Raman optical activity study on insulin amyloid- and prefibril intermediate

Chirality

Volumn 24, Issue 2, 2012, Pages 97-103

  Yamamoto, Shigeki ^a   Watarai, Hitoshi ^b  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

Amyloid; Fibril; Insulin; Intermediate; Raman optical activity

Indexed keywords

AMYLOID; BOVINE INSULIN; PROLINE;

ACIDITY; ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; MOLECULAR INTERACTION; NONHUMAN; OPTICAL ROTATION; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN MODIFICATION; PROTEIN RENATURATION; PROTEIN STRUCTURE; RAMAN OPTICAL ACTIVITY; RAMAN SPECTROMETRY;

AMYLOID; ANIMALS; CATTLE; INSULIN; PEPTIDES; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS, RAMAN; TYROSINE;

EID: 84855516998     PISSN: 08990042     EISSN: 1520636X     Source Type: Journal    
DOI: 10.1002/chir.21029     Document Type: Article

References (82)

1. Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CCF. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997;273:729-739. (Pubitemid 27488813)
2. Serpell LC. Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 2000;1502:16-30. (Pubitemid 30433852)
3. Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999;24:329-332. (Pubitemid 29421804)
4. Kelly JW. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 1998;8:101-106. (Pubitemid 28107921)
5. Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D. Structure of the cross-β spine of amyloid-like fibrils. Nature 2005;435:773-778. (Pubitemid 40839722)
6. Kishimoto A, Hasegawa K, Suzuki H, Taguchi H, Namba K, Yoshida M. β-helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem Biophys Res Commun 2004;315:739-745. (Pubitemid 38229404)
7. Serpell LC, Smith JM. Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid. J Mol Biol 2000;299:225-231.
8. Brange J, Anderson L, Laursen ED, Meyn G, Rasmussen E. Toward Understanding insulin fibrillation. J Pharma Sci 1997;86:517-525. (Pubitemid 27203397)
9. Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001;40:6036-6046. (Pubitemid 32466306)
10. Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 2001;40:8397-8407.
11. Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci 2000;9:1960-1967.
12. Jimenez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR. The protofilament strucutre of insulin amyloid fibrils. PNAS 2002;99:9196-9201. (Pubitemid 34764590)
13. Burke MJ, Rougvie MA. Cross-beta protein structures. I. Insulin fibrils. Biochemistry 1972;11:2435-2439.
14. Dzwolak W, Loksztejn A, Smirnovas V. New insights into the self-assembly of insulin amyloid fibrils: an H-D exchange FTIR study. Biochemistry 2006;45:8143-8151. (Pubitemid 43993235)
15. Yu N, Liu CS, O'shea DC. Laser Raman spectroscopy and the comformation of insulin and proinsulin. J Mol Biol 1972;70:117-132.
16. Yu N, Jo BH, Chang RCC, Huber JD. Single-crystal Raman spectra of native insulin. Arch Biochem Biophys 1974;160:614-622.
17. Dong J, Wan Z, Popov M, Carey PR, Weiss MA. Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils. J Mol Biol 2003;330:431-442. (Pubitemid 36773714)
18. Ma S, Cao X, Mak M, Sadik A, Walkner C, Freedman TB, Lednev I, Dukor R, Nafie LA. Vibrational circular dichroism shows unusual sensitivity to protein fibril formation and development in solution. J Am Chem Soc 2007;129:12364- 12365. (Pubitemid 47598215)
19. Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys J 2000;79:1053-1065. (Pubitemid 30626196)
20. Barron LD, Buckingham AD. Vibrational optical activity. Chem Phys Lett 2010;492:199-213.
21. Barron LD. Molecular light scattering and optical activity, 2nd ed. Cambridge: Cambridge University Press; 2004.
22. Barron LD, Buckingham AD. Rayleigh and Raman scattering from optically active molecules. Mol Phys 1971;20:1111-1119.
23. Barron LD, Bogaard MP, Buckingham AD. Raman scattering of circularly polarized light by optically active molecules. J Am Chem Soc 1973;95:603-605.
24. Hug W, Kint S, Bailey GF, Schere JR. Raman circular intensity differential spectroscopy. The spectra of (-)-a-Pinene and (+)-a- Phenylethylamine. J Am Chem Soc 1975;97:5589-5590.
25. Haesler J, Schindelholz I, Riguet E, Bochet CG, Hug W. Absolute configuration of chirally deuterated neopentane. Nature 2007;446:526-529. (Pubitemid 46514729)
26. Zuber G, Hug W. Computational interpretation of vibrational optical activity: The ROA spectra of (4S)-4-methylisochromane and the (4S)-isomers of Galaxolide((R)) Helv. Chim Acta 2004;87:2208-2234. (Pubitemid 39371891)
27. Costante J, Hecht L, Polavarapu PL, Collet A, Barron LD. Absolute configuration of bromochlorofluoromethane from experimental and ab initio theoretical vibrational Raman optical activity. Angew Chem Int Edit 1997;36:885-887. (Pubitemid 27222056)
28. Yamamoto S, Watarai H, Bour P. Monitoring the backbone conformation of valinomycin by Raman optical activity. Chem Phys Chem 2011;12:1509-1518.
29. Yamamoto S, Straka M, Watarai H, Bour P. Formation and structure of the potassium complex of valinomycin in solution studied by Raman optical activity spectroscopy. Phys Chem Chem Phys 2010;12:11021-11032.
30. Mukhopadhyay P, Zuber G, Beratan DN. Characterizing aqueous solution conformations of a peptide backbone using Raman optical activity computations. Biophys J 2008;95:5574-5586.
31. Hudecová J, Kapitán J, Baumruk V, Hammer RP, Keiderling TA, Bour P. Side chain and flexibility contributions to the Raman optical activity spectra of a model cyclic hexapeptide. J Phys Chem A 2010;114:7642-7651.
32. Kaminský J, Kapitán J, Baumruk V, Bednárová L, Bour P. Interpretation of Raman and Raman optical activity spectra of a flexible sugar derivative, the gluconic acid anion. J Phys Chem A 2009;113:3594-3601.
33. Buděšínský M, Danecek P, Bedná rová L, Kapitán J, Baumruk V, Bour P. Comparison of quantitative conformer analyses by nuclear magnetic resonance and Raman optical activity spectra for model dipeptides. J Phys Chem A 2008;112:8633-8640.
34. Jacob CR, Luber S, Reiher M. Calculated Raman optical activity signatures of Tryptophan side chains. Chem Phys Chem 2008;9:2177-2188.
35. Kapitán J, Baumruk V, Kopecký V Jr, Bour P. Demonstration of the ring conformation in polyproline by the Raman optical activity. J Am Chem Soc 2006;128:2438-2443.
36. Kapitán J, Baumruk V, Kopecký V Jr, Bour P. Conformational flexibility of L-alanine zwitterion determines shapes of Raman and Raman optical activity spectral bands. J Phys Chem A 2006;110:4689-4696.
37. Barron LD, Hecht L, Blanch EW, Bell AF. Solution structure and dynamics of biomolecules from Raman optical activity. Prog Biophys Mol Biol 2000;73:1-49. (Pubitemid 30252105)
38. Blanch EW, Morozova-Roche LA, Cochran DAE, Doig AJ, Hecht L, Barron LD. Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. J Mol Biol 2000;301:553-563.
39. Blanch EW, Morozova-Roche LA, Hecht L, Noppe W, Barron LD. Raman optical activity characterization of native and molten globule states of equine lysozyme: Comparison with hen lysozyme and bovine alpha-lactalbumin. Biopolymers 2000;57:235-248. (Pubitemid 30415071)
40. Blanch EW, Gill AC, Rhie AGO, Hope J, Hecht L, Nielsen K, Barron LD. Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction. J Mol Biol 2004;343:467-476. (Pubitemid 39296879)
41. Blanch EW, McColl IH, Hecht L, Nielsen K, Barron LD. Structural characterization of proteins and viruses using Raman optical activity. Vib Spectrosc 2004;35:87-92.
42. McColl IH, Blanch EW, Hecht L, Barron LD. A study of alpha-helix hydration in polypeptides, proteins, and viruses using vibrational Raman optical activity. J Am Chem Soc 2004;126:8181-8188. (Pubitemid 38878963)
43. McColl IH, Blanch EW, Hecht L, Kallenbach NR, Barron LD. Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides. J Am Chem Soc 2004;126:5076-5077. (Pubitemid 38509458)
44. Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD. New insight into the solution structures of wheat gluten proteins from Raman optical activity. Biochemistry 2003;42:5665-5673. (Pubitemid 36582857)
45. McColl IH, Blanch EW, Gill AC, Rhie AGO, Ritchie MA, Hecht L, Nielsen K, Barron LD. A new perspective on beta-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein. J Am Chem Soc 2003;125:10019-10026. (Pubitemid 36994931)
46. Barron LD, Blanch EW, Hecht L. Unfolded proteins studied by raman optical activity. Adv Prot Chem 2002;62:51-90. (Pubitemid 35204868)
47. Blanch EW, Robinson DJ, Hecht L, Syme CD, Nielsen K, Barron LD. Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity. J Gen Virol 2002;83:241-246. (Pubitemid 34030828)
48. Blanch EW, Hecht L, Day LA, Pederson DM, Barron LD. Tryptophan absolute stereochemistry in viral coat proteins from Raman optical activity. J Am Chem Soc 2001;123:4863-4864. (Pubitemid 32895795)
49. Blanch EW, Robinson DJ, Hecht L, Barron LD. A comparison of the solution structures of tobacco rattle and tobacco mosaic viruses from Raman optical activity. J Gen Virol 2001;82:1499-1502. (Pubitemid 32519782)
50. Smyth E, Syme CD, Blanch EW, Hecht L, Vasak M, Barron LD. Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 2001;58:138-151. (Pubitemid 32096458)
51. Hug W, Hangartner G. A novel high-throughput Raman spectrometer for polarization difference measurements. J Raman Spectrosc 1999;30:841-852.
52. Hug W. Virtual enantiomers as the solution of optical activity's deterministic offset problem. Appl Spectrosc 2003;57:1-13.
53. Yamamoto S, Watarai H. Incident circularly polarized Raman optical activity spectrometer based on circularity conversion method. J Raman Spectrosc 2010;41:1664.
54. Smith GD, Pangborn WA, Blessing RH. The structure of T6 bovine insulin. Acta Cryst D 2005;61:1476-1482.
55. Heinig M, Frishman D. STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucl Acids Res 2004;32:W500-W502. (Pubitemid 38997383)
56. Colaianni SEM, Nielsen OF. Low-frequency Raman spectroscopy. J Mol Struct 1995;347:267-284.
57. Lee SH, Krimm S. Polarized Raman spectra of oriented films of alpha-helical poly(L-alanine) and its N-deuterated analogue. J Raman Spectrosc 1998;29:73-80. (Pubitemid 128490058)
58. Lee SH, Krimm S. Ab initio-based vibrational analysis of alpha-poly(L-alanine). Biopolymers 1998;46:283-317.
59. Perczel A, Park K, Fasman GD. Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of antiparallel β-sheet in proteins. Proteins 1992;13:57-69.
60. Vass E, Hollosi M, Besson F, Buchet R. Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins. Chem Rev 2003;103:1917-1954.
61. Blanch EW, Hecht L, Barron LD. New insight into the pH-dependent conformational changes in bovine beta-lactoglobulin from Raman optical activity. Prot Sci 1999;8:1362-1367. (Pubitemid 29264968)
62. Tanford C, Bunville LG, Nozaki Y. The reversible transformation of β-lactoglobulin at pH 7.5. J Am Chem Soc 1959;81:4032-4036.
63. Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB. Structural basis of the tanford transition of bovine ǎ;-lactoglobulin. Biochemistry 1998;37:14014-14023. (Pubitemid 28471234)
64. Taulier N, Chalikian TV. Characterization of pH-induced transitions of blactoglobulin: ultrasonic, densimetric, and spectroscopic studies. J Mol Biol 2001;314:873-889. (Pubitemid 34087854)
65. Sakurai K, Konuma T, Yagi M, Goto Y. Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR. Biochim Biophys Acta 2009;1790:527-537.
66. Sakurai K, Goto Y. Dynamics and mechanism of the tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy. J Mol Biol 2006;356:483-496. (Pubitemid 43099985)
67. Sakurai K, Goto Y. Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR. Proc Natl Acad Sci U S A 2007;104:15346-15351. (Pubitemid 47502920)
68. Brownlow S, Cabral JHM, Cooper R, Flower DR, Yewdall SJ, Polikarpov I, North ACT, Sawyer L. Bovine β-lactoglobulin at 1.8 angstrom resolution-still an enigmatic lipocalin. Structure 1997;5:481-495. (Pubitemid 27191225)
69. -1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds. Biochemistry 1975;14:4870-4876.
70. Arp Z, Autrey D, Laane J, Overman SA, Thomas GJ Jr. Tyrosine Raman signatures of the filamentous virus Ff are diagnostic of non-hydrogenbonded phenoxyls: demonstration by Raman and infrared spectroscopy of p-cresol vapor. Biochemistry 2001;40:2522-2529. (Pubitemid 32171726)
71. Perutz MF, Finch JT, Berriman J, Lesk A. Amyloid fibers are water-filled nanotubes. PNAS 2002;99:5591-5595. (Pubitemid 34411593)
72. Schulman BA, Kim PS, Dobson CM, Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Struct Biol 1997;4:630-634. (Pubitemid 27323445)
73. Schulman BA, Redfield C, Peng ZY, Dobson CM, Kim PS. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin. J Mol Biol 1995;253:651-657.
74. Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. Structure and dynamics of the acid-denatured molten globule state of alphalactalbumin: a two-dimensional NMR study. Biochemistry 1993;32:1707-1718. (Pubitemid 23066443)
75. Baum J, Dobson CM, Evans PA, Hanley C. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. Biochemistry 1989;28:7-13. (Pubitemid 19046715)
76. Ewbank JJ, Creighton TE. The molten globule protein conformation probed by disulphide bonds. Nature 1991;350:518-520. (Pubitemid 21912268)
77. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Prot: Struct Funct Genet 1989;6:87-103. (Pubitemid 19286669)
78. Peng Z, Kim PS. A protein dissection study of a molten globule. Biochemistry 1994;33:2136-2141. (Pubitemid 24099610)
79. Wu LC, Peng Z, Kim PS. Bipartite structure of the β-lactalbumin molten globule. Nat Nat Struct Biol 1995;2:281-286.
80. Yutani K, Ogasahara K, Kuwajima K. Absence of the thermal transition in apo-alphalactalbumin in the molten globule state. A study by differential scanning microcalorimetry. J Mol Biol 1992;228:347-350. (Pubitemid 23007558)
81. Setnicka V, Huang R, Thomas CL, Etienne MA, Kubelka J, Hammer RP, Keiderling TA. IR study of cross-strand coupling in a beta-hairpin peptide using isotopic labels. J Am Chem Soc 2005;127:4992-4993. (Pubitemid 40523438)
82. Huang R, Kubelka J, Barber-Armstrong W, Silva RAGD, Decatur SM, Keiderling TA. Nature of vibrational coupling in helical peptides: an isotopic labeling study. J Am Chem Soc 2004;126:2346-2354. (Pubitemid 38295714)