Abstract
Congo red (CR) and other self-assembling compounds creating supramolecular structures of rod- or ribbon-like architecture form specific complexes with cellulose and also with many proteins, including antibodies bound to the antigen and amyloids in particular. The mechanism of complexation and structure of these complexes are still poorly recognized despite the importance of the problem for medicine. This work proposes the progress in electron microscopy studies of amyloid-dye complexes by labeling supramolecular ligand CR with silver ions as a marker. Silver ions are introduced to CR carried by the strongly binding silver dye Titan yellow, which in addition form comicellar structures with CR. Silver carried by self-assembled dye molecules forms in the resulting metal nanoparticles, making the specific amyloid ligand CR perceptible in EM studies.
Acknowledgments
The authors acknowledge the financial support from the project Interdisciplinary PhD Studies “Molecular Sciences for Medicine” (co-financed by the European Social Fund within the Human Capital Operational Programme).
Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: None declared.
Employment or leadership: None declared.
Honorarium: None declared.
Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.
References
1. Rudyk H, Vasiljevic S, Hennion RM, Birkett CR, Hope J, Gilbert IH. Screening Congo red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. J Gen Virol 2000;81:1155–64.10.1099/0022-1317-81-4-1155Search in Google Scholar
2. Lai L-L, Su F-Y, Lin Y-J, Ho C-H, Wang E. Synthesis and study of azo-dye compounds: various molecular stackings from different polarities of the molecules. Helv Chim Acta 2002;85:1517–22.10.1002/1522-2675(200205)85:5<1517::AID-HLCA1517>3.0.CO;2-6Search in Google Scholar
3. Rudyk H, Knaggs MH, Vasiljevic S, Hope J, Birkett C, Gilbert IH. Synthesis and evaluation of analogues of Congo red as potential compounds against transmissible spongiform encephalopathies. Eur J Med Chem 2003;38:567–79.10.1016/S0223-5234(03)00081-3Search in Google Scholar
4. Spólnik P, Konieczny L, Piekarska B, Rybarska J, Stopa B, Zemanek G, et al. The use of the Congo red-related dye DBACR to recognize the heavy chain-derived abnormality of myeloma immunoglobulins. Arch Immunol Ther Exp (Warsz) 2006;54: 217–21.10.1007/s00005-006-0024-0Search in Google Scholar
5. Lorenzo A, Yankner BA. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA 1994;91:12243–7.10.1073/pnas.91.25.12243Search in Google Scholar
6. Woodcock S, Henrissat B, Sugiyama J. Docking of Congo red to the surface of crystalline cellulose using molecular mechanics. Biopolymers 1995;36:201–10.10.1002/bip.360360208Search in Google Scholar
7. Benzinger TL, Gregory DM, Burkoth TS, Miller-Auer H, Lynn DG, Botto RE, et al. Propagating structure of Alzheimer’s beta-amyloid(10–35) is parallel beta-sheet with residues in exact register. Proc Natl Acad Sci USA 1998;95:13407–12.10.1073/pnas.95.23.13407Search in Google Scholar
8. Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Condron MM, Lomakin A, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999;274:25945–52.10.1074/jbc.274.36.25945Search in Google Scholar
9. Lim A, Makhov AM, Bond J, Inouye H, Connors LH, Griffith JD, et al. Betabellins 15D and 16D, de novo designed beta-sandwich proteins that have amyloidogenic properties. J Struct Biol 2000;130:363–70.10.1006/jsbi.2000.4272Search in Google Scholar
10. Skowronek M, Stopa B, Konieczny L, Rybarska J, Piekarska B, Szneler E, et al. Self-assembly of Congo red – a theoretical and experimental approach to identify its supramolecular organization in water and salt solutions. Biopolymers 1998;46:267–81.10.1002/(SICI)1097-0282(19981015)46:5<267::AID-BIP1>3.0.CO;2-NSearch in Google Scholar
11. Stopa B, Piekarska B, Konieczny L, Rybarska J, Spólnik P, Zemanek G, et al. The structure and protein binding of amyloid-specific dye reagents. Acta Biochim Pol 2003;50:1213–27.10.18388/abp.2003_3645Search in Google Scholar
12. Król M, Roterman I, Piekarska B, Konieczny L, Rybarska J, Stopa B, et al. An approach to understand the complexation of supramolecular dye Congo red with immunoglobulin L chain lambda. Biopolymers 2005;77:155–62.10.1002/bip.20197Search in Google Scholar
13. Piekarska B, Konieczny L, Rybarska J, Stopa B, Zemanek G, Szneler E, et al. Heat-induced formation of a specific binding site for self-assembled Congo red in the V domain of immunoglobulin L chain lambda. Biopolymers 2001;59:446–56.10.1002/1097-0282(200111)59:6<446::AID-BIP1049>3.0.CO;2-XSearch in Google Scholar
14. Spólnik P, Konieczny L, Piekarska B, Rybarska J, Stopa B, Zemanek G, et al. Instability of monoclonal myeloma protein may be identified as susceptibility to penetration and binding by newly synthesized Congo red derivatives. Biochimie 2004;86:397–401.10.1016/j.biochi.2004.05.002Search in Google Scholar
15. Piekarska B, Skowronek M, Rybarska J, Stopa B, Roterman I, Konieczny L. Congo red-stabilized intermediates in the lambda light chain transition from native to molten state. Biochimie 1996;78:183–9.10.1016/0300-9084(96)89503-4Search in Google Scholar
16. Glenner GG, Yanes ED, Page DI. The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation. J Histochem Cytochem 1972;20:821–6.10.1177/20.10.821Search in Google Scholar
17. Roterman I, Rybarska J, Konieczny L, Skowronek M, Stopa B, Piekarska B, et al. Congo red bound to α-1-proteinase inhibitor as a model of supramolecular ligand and protein complex. Comput Chem 1998;22:61–70.10.1016/S0097-8485(97)00014-4Search in Google Scholar
18. Krol M, Roterman I, Drozd A, Konieczny L, Piekarska B, Rybarska J, et al. The increased flexibility of CDR loops generated in antibodies by Congo red complexation favors antigen binding. J Biomol Struct Dyn 2006;23:407–16.10.1080/07391102.2006.10531235Search in Google Scholar
19. Jagusiak A, Konieczny L, Król M, Marszałek P, Piekarska B, Piwowar P, et al. Intramolecular immunological signal hypothesis revived – structural background of signalling revealed by using Congo red as a specific tool. Mini Rev Med Chem 2014 [Epub available in PubMed].10.2174/1389557514666141127150803Search in Google Scholar
20. Stopa B, Jagusiak A, Konieczny L, Piekarska B, Rybarska J, Zemanek G, et al. The use of supramolecular structures as protein ligands. J Mol Model 2013;19:4731–40.10.1007/s00894-012-1744-1Search in Google Scholar
21. Rybarska J, Konieczny L, Roterman I, Piekarska B. The effect of azo dyes on the formation of immune complexes. Arch Immunol Ther Exp (Warsz) 1991;39:317–27.Search in Google Scholar
22. Kaszuba J, Konieczny L, Piekarska B, Roterman I, Rybarska J. Bis-azo dyes interference with effector activation of antibodies. J Physiol Pharmacol 1993;44:233–42.Search in Google Scholar
23. Rybarska J, Piekarska B, Stopa B, Zemanek G, Konieczny L, Nowak M, et al. Evidence that supramolecular Congo red is the sole ligation form of this dye for L chain lambda derived amyloid proteins. Folia Histochem Cytobiol 2001;39:307–14.Search in Google Scholar
24. Carter DB, Chou KC. A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils. Neurobiol Aging 1998;19:37–40.10.1016/S0197-4580(97)00164-4Search in Google Scholar
25. Caughey B, Brown K, Raymond GJ, Katzenstein GE, Thresher W. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and Congo red [corrected]. J Virol 1994;68:2135–41.10.1128/jvi.68.4.2135-2141.1994Search in Google Scholar
26. Klunk WE, Jacob RF, Mason RP. Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol 1999;309:285–305.10.1016/S0076-6879(99)09021-7Search in Google Scholar
27. Chrambach A, Chrambach A, Brining SK. Gel electrophoretic distinction between Congo red nonreactive beta-amyloid (1–42) and beta-amyloid (1–40). Electrophoresis 2000;21: 760–1.10.1002/(SICI)1522-2683(20000301)21:4<760::AID-ELPS760>3.0.CO;2-5Search in Google Scholar
28. Findeis MA. Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization. Biochim Biophys Acta 2000;1502:76–84.10.1016/S0925-4439(00)00034-XSearch in Google Scholar
29. King HG, Pruden G. The component of commercial Titan yellow most reactive towards magnesium: its isolatin and use in determining magnesium in silicate minerals. Analyst 1967;92:83–90.10.1039/an9679200083Search in Google Scholar
30. Garner RJ. Colorimetric determination of magnesium in plasma or serum by means of Titan yellow. Biochem J 1946;40:828–31.10.1042/bj0400828Search in Google Scholar
31. Perez S, Mazeau K. Conformations, structures, and morphologies of celluloses. In: Diversity and functional versatility. Dumitriu S, editor. New York: Marcel Dekker, Inc., 2005:41–157.Search in Google Scholar
32. Moon RJ, Martini A, Nairn J, Simonsen J, Youngblood J. Cellulose nanomaterials review: structure, properties and nanocomposites. Chem Soc Rev 2011;40:3941–4.10.1039/c0cs00108bSearch in Google Scholar
33. Liao H-G, Zherebetskyy D, Xin H, Czarnik C, Ercius P, Elmund H, et al. Facet development during platinum nanocube growth. Science 2014;345:916–9.10.1126/science.1253149Search in Google Scholar
34. Azubel M, Koivisto J, Malola S, Bushnell D, Hura GL, Koh AL, et al. Electron microscopy of gold nanoparticles at atomic resolution. Science 2014;345:909–12.10.1126/science.1251959Search in Google Scholar
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