Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family

Journal of Structural Biology

Volumn 156, Issue 3, 2006, Pages 480-488

  Iconomidou, Vassiliki A ^a   Chryssikos, Georgios D ^b   Gionis, Vassilis ^b   Galanis, Athanassios S ^c   Cordopatis, Paul ^c   Hoenger, Andreas ^d   Hamodrakas, Stavros J ^a  

^a UNIVERSITY OF ATHENS   (Greece)

^b THEORETICAL AND PHYSICAL CHEMISTRY INSTITUTE   (Greece)

^c UNIVERSITY OF PATRAS   (Greece)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Pleated sheet; Amyloids; ATR FT IR; Electron microscopy; Formation; Silkmoth chorion peptides; X ray diffraction

Indexed keywords

AMYLOID; CELL PROTEIN; HEXAPEPTIDE; PEPTIDE DERIVATIVE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHORION; LIQUID CRYSTAL; MUTATION; NONHUMAN; OOCYTE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROCESS DESIGN; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN SYNTHESIS; SILKWORM; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMYLOID; ANIMALS; BOMBYX; COMPUTER SIMULATION; EGG PROTEINS; INSECT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY, INFRARED; X-RAY DIFFRACTION;

EID: 33750994604     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.08.011     Document Type: Article

References (36)

1. Barlos K., Gatos D., Kallitsis J., Papaphotiou G., Sotiriou P., Wenquing Y., and Shafer W. Darstellung geschützter Peptid-fragmente unter Einsatz substituierter Triphenylmethyl-harze. Tetrahedron Lett. 30 (1989) 3943-3946
2. Benaki D.C., Aggeli A., Chryssikos G.D., Yiannopoulos Y.D., Kamitsos E.I., Brumley E., Case S.T., Boden N., and Hamodrakas S.J. Laser-Raman and FT-IR spectroscopic studies of peptide-analogues of silkmoth chorion protein segments, Int. J. Biol. Macromol. 23 (1998) 49-59
3. Cai S., and Singh B.R. Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophys. Chem. 80 (1999) 7-20
4. Collaborative Computational Project, Number 4 The CCP4 Suite: Programs for Protein Crystallography 1994 Acta Crystallogr. D50, 760-763.
5. De Jongh H.H.J., Goormaghtigh E., and Ruysschaert J.M. The different molar absorptivities of the secondary structure types in the Amide I region: An attenuated total reflection infrared study on globular proteins. Anal. Chem. 242 (1996) 95-103
6. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
7. Fields G.B., and Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35 (1990) 161-214
8. Geddes A.J., Parker K.D., Atkins E.D.T., and Beighton E. "Cross-β" conformation in proteins. J. Mol. Biol. 32 (1968) 343-358
9. Govaerts C., Wille H., Prusiner S.B., and Cohen F.E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Aacd. Sic. USA 101 22 (2004) 8342-8347
10. Hamodrakas S.J., Jones C.W., and Kafatos F.C. Secondary structure predictions for silkmoth chorion proteins. Biochim. Biophys. Acta 700 (1982) 42-51
11. Hamodrakas S.J., Etmektzoglou T.H., and Kafatos F.C. Amino acid periodicities and their structural implications for the evolutionarily conservative central domain of some silkmoth chorion proteins. J. Mol. Biol. 186 (1985) 583-589
12. Hamodrakas S.J. Molecular architecture of helicoidal proteinaceous eggshells. In: Case S.T. (Ed). Results and Problems in Cell Differentiation (1992), Springer, Berlin 115-186 vol. 19 (Ch. 6)
13. Hamodrakas S.J., Hoenger A., and Iconomidou V.A. Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid crystalline intermediate phase. J. Struct. Biol. 145 (2004) 226-235
14. Haris P.I., and Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers (Pept. Sci.) 37 (1995) 251-263
15. Haris P.I., and Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catalysis B: Enzymatic 7 (1999) 207-221
16. Iconomidou V.A., Vriend G., and Hamodrakas S.J. Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 479 (2000) 141-145
17. Iconomidou V.A., Chryssikos G.D., Gionis V., Vriend G., Hoenger A., and Hamodrakas S.J. Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins. FEBS Lett. 499 (2001) 268-273
18. Jackson M., and Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30 2 (1995) 95-120
19. Kafatos F.C., Regier J.C., Mazur G.D., Nadel M.R.H.M., Petri W.H., Wyman A.R., Gelinas R.E.P.B., Paul M., Efstratiadis A., Vournakis J.N., Goldsmith M.R., Hunsley J.R., Baker B., Nardi J., and Koehler M. The eggshell of insects: differentiation-specific proteins and the control of their synthesis and accumulation during development. In: Beerman W. (Ed). Results and Problems in Cell Differentiation (1977), Springer-Verlag, Berlin Heidelberg New York 45-145 Vol 8
20. Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior, Curr. Opin. Struct. Biol. 6 (1996) 11-17
21. Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways, Curr. Opin. Struct. Biol. 8 (1998) 101-106
22. Khurana R., and Fink A.L. Do parallel β-helix proteins have a unique Fourier transform infrared spectrum. Biophys. J. 78 (2000) 994-1000
23. Kishimoto A., Hasegawa K., Suzuki H., Taguchi H., Namba K., and Yoshida M. β-Helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem. Biophys. Res. Commun. 315 (2004) 739-745
24. Kraulis P.J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
25. Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-386
26. Lekanidou R., Rodakis G.C., Eickbush T.H., and Kafatos F.C. Evolution of the silkmoth chorion gene superfamily: gene families CA and CB. Proc. Natl. Acad. Sci. USA 83 (1986) 6514-6518
27. Miranda L.P., and Alewood P.F. Accelerated chemical synthesis of peptides and small proteins. Proc. Natl. Acad. Sci. U S A 96 (1999) 1181-1186
28. Pepys M.B. Amyloidosis. In: Weatherall D.J., Ledingham J.G.G., and Warell D.A. (Eds). The Oxford Textbook of Medicine (1996), Oxford University Press, Oxford, UK 1512-1524 3rd ed. Vol 2
29. Pickersgill R.W. A primordial structure underlying amyloid. Structure 11 (2003) 137-138
30. Regier J.C., and Kafatos F.C. Molecular aspects of chorion formation. In: Gilbert L.I., and Kerkut G.A. (Eds). Comprehensive Insect Biochemistry. Physiology and Pharmacology (1985), Pergamon Press, Oxford and New York 113-151 Vol I.
31. Savitsky A., and Golay M.J.E. Smoothing and differentiation of data by simplified least-squares procedures, Anal. Chem. 36 (1964) 1627-1639
32. Sunde M., and Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
33. Surewicz W.K., Mantsch H.H., and Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy:. A critical assessment, Biochemistry 32 2 (1993) 389-394
34. Wetzel R. Ideas of order for amyloid fibril structure. Structure 10 (2002) 1031-1036
35. Wille H., Mitchelitsch M.D., Guénebaut V., Supattapone S., Serban A., Cohen F.E., Agard D.A., and Prusiner S.B. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Aacd. Sic. USA 99 6 (2002) 3563-3568
36. Williams A.D., Portelius E., Kheterpal I., Jun-Tao G., Cook K.D., Hu Y., and Wetzel R. Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis. J. Mol. Biol. 335 (2004) 833-842