/S0006-3495(95)79940-4
Wei G, Shea JE (2006) Effects of solvent on the structure of the Alzheimer amyloid-β(25-35) peptide. Biophys J 91:1638–1647. https://doi.org/10.1529/biophysj.105.079186
Gade Malmos K, Blancas-Mejia LM, Weber B et al (2017) ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid 24:1–16. https://doi.org/10.1080/13506129.2017.1304905
Pachahara SK, Chaudhary N, Subbalakshmi C, Nagaraj R (2012) Hexafluoroisopropanol induces self-assembly of β-amyloid peptides into highly ordered nanostructures. J Pept Sci 18:233–241. https://doi.org/10.1002/psc.2391
Ryan TM, Caine J, Mertens HDT et al (2013) Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization. PeerJ 1:e73. https://doi.org/10.7717/peerj.73
Teplow DB (2006) Preparation of amyloid β-protein for structural and functional studies. Methods Enzymol 413:20–33
Rajamohamedsait HB, Sigurdsson EM (2012) Histological staining of amyloid and pre-amyloid peptides and proteins in mouse tissue. In: Amyloid proteins. Humana Press, Totowa, NJ, pp 411–424
Westermark GT, Johnson KH, Westermark P (1999) Staining methods for identification of amyloid in tissue. Methods Enzymol 309:3–25. https://doi.org/10.1016/S0076-6879(99)09003-5
Azriel R, Gazit E (2001) Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J Biol Chem 276:34156–34161. https://doi.org/10.1074/jbc.M102883200
Linke RP (2007) Congo red staining of amyloid: improvements and practical guide for a more precise diagnosis of amyloid and the different amyloidoses. In: Protein misfolding, aggregation, and conformational diseases. Springer, New York, NY, pp 239–276
Howie AJ (2019) Origins of a pervasive, erroneous idea: the “green birefringence” of congo red‐stained amyloid. Int J Exp Pathol 100:208–221. https://doi.org/10.1111/iep.12330
Clement CG, Truong LD (2014) An evaluation of Congo red fluorescence for the diagnosis of amyloidosis. Hum Pathol 45:1766–1772. https://doi.org/10.1016/j.humpath.2014.04.016
Yakupova EI, Vikhlyantsev IM, Bobyleva LG et al (2018) Different amyloid aggregation of smooth muscles titin in vitro. J Biomol Struct Dyn 36:2237–2248. https://doi.org/10.1080/07391102.2017.1348988
Nielsen L, Khurana R, Coats A et al (2001) Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40:6036–6046. https://doi.org/10.1021/bi002555c
Frid P, Anisimov SV, Popovic N (2007) Congo red and protein aggregation in neurodegenerative diseases. Brain Res Rev 53:135–160. https://doi.org/10.1016/j.brainresrev.2006.08.001
Podlisny MB, Walsh DM, Amarante P et al (1998) Oligomerization of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37:3602–3611. https://doi.org/10.1021/bi972029u
Ivancic VA, Ekanayake O, Lazo ND (2016) Binding modes of thioflavin T on the surface of amyloid fibrils studied by NMR. ChemPhysChem 17:2461–2464. https://doi.org/10.1002/cphc.201600246
Ziaunys M, Smirnovas V (2019) Additional thioflavin-T binding mode in insulin fibril inner core region. J Phys Chem B 123:8727–8732. https://doi.org/10.1021/acs.jpcb.9b08652
Lindberg DJ, Wenger A, Sundin E et al (2017) Binding of thioflavin-T to amyloid fibrils leads to fluorescence self-quenching and fibril compaction. Biochemistry 56:2170–2174. https://doi.org/10.1021/acs.biochem.7b00035
Morimoto K, Kawabata K, Kunii S et al (2009) Characterization of type I collagen fibril formation using thioflavin T fluorescent dye. J Biochem 145:677–684. https://doi.org/10.1093/jb/mvp025
Elghetany MT, Saleem A (1988) Methods for staining amyloid in tissues: a review. Stain Technol 63:201–212. https://doi.org/10.3109/10520298809107185
Hackl EV, Darkwah J, Smith G, Ermolina I (2015) Effect of acidic and basic pH on thioflavin T absorbance and fluorescence. Eur Biophys J 44:249–261. https://doi.org/10.1007/s00249-015-1019-8
Girych M, Gorbenko GP, Maliyov I et al (2016) Combined thioflavin T-congo red fluorescence assay for amyloid fibril detection. Methods Appl Fluoresc 4:034010. https://doi.org/10.1088/2050-6120/4/3/034010
Khurana R, Uversky VN, Nielsen L, Fink AL (2001) Is congo red an amyloid-specific dye? J Biol Chem 276:22715–22721. https://doi.org/10.1074/jbc.M011499200
Gilbertson JA, Theis JD, Vrana JA et al (2015) A comparison of immunohistochemistry and mass spectrometry for determining the amyloid fibril protein from formalin-fixed biopsy tissue. J Clin Pathol 68:314–317. https://doi.org/10.1136/jclinpath-2014-202722
Kebbel A, Röcken C (2006) Immunohistochemical classification of amyloid in surgical pathology revisited. Am J Surg Pathol 30:673–683. https://doi.org/10.1097/00000478-200606000-00002
Joo Kim M, Baek D, Truong L, Ro JY (2019) Pathologic findings of amyloidosis: recent advances. In: Amyloid diseases. IntechOpen, Rijeka
Ahmed M, Broeckx G, Baggerman G et al (2020) Next-generation protein analysis in the pathology department. J Clin Pathol 73:1–6
Li H, Rahimi F, Sinha S et al (2009) Amyloids and protein aggregation-analytical methods. In: Encyclopedia of analytical chemistry, 1st edn. Wiley, New York, NY
Nichols MR, Colvin BA, Hood EA et al (2015) Biophysical comparison of soluble amyloid-β(1-42) protofibrils, oligomers, and protofilaments. Biochemistry 54:2193–2204. https://doi.org/10.1021/bi500957g
Bruggink KA, Müller M, Kuiperij HB, Verbeek MM (2012) Methods for analysis of amyloid-β aggregates. J Alzheimers Dis 28:735–758. https://doi.org/10.3233/JAD-2011-111421
Mrdenovic D, Majewska M, Pieta IS et al (2019) Size-dependent interaction of amyloid β oligomers with brain total lipid extract bilayer - fibrillation versus membrane destruction. Langmuir 35:11940–11949. https://doi.org/10.1021/acs.langmuir.9b01645
Zhang H, Zheng X, Kwok RTK et al (2018) In situ monitoring of molecular aggregation using circular dichroism. Nat Commun 9:1–9. https://doi.org/10.1038/s41467-018-07299-3
Banerjee B, Misra G, Ashraf MT (2019) Circular dichroism. In: Data processing handbook for complex biological data sources. Elsevier, Amsterdam, pp 21–30
Joshi V, Shivach T, Yadav N, Rathore AS (2014) Circular dichroism spectroscopy as a tool for monitoring aggregation in monoclonal antibody therapeutics. Anal Chem 86:11606–11613. https://doi.org/10.1021/ac503140j
Miles AJ, Wallace BA (2016) Circular dichroism spectroscopy of membrane proteins. Chem Soc Rev 45:4859–4872. https://doi.org/10.1039/c5cs00084j
Ranjbar B, Gill P (2009) Circular dichroism techniques: biomolecular and nanostructural analyses - a review. Chem Biol Drug Des 74:101–120. https://doi.org/10.1111/j.1747-0285.2009.00847.x
Ren B, Hu R, Zhang M et al (2018) Experimental and computational protocols for studies of cross-seeding amyloid assemblies. In: Methods in molecular biology. Humana Press Inc., Totowa, NJ, pp 429–447
Juszczyk P, Kołodziejczyk AS, Grzonka Z (2005) Circular dichroism and aggregation studies of amyloid β (11-28) fragment and its variants. Acta Biochim Pol 52:425–431. https://doi.org/10.18388/abp.2005_3455
Benjwal S (2006) Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15:635–639. https://doi.org/10.1110/ps.051917406
Haken H, Wolf HC (2004) Vibrational spectroscopy. Springer, New York, NY, pp 193–224
Sarroukh R, Goormaghtigh E, Ruysschaert JM, Raussens V (2013) ATR-FTIR: a “rejuvenated” tool to investigate amyloid proteins. Biochim Biophys Acta Biomembr 1828:2328–2338
Zandomeneghi G, Krebs MRH, McCammon MG, Fändrich M (2009) FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci 13:3314–3321. https://doi.org/10.1110/ps.041024904
Shivu B, Seshadri S, Li J et al (2013) Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry 52:5176–5183. https://doi.org/10.1021/bi400625v
Ruysschaert JM, Raussens V (2018) ATR-FTIR analysis of amyloid proteins. In: Methods in molecular biology. Humana Press Inc., Totowa, NJ, pp 69–81
Cerf E, Sarroukh R, Tamamizu-Kato S et al (2009) Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide. Biochem J 421:415–423. https://doi.org/10.1042/BJ20090379
Grdadolnik J (2002) Atr-ftir spectroscopy: its advantages and limitations. Acta Chim Slov 49:631–642
Kazarian SG, Chan KLA (2013) ATR-FTIR spectroscopic imaging: recent advances and applications to biological systems. Analyst 138:1940–1951. https://doi.org/10.1039/c3an36865c
Corujo MP, Sklepari M, Ang DL et al (2018) Infrared absorbance spectroscopy of aqueous proteins: comparison of transmission and ATR data collection and analysis for secondary structure fitting. Chirality 30:957–965. https://doi.org/10.1002/chir.23002
Huang JB, Urban MW (1992) Evaluation and analysis of attenuated total reflectance FT-IR Spectra using Kramers-Kronig transforms. Appl Spectrosc 46:1666–1672. https://doi.org/10.1366/0003702924926970
Miljković M, Bird B, Diem M (2012) Line shape distortion effects in infrared spectroscopy. Analyst 137:3954–3964. https://doi.org/10.1039/c2an35582e
Goldberg ME, Chaffotte AF (2005) Undistorted structural analysis of soluble proteins by attenuated total reflectance infrared spectroscopy. Protein Sci 14:2781–2792. https://doi.org/10.1110/ps.051678205
Zuber G, Prestrelski SJ, Benedek K (1992) Application of Fourier transform infrared spectroscopy to studies of aqueous protein solutions. Anal Biochem 207:150–156. https://doi.org/10.1016/0003-2697(92)90516-A
Bonner OD, Curry JD (1970) Infrared spectra of liquid H2O and D2O. Infrared Phys 10:91–94. https://doi.org/10.1016/0020-0891(70)90003-5
Fabian H, Mantele W (2006) Infrared spectroscopy of proteins. In: Chalmers JM (ed) Handbook of vibrational spectroscopy. John Wiley & Sons, Ltd, Chichester
Cioni P, Strambini GB (2002) Effect of heavy water on protein flexibility. Biophys J 82:3246–3253. https://doi.org/10.1016/S0006-3495(02)75666-X
Sheu SY, Schlag EW, Selzle HL, Yang DY (2008) Molecular dynamics of hydrogen bonds in protein-D20: the solvent isotope effect. J Phys Chem A 112:797–802. https://doi.org/10.1021/jp0771668
Zhang J, Zhang X, Zhang F, Yu S (2017) Solid-film sampling method for the determination of protein secondary structure by Fourier transform infrared spectroscopy. Anal Bioanal Chem 409:4459–4465. https://doi.org/10.1007/s00216-017-0390-y
Kočišová E, Petr M, Šípová H et al (2017) Drop coating deposition of a liposome suspension on surfaces with different wettabilities: “coffee ring” formation and suspension preconcentration. Phys Chem Chem Phys 19:388–393. https://doi.org/10.1039/c6cp07606h
Kopecký V, Baumruk V (2006) Structure of the ring in drop coating deposited proteins and its implication for Raman spectroscopy of biomolecules. Vib Spectrosc 42:184–187. https://doi.org/10.1016/j.vibspec.2006.04.019
Krüger A, Bürkle A, Mangerich A, Hauser K (2018) A combined approach of surface passivation and specific immobilization to study biomolecules by ATR-FTIR spectroscopy1. Biomed Spectrosc Imaging 7:25–33. https://doi.org/10.3233/bsi-180174
Palombo F, Tamagnini F, Jeynes JCG et al (2018) Detection of Aβ plaque-associated astrogliosis in Alzheimer’s disease brain by spectroscopic imaging and immunohistochemistry. Analyst 143:850–857. https://doi.org/10.1039/c7an01747b
Ami D, Mereghetti P, Leri M et al (2018) A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes. Sci Rep 8:1–15. https://doi.org/10.1038/s41598-018-30995-5
Miller LM, Bourassa MW, Smith RJ (2013) FTIR spectroscopic imaging of protein aggregation in living cells. Biochim Biophys Acta Biomembr 1828:2339–2346
Zohdi V, Whelan DR, Wood BR et al (2015) Importance of tissue preparation methods in FTIR micro-spectroscopical analysis of biological tissues: “Traps for new users”. PLoS One 10:e0116491. https://doi.org/10.1371/journal.pone.0116491
Tuma R (2005) Raman spectroscopy of proteins: from peptides to large assemblies. J Raman Spectrosc 36:307–319. https://doi.org/10.1002/jrs.1323
Flynn JD, Lee JC (2018) Raman fingerprints of amyloid structures. Chem Commun 54:6983–6986. https://doi.org/10.1039/c8cc03217c
Kurouski D, Van Duyne RP, Lednev IK (2015) Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review. Analyst 140:4967–4980
Lochocki B, Morrema THJ, Ariese F et al (2020) The search for a unique Raman signature of amyloid-beta plaques in human brain tissue from Alzheimer’s disease patients. Analyst 145:1724–1736. https://doi.org/10.1039/c9an02087j
Fan W, **ng L, Chen N et al (2019) Promotion effect of succinimide on amyloid fibrillation of hen egg-white lysozyme. J Phys Chem B 123:8057. https://doi.org/10.1021/acs.jpcb.9b06958
Ishigaki M, Morimoto K, Chatani E, Ozaki Y (2019) Exploration of insulin amyloid polymorphism using Raman spectroscopy and imaging. bioRxiv:782672. https://doi.org/10.1101/782672
Astbury WT, Dickinson S, Bailey K (1935) The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem J 29:2351–2360.1. https://doi.org/10.1042/bj0292351
Parker MW (2003) Protein structure from X-ray diffraction. J Biol Phys 29:341–362
Carbajo RJ, Neira JL (2013) NMR for chemists and biologists. Springer, New York, NY
Haken H, Wolf HC (2004) The multi-electron problem in molecular physics and quantum chemistry. Springer, Berlin, pp 147–164
Tycko R (2011) Solid-state NMR studies of amyloid fibril structure. Annu Rev Phys Chem 62:279–299. https://doi.org/10.1146/annurev-physchem-032210-103539
Raghothama S (2010) NMR of peptides. J Indian Inst Sci 90:145
Sugiki T, Kobayashi N, Fujiwara T (2017) Modern technologies of solution nuclear magnetic resonance spectroscopy for three-dimensional structure determination of proteins open avenues for life scientists. Comput Struct Biotechnol J 15:328–339
Karamanos TK, Kalverda AP, Thompson GS, Radford SE (2015) Mechanisms of amyloid formation revealed by solution NMR. Prog Nucl Magn Reson Spectrosc 88–89:86–104
Loquet A, El Mammeri N, Stanek J et al (2018) 3D structure determination of amyloid fibrils using solid-state NMR spectroscopy. Methods 138–139:26–38
Simone Ruggeri F, Habchi J, Cerreta A, Dietler G (2016) AFM-based single molecule techniques: unraveling the amyloid pathogenic species. Curr Pharm Des 22:3950–3970. https://doi.org/10.2174/1381612822666160518141911
Cohen AS, Calkins E (1959) Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183:1202–1203. https://doi.org/10.1038/1831202a0
Galzitskaya O (2019) New mechanism of amyloid fibril formation. Curr Protein Pept Sci 20:630–640. https://doi.org/10.2174/1389203720666190125160937
Goldsbury C, Baxa U, Simon MN et al (2011) Amyloid structure and assembly: insights from scanning transmission electron microscopy. J Struct Biol 173:1–13. https://doi.org/10.1016/j.jsb.2010.09.018
Voigtländer B (2019) Atomic force microscopy. Springer International Publishing, Cham
Ruggeri FS, Šneideris T, Vendruscolo M, Knowles TPJ (2019) Atomic force microscopy for single molecule characterisation of protein aggregation. Arch Biochem Biophys 664:134–148. https://doi.org/10.1016/j.abb.2019.02.001
Chiang YL, Chang YC, Chiang IC et al (2015) Atomic force microscopy characterization of protein fibrils formed by the amyloidogenic region of the bacterial protein MinE on mica and a supported lipid bilayer. PLoS One 10:1–16. https://doi.org/10.1371/journal.pone.0142506
Shlyakhtenko LS, Gall AA, Lyubchenko YL (2013) Mica functionalization for imaging of DNA and protein-DNA complexes with atomic force microscopy. Methods Mol Biol 931:295–312. https://doi.org/10.1007/978-1-62703-056-4_13
Möller C, Allen M, Elings V et al (1999) Tap**-mode atomic force microscopy produces faithful high-resolution images of protein surfaces. Biophys J 77:1150–1158. https://doi.org/10.1016/S0006-3495(99)76966-3
Watanabe-Nakayama T, Ono K, Itami M et al (2016) High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates. Proc Natl Acad Sci U S A 113:5835–5840. https://doi.org/10.1073/pnas.1524807113
Adamcik J, Lara C, Usov I et al (2012) Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method. Nanoscale 4:4426–4429. https://doi.org/10.1039/c2nr30768e
Sweers K, van der Werf K, Bennink M, Subramaniam V (2011) Nanomechanical properties of α-synuclein amyloid fibrils: a comparative study by nanoindentation, harmonic force microscopy, and peakforce QNM. Nanoscale Res Lett 6:1–10. https://doi.org/10.1186/1556-276X-6-270
Winey M, Meehl JB, O’Toole ET, Giddings TH (2014) Conventional transmission electron microscopy. Mol Biol Cell 25:319–323. https://doi.org/10.1091/mbc.E12-12-0863
Williams DB, Carter CB, Williams DB, Carter CB (2009) Inelastic scattering and beam damage. In: Transmission electron microscopy. Springer, New York, NY, pp 53–71
Gras SL, Waddington LJ, Goldie KN (2011) Transmission electron microscopy of amyloid fibrils. Methods Mol Biol 752:197–214. https://doi.org/10.1007/978-1-60327-223-0_13
Leung N, Nasr SH, Sethi S (2012) How I treat amyloidosis: the importance of accurate diagnosis and amyloid ty**. Blood 120:3206–3213. https://doi.org/10.1182/blood-2012-03-413682
Fischer ER, Hansen BT, Nair V et al (2012) Scanning electron microscopy. In: Current protocols in microbiology. John Wiley & Sons, Inc, Hoboken, NJ, pp 2B.2.1–2B.2.47
Chiti F, Dobson CM (2017) Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade. Annu Rev Biochem 86:27–68. https://doi.org/10.1146/annurev-biochem-061516-045115
Langkilde AE, Vestergaard B (2009) Methods for structural characterization of prefibrillar intermediates and amyloid fibrils. FEBS Lett 583:2600–2609. https://doi.org/10.1016/j.febslet.2009.05.040
Orlov I, Myasnikov AG, Andronov L et al (2017) The integrative role of cryo electron microscopy in molecular and cellular structural biology. Biol Cell 109:81–93
Dubochet J, McDowall AW (1981) Vitrification of pure water for electron microscopy. J Microsc 124:3–4. https://doi.org/10.1111/j.1365-2818.1981.tb02483.x
Grassucci RA, Taylor DJ, Frank J (2007) Preparation of macromolecular complexes for cryo-electron microscopy. Nat Protoc 2:3239–3246. https://doi.org/10.1038/nprot.2007.452
Sorci M, Grassucci RA, Hahn I et al (2009) Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding. Proteins Struct Funct Bioinf 77:62–73. https://doi.org/10.1002/prot.22417
Kollmer M, Close W, Funk L et al (2019) Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue. Nat Commun 10:4760. https://doi.org/10.1038/s41467-019-12683-8
Almeida ZL, Brito RMM (2020) Structure and aggregation mechanisms in amyloids. Molecules 25:1195
Guerrero-Ferreira R, Taylor NMI, Arteni AA et al (2019) Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy. elife 8:e48907. https://doi.org/10.7554/eLife.48907
Malishev R, Tayeb-Fligelman E, David S et al (2018) Reciprocal interactions between membrane bilayers and S. aureus PSMα3 cross-α amyloid fibrils account for species-specific cytotoxicity. J Mol Biol 430:1431–1441. https://doi.org/10.1016/j.jmb.2018.03.022
Ruggeri FS, Šneideris T, Chia S et al (2019) Characterizing individual protein aggregates by infrared nanospectroscopy and atomic force microscopy. J Vis Exp:1–12. https://doi.org/10.3791/60108
Kulik AJ, Ruggeri FS, Gruszecki WI, Dietler G (2014) Nanoscale infrared spectroscopy of light harvesting proteins, amyloid structures and collagen fibres. Microsc Anal 28:11–14
Kurouski D, Deckert-gaudig T, Deckert V, Lednev IK (2014) Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced raman spectroscopy (TERS). Biophys J 106:263–271. https://doi.org/10.1016/j.bpj.2013.10.040
Kurouski D, Deckert-gaudig T, Deckert V, Lednev IK (2012) Structure and composition of insulin fibril surfaces probed by TERS. J Am Chem Soc 134:13323–13329. https://doi.org/10.1021/ja303263y
Fränzl M, Thalheim T, Adler J et al (2019) Thermophoretic trap for single amyloid fibril and protein aggregation studies. Nat Methods 16:611–614. https://doi.org/10.1038/s41592-019-0451-6
Acknowledgement
This work was partially supported by the National Science Centre, Poland, Grant 2019/35/B/NZ2/03997(MGG) and Grant No. 2017/26/D/ST5/00341 (MS), National Centre for Research and Development, Poland under POWR.03.02.00-00-I003/16 (NS).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Gąsior-Głogowska, M.E., Szulc, N., Szefczyk, M. (2022). Challenges in Experimental Methods. In: Li, M.S., Kloczkowski, A., Cieplak, M., Kouza, M. (eds) Computer Simulations of Aggregation of Proteins and Peptides . Methods in Molecular Biology, vol 2340. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1546-1_13
Download citation
DOI: https://doi.org/10.1007/978-1-0716-1546-1_13
Published:
Publisher Name: Humana, New York, NY
Print ISBN: 978-1-0716-1545-4
Online ISBN: 978-1-0716-1546-1
eBook Packages: Springer Protocols