The terminally protected peptide Boc-Leu-Val-Phe-Phe-Ala-OMe bearing sequence similarity with the central hydrophobic cluster (CHC) of Alzheimer’s Aβ17–21 peptide self-assembles to produce amyloid-like straight unbranched fibrils from organic solvents. The fibrils readily bind with a physiological dye Congo red (CR) and exhibits green gold birefringence under polarized light, a characteristic feature of amyloid plaque obtained from many neurodegenerative diseases. FTIR spectroscopy and in silico energy minimization study shed some light on the antiparallel supramolecular β-sheet aggregation of the peptide.
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Abbenante G., March D. R., Bergman D. A., Hunt P. A., Garnham B., Dancer R. J., Martin J. L., Fairlie D. P. (1995) J. Am. Chem. Soc. 41: 10220–10226
Antzutkin O. N., Balbach J. J., Leapman R. D., Rizzo N. W., Reed J., Tycko R., (2000) Proc. Natl. Acad. Sci. U. S. A. 97: 13045–13050
Arimon, M., Díez-Pérez, I., Kogan, M. J., Durany, N., Giralt, E., Sanz, F., and Fernàndez-Busquets, X.: 2005, FASEB J. 19, 1344–1346
Arvinte T., Cudd A., Drake A. F. (1993) J. Biol. Chem. 268: 6415–6422
Azriel R., Gazit E. (2001) J. Biol. Chem. 226: 34156–34161
Balbach J. J., Ishii Y., Antzutkin O. N., Leapman R. D., Rizto N. W., Dyda F., Reed J., Tycko R. (2000) Biochemistry 39: 13748–13759
Baldwin M. A., Cohen F. E., Prusiner S. B. (1995) J. Biol. Chem. 270: 19197–19200
Barrow C. J., Zagorski M. G. (1991) Science 253: 179–182
Baumeister R., Eimer S. (1998) Angew. Chem. Int. Ed. 37: 2978–2982
Benzinger T. L. S., Gregory D. M., Burkoth T. S., Miller-Auer H., Lynn D. G., Botto R. E., Meredith S. C. (1998) . Sci. U. S. A. 95: 13407–13412
Binder W. H., Smrzka O. S. (2006) Angew. Chem. Int. Ed. 45: 7324–7328
Blondelle S. E., Forood B., Houghten R. A., Peraz-Paya E. (1997) Biochemistry 36: 8393–8400
Chen S., Ferrone F. A., Wetzel R. (2002) Proc. Natl. Acad. Sci. U.S.A. 99:11884–11889
Dado G. P., Gellman S. H. (1994) J. Am. Chem. Soc. 116: 1054–1062
Der-Sarkissian A., Jao C. C., Chen J., Langen R. (2003) J. Biol. Chem. 278: 37530–37535
Dobson C. M. (2002) Nature 418: 729–730
Eisenberg D., Nelson R., Sawaya M. R., Balbirnie M., Sambashivan S., Ivanova M. I., Madsen A. Ø., Riekel C. (2006) Acc. Chem. Res. 39: 568–575
Formaggio F., Bettio A., Moretto V., Crisma M., Toniolo C., Broxterman Q. B. (2003) J. Pept. Sci. 9: 461–466
Fraser P. E., Nguyen J. T., Surewicz W. K., Kirschner D. A. (1991) Biophys. J. 60: 1190–1201
Goldsbury C., Goldie K., Pellaud J., Seelig J., Frey P., Müller S. A., Kister J., Cooper G. J. S., Aebi U. (2000) J. Struct. Biol. 130: 352–362
Haldar D., Drew M. G. B., Banerjee A. (2006) Tetrahedron 62: 6370–6378
Haldar, D. and Banerjee, A.: 2006, Int. J. Pept. Res. Therap. 12, 341–348.
Harper J. D., Wong S. S., Lansbury P. T. Jr. (1997) Chem. Biol. 4: 119–125
Inoyue H., Deepak S., Goux W., Kirschner D. A. (2006) Biophys. J. 90: 1774–1789
Inouye H., Fraser P. E., Kirschner D. A. (1993) Biophys. J. 64: 502–519
Iwata K., Fujiwara T., Matsuki Y., Akutsu H., Takahashi S. Naiki H., Goto Y. (2006) Proc. Natl. Acad. Sci. 103:18119–18124
Jayasinghe S. A., Langen R. (2004) J. Biol. Chem. 279: 48420–48425
Johansson J. (2005) FEBS J. 272: 5941–5941
Junn E., Ronchetti R. D., Quezado M. M., Kim S. Y., Mouradian M. M. (2003) Proc. Natl. Acad. Sci. 100: 2047–2052
Kelly J. W. (1996) Curr. Opin. Struct. Biol. 6: 11–17
Khurana R., Uversky V. N., Nielsen L., Fink A. L. (2001) J. Biol. Chem. 276: 22715–22721
Kim Y. S., Randolph T. W., Manning M. C., Stevens F. J., Carpenter J. F. (2003) J. Biol. Chem. 278: 10842–10850
Lansbury P. T. Jr. (1996) Acc. Chem. Res. 29: 317–321
Lansbury, P. T., Costa, P. R., Griffiths, J. M., Simon, E. J., Auger, M., Halverson, K. J., Kocisko, D. A., Hendsch Z. S., Ashburn, T. T., Spencer, R. G. S., Tidor, B. and Griffin, R. G.: 1995, Nat. Struct. Biol. 2, 990–998
Lim A., Makhov A. M., Bond J., Inouye H., Conmors L. H., Griffith J. D., Erickson W. B., Kirschner D. A., Costello C. E. (2000) J. Struct Biol. 130: 363–370
Lynn D. G., Meredith S. C. (2000) J. Struct. Biol. 130: 153–173
Maji S. K., Amsden J. J., Rothschild K. J., Condron M. M., Teplow D. B. (2005) Biochemistry 44: 13365–13376
Makin O. S., Serpell L. C. (2005) FEBS J. 272: 5950–5961
Margittai M., Langen R. (2004) Proc. Natl. Acad. Sci. 101:10278–10283
Meital R., Parot Y., Gazit E. (2002) J. Biol. Chem. 277: 35475–35480
Moretto V., Crisma M., Bonora G. M., Toniolo C., Balaram H., Balaram P. (1989) Macromolecules 22: 2939–2944
Ng S. B. L., Doig A. J. (1997) Chem. Soc. Rev. 26: 425–432
Paz M. L., Goldie K., Zurdo J., Lacroix E., Dobson C. M., Hoenger A., Serrano L. (2002) Proc. Natl. Acad. Sci. U. S. A. 99: 16052–16057
Petkova A. T., Ishii Y., Balbach J. J., Antzutkin O. N., Leapman R. D., Delaglio F., Tycko R. (2002) Proc. Natl. Acad. Sci. U. S. A. 99: 16742–16747
Petkova A. T., Buntkowsky G., Dyda F., Leapman R. D., Yau W. M., Tycko R. (2004) J. Mol. Biol. 335: 247–260
Prusiner S. B. (1998) Proc. Natl. Acad. Sci. U. S. A. 95: 13363–13383
Puglielli L., Tanzi R. E., Kovacs D. M. (2003) Nat. Neurosci. 6: 345–351
Rochet J. C., Lansbury P. T. Jr. (2000) Curr. Opin. Struct. Biol. 10: 60–68
Ray, S., Das, A. K., Drew, M. G. B. and Banerjee, A.: 2006, Chem. Commun., 4230–4232
Sadqi M., Hernández F., Pan U., Pérez M., Schaeberle M. D., Ávila J., Muñoz V. (2002) Biochemistry 41: 7150–7155
Schaftennar, G., Molden a package for displaying molecular density, e-mail: shaaft@caos.kun.nl
Scherzinger E., Sittler A., Schweiger K., Heiser V., Lurz R., Hasenbank R., Bates G. P., Lehrach H., Wanker E. E. (1999) Proc. Natl. Acad. Sci. U. S. A. 96: 4604–4609
Selkoe D. J. (2003) Nature 426: 900–904
Soto C., Sigurdsson E. M., Morelli L., Kumar R. A., Castano E. M., Frangione B. (1998) Nat. Med. 4: 822–826
Soto C. (2001) FEBS Lett. 498: 204–207
Spillantini M. G., Crowther R. A., Jakes R., Hasegawa M., Goedert M. (1998) Proc. Natl. Acad. Sci. U. S. A. 95: 6469–6473
Stewart J. J. P. (1990) J. Comput Aided Mol Des 4: 1–105
Taubes G. (1996) Science 271: 1493–1495
Taylor D. L., Allen R. D., Benditt E. P. (1974) J. Histochem. Cytochem. 22: 1105–1112
Toniolo C., Palumbo M. (1977) Biopolymers 16: 219–224
Török M., Milton S., Kayed R., Wu P., McIntire T., Glabe C. G., Langen R. (2002) J. Biol. Chem. 277: 40810–40815
Tycko R. (2003) Biochemistry 42: 3151–3159
Walsh D. M., Hartley D. M., Kusumoto Y., Fezoui Y., Condron M. M., Lomakin A., Benedek G. B., Selkoe D. J., Teplow D. B. (1999) J. Biol. Chem. 274: 25945–25945
Walsh D. M., Lomakin A., Benedek G. B., Condron M. M. and Teplow D. B. (1997) J. Biol. Chem. 272: 22364–22372
Westermark P. (2005) FEBS J. 272: 5942–5949
Zhang S., Iwata K., Lachenmann M. J., Peng J. W., Li S., Stimson E. R., Lu Y.-A., Felix A. M., Maggio J. E., Lee J. P. (2000) J. Struct. Biol. 130: 130–141
Acknowledgments
Arindam Banerjee thanks Department of Science and Technology, New Delhi, India for financial assistance [Grant No. SR/S5/OC-29/2003]. We thank the anonymous referees for critical comments that help to improve the work.
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Haldar, D., Banerjee, A. Intrinsic Amyloidogenic Behavior of Terminally Protected Alzheimer’s Aβ17–21 Peptide: Self-Aggregation and Amyloid-Like Fibril Formation. Int J Pept Res Ther 13, 439–446 (2007). https://doi.org/10.1007/s10989-006-9072-x
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DOI: https://doi.org/10.1007/s10989-006-9072-x