Insulin amyloid fibrils form an inclusion complex with molecular iodine: A misfolded protein as a nanoscale scaffold

Biochemistry

Volumn 46, Issue 6, 2007, Pages 1568-1572

  Dzwolak, Wojciech ^a,b  

^a INSTITUTE OF HIGH PRESSURE PHYSICS   (Poland)

^b UNIVERSITY OF WARSAW   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

CONTROLLED DRUG DELIVERY; INSULIN; IODINE; MOLECULAR DYNAMICS; NANOSTRUCTURED MATERIALS; RESONANCE;

CHEMICAL REAGENT; FIBRILS; NANOSCALE SCAFFOLD; RESONANCE RAMAN SPECTRA;

PROTEINS;

AMYLOID; DIMETHYL SULFOXIDE; INSULIN; IODINE; MOLECULAR SCAFFOLD; NANOFIBER;

ARTICLE; BETA SHEET; COMPLEX FORMATION; CONTROLLED STUDY; NANOANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BOUND IODINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; STRUCTURE ANALYSIS;

AMYLOID; INSULIN; IODINE; PROTEIN FOLDING; SPECTRUM ANALYSIS, RAMAN; ULTRAVIOLET RAYS;

EID: 33847000210     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061985l     Document Type: Article

References (33)

1. Uversky, V. N., and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: The importance of being unfolded, Biochim. Biophys. Acta 1698, 131-153.
2. Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease, Nat. Med. Suppl., S10-S17.
3. Dobson, C. M. (2003) Protein folding and misfolding, Nature 426, 884-890.
4. Virchow, R. (1853) Nouvelles observations sur la substance animale analogue à la cellulose végétale, C. R. Acad. Sci., Paris 37, 860-861.
5. Virchow, R. (1854) Weitere Mittheilungen über das Vorkommen der pflanzlichen Cellulose beim Menschen, Virchows Arch. 6, 268-271.
6. Aterman, K. (1976) A historical note on the iodine-sulphuric acid reaction of amyloid, Histochemistry 49, 131-143.
7. Puchtler, H., and Sweat, F. J. (1966) A review of early concepts of amyloid in context with contemporary chemical literature from 1839 to 1859, Histochem. Cytochem. 14, 123-134.
8. Teitelbaum, R. C., Ruby, S. L., and Marks, T. J. (1978) On the structure of starch-iodine, J. Am. Chem. Soc. 100, 3215-3217.
9. Calabrese, V. T., and Khan, A. (2000) Polyiodine and polyiodide species in an aqueous solution of iodine + KI: Theoretical and experimental studies, J. Phys. Chem. A 104, 1287-1292.
10. Svensson, P. H., and Kloo, L. (2003) Synthesis, structure, and bonding in polyiodide and metal iodide-iodine systems, Chem. Rev. 103, 1649-1684.
11. Foguel, D., Suarez, M. C., Ferrao-Gonzales, A. D., Porto, T. C. R., Palmieri, L., Einsiedler, C. M., Andrade, L. R., Lashuel, H. A., Lansbury, P. T., Kelly, J. W., and Silva, J. L. (2003) Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities, Proc. Natl. Acad. Sci. U.S.A. 100, 9831-9836.
12. Smirnovas, V., Winter, R., Funck, T., and Dzwolak, W. (2006) Protein amyloidogenesis in the context of volume fluctuations: An insulin case study, Chem. Phys. Chem. 7, 1046-1049.
13. Jimenez, J. L., Guijarro, J. L., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., and Saibil, H. R. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing, EMBO J. 18, 815-821.
14. Perutz, M. F., Finch, J. T., Berriman, J., and Lesk, A. (2002) Amyloid fibers are water-filled nanotubes, Proc. Natl. Acad. Sci. U.S.A. 99, 5591-5595.
15. 15.Dzwolak, W., Loksztejn, A., and Smirnovas, V. (2006) New insights into the self-assembly of insulin amyloid fibrils: An H-D exchange FT-IR study, Biochemistry 45, 8143-8151.
16. Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1, Anal. Biochem. 177, 244-249.
17. LeVine, H. (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T, Methods Enzymol. 309, 274-284.
18. Bennhold, H. (1922) Eine spesifische Amyloid-farbung mit Kongrot, Munchen. Med. Wochen. 69, 1537-1538.
19. Nilsson, K. P. R., Herland, A., Hammarstrom, P., and Inganas, O. (2005) Conjugated polyelectrolytes: Conformation-sensitive optical probes for detection of amyloid fibril formation, Biochemistry 44, 3718-3724.
20. Jansen, R., Dzwolak, W., and Winter, R. (2005) Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy, Biophys. J. 88, 1344-1353.
21. Cooper, J. H. (1974) Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods, Lab. Invest. 31, 232-238.
22. Dzwolak, W., Smirnovas, V., Jansen, R., and Winter, R. (2004) Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study, Protein Sci. 13, 1927-1932.
23. Heyde, M. E., Rimai, L., Kilponen, R. G., and Gill, D. (1972) Resonance-enhanced Raman spectra of iodine complexes with amylose and poly(vinyl alcohol), and of some iodine-containing trihalides, J. Am. Chem. Soc. 94, 5222-5227.
24. Teitelbaum, R. C., Ruby, S. L., and Marks, T. J. (1980) A resonance Raman/iodine Moessbauer investigation of the starch-iodine structure. Aqueous solution and iodine vapor preparations, J. Am. Chem. Soc. 102, 3322-3328.
25. Yu, X., and Atalla, R. H. (2005) The complex of xylan and iodine: The induction and detection of nanoscale order, Carbohydr. Res. 340, 981-988.
26. Sengupta, A., Quitevis, E. L., and Holtz, M. W. (1997) Effect of high pressure on vibrational modes of polyiodides in poly(vinyl alcohol) films, J. Phys. Chem. B 101, 11092-11098.
27. Sengupta, A., Holtz, M., and Quitevis, E. L. (1996) Temperature-dependent resonance Raman study of iodine-doped poly(vinyl alcohol) films, Chem. Phys. Lett. 263, 25-32.
28. 2 vibration, J. Raman Spectrosc. 1, 417-431.
29. 2 in solutions, Chem. Phys. Lett. 28, 27-30.
30. Rousseau, D. L. (1976) Resonance Raman scattering of light from a diatomic molecule, J. Chem. Phys. 64, 3519-3537.
31. Sharp, S. B., and Gellene, G. I. (1997) Ab initio calculations of the ground electronic states of poiyiodide anions, J. Phys. Chem. A 101, 2192-2197.
32. Jimenez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., and Saibil, H. R. (2002) The protofilament structure of insulin amyloid fibrils, Proc. Natl. Acad. Sci. U.S.A. 99, 9196-9201.
33. 2-microglobulin amyloid fibrils by dimethylsulfoxide, J. Biochem. 134, 159-164.