Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase

Journal of Structural Biology

Volumn 145, Issue 3, 2004, Pages 226-235

  Hamodrakas, S J ^a   Hoenger, A ^b   Iconomidou, V A ^a  

^a UNIVERSITY OF ATHENS   (Greece)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Amyloids; ATR FT IR; Electron microscopy; Fibrillogenesis; Liquid crystals; Silkmoth chorion peptides; X ray diffraction; pleated sheet

Indexed keywords

AMYLOID PROTEIN; CELL PROTEIN; CHORION PROTEIN; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL STRUCTURE; CHORION; CONTROLLED STUDY; ELECTRON MICROSCOPY; FIBRILLOGENESIS; INFRARED SPECTROSCOPY; LIQUID CRYSTAL; MOLECULAR BIOLOGY; MOLECULAR EVOLUTION; MORPHOGENESIS; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; X RAY DIFFRACTION;

ARANEAE;

EID: 1042267371     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.10.004     Document Type: Article

References (32)

1. Benaki D.C., Aggeli A., Chryssikos G.D., Yiannopoulos Y.D., Kamitsos E.I., Brumley E., Case S.T., Boden N., 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.
2. Cai S., 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.
3. Carel R.W., Gooptu B. Conformational changes and disease- serpins, prions and Alzheimer's. Curr. Opin. Struct. Biol. 8:1998;799-809.
4. Collaborative Computational Project, Number 4 The CCP4 Suite: Programs for Protein Crystallography 1994. Acta Cryst., D50, 760-763.
5. De Jongh H.H.J., Goormaghtigh E., 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. Guijarro J.I., Sunde M., Jones J.A., Cambell I.D., Dobson C.M. Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. USA. 95:1998;4224-4228.
8. Hamodrakas S.J. Molecular architecture of helicoidal proteinaceous eggshells. Case S.T. Results and Problems in Cell Differentiation. vol. 19:1992;115-186 Springer-Verlag, Berlin and Heidelberg. (Ch. 6).
9. Hamodrakas S.J., Etmektzoglou T., 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;583589.
10. Haris P.I., Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers (Peptide Science). 37:1995;251-263.
11. Iconomidou V.A., Vriend G., Hamodrakas S.J. Amyloids protect the silkmoth oocyte and embryo. FEBS Letters. 479:2000;141-145.
12. Iconomidou V.A., Chryssikos G.D., Gionis V., Vriend G., Hoenger A., 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 Letters. 499:2001;268-273.
13. Jackson M., Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Critical Reviews in Biochemistry and Molecular Biology. 30(2):1995;95-120.
14. Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6:1996;11-17.
15. Kelly J.W. Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7:2000;824-826.
16. Kenney J.M., Knight D., Wise M.J., Vollrath F. Amyloidogenic natue of spider silk. Eur. J. Biochem. 269:2002;4159-4163.
17. Krimm S., Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Prot. Chem. 38:1986;181-386.
18. Lekanidou R., Rodakis G.C., Eickbush T.H., Kafatos F.C. Evolution of the silkmoth chorion gene superfamily: gene families CA and CB. Proc. Natl. Acad. Sci. USA. 83:1986;6514-6518.
19. Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA. 93:1996;1125-1129.
20. Parbhu A., Lin H., Thimm J., Lal R. Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy. Peptides. 23:2002;1265-1270.
21. Regier J.C., Kafatos F.C. Molecular aspects of chorion formation. Gilbert L.I. Comprehensive Insect Biochemistry, Physiology and Pharmacology. vol. I:1985;113-151 Pergamon Press, Oxford and New York.
22. Rochet J.C., Lansbury P.T. Jr. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10:2000;60-68.
23. Savitsky A., Golay M.J.E. Smoothing and differentiation of data by simplified least-squares procedures. Anal. Chem. 36:1964;1627-1639.
24. Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498:2001;204-207.
25. Sunde M., Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Prot. Chem. 50:1997;123-159.
26. Sunde M., Blake C. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Quart. Rev. of Biophysics. 31(1):1998;1-39.
27. Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment. Biochemistry. 32(2):1993;389-394.
28. Tan S.Y., Pepys M.B. Amyloidosis. Histopathology. 25:1994;403-414.
29. Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., Benedek G.B., Selkoe D.J., Teplow D.B. Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274:1999;25945-25952.
30. Vollrath F., Knight D.P. Liquid crystalline spinning of spider silk. Nature. 410:2001;541-548.
31. Westlind-Danielsson A., Arnerup G. Spontaneous in vitro formation of supramolecular β-amyloid structures, "β amy balls", by β-amyloid 1-40 peptide. Biochemistry. 40:2001;14736-14743.
32. Žerovnik E. Amyloid fibril formation: Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 269:2002;3362-3371.