Active site environment of heme-bound amyloid β peptide associated with Alzheimers Disease

Journal of the American Chemical Society

Volumn 133, Issue 1, 2011, Pages 81-87

  Pramanik, Debajyoti ^a   Dey, Somdatta Ghosh ^a  

^a DEPARTMENT OF MATERIALS SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALZHEIMERS DISEASE; AXIAL LIGAND; BRAIN CELLS; H-BONDS; HEME BINDING; IRON HOMEOSTASIS; IRON REGULATORY PROTEINS; MITOCHONDRIAL COMPLEX; NATURALLY OCCURRING; PEPTIDE COMPLEX; PEROXIDASE ACTIVITIES; PHYSIOLOGICAL CONDITION; SPIN STATE; WILD TYPES;

BINDING SITES; BIOCHEMISTRY; COMPLEXATION; GLYCOPROTEINS; IRON COMPOUNDS; LIGANDS; MAMMALS; PEPTIDES; SPHERES; SPIN DYNAMICS;

PORPHYRINS;

AMYLOID BETA PROTEIN; ARGININE; HEME; HISTIDINE; PEROXIDASE; REGULATOR PROTEIN;

ABSORPTION SPECTROSCOPY; ALZHEIMER DISEASE; ARTICLE; BINDING SITE; BIOSYNTHESIS; BRAIN CELL; COMPLEX FORMATION; DISEASE ASSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HOMEOSTASIS; HUMAN; LIGAND BINDING; OXIDATIVE STRESS; PH;

ABSORPTION; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; CATALASE; CATALYTIC DOMAIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HUMANS; HYDROGEN-ION CONCENTRATION; LIGANDS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PEROXIDASE;

EID: 78650974416     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1084578     Document Type: Article

References (41)

1. Rauk, A. Chem. Soc. Rev. 2009, 38, 2698
2. Maurer, I., Zierz, S., and Moller, H. J. Neurobiol. Aging 2000, 21, 455
3. Blass, J. P. J. Neurosci. Res. 2001, 66, 851
4. Nelson, P. G. Curr. Alzheimer Res. 2005, 2, 497
5. Hardy, J. and Selkoe, D. J. Science 2002, 297, 353
6. Glenner, G. G. and Wong, C. W. Biochem. Biophys. Res. Commun. 1984, 120, 885
7. Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., and Beyreuther, K. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 4245
8. Huang, X., Atwood, C. S., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J., Moir, R. D., Tanzi, R. E., and Bush, A. I. Biochemistry 1999, 38, 7609
9. Opazo, C., Huangs, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., and Bush, A. I. J. Biol. Chem. 2002, 277, 40302
10. Bush, A. I. Trends Neurosci. 2003, 26, 207
11. Guilloreau, L., Combalbert, S., Sournia-Saquet, A., Mazarguil, H., and Faller, P. ChemBioChem 2007, 8, 1317
12. Smith, D. P., Smith, D. G., Curtain, C. C., Boas, J. F., Pilbrow, J. R., Ciccotosto, G. D., Lau, T.-L., Tew, D. J., Perez, K., Wade, J. D., Bush, A. I., Drew, S. Z., Separovic, F., Master, C. L., Cappai, R., and Barnham, K. J. J. Biol. Chem. 2006, 281, 15145
13. Curtain, C. C., Ali, F., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K., Barrow, C. J., Masters, C. L., Bush, A. I., and Barnham, K. J. J. Biol. Chem. 2001, 276, 20466
14. Bush, A. I. Alzheimer Dis. Assoc. Disord. 2003, 17, 147
15. Lynch, T., Cherny, R. A., and Bush, A. I. Exp. Gerontol. 2000, 35, 445
16. Markesbury, W. R. and Carney, J. M. Brain Pathol. 1999, 9, 133
17. Syme, C. D., Nadal, R. C., Rigby, S. E. J., and Viles, J. H. J. Biol. Chem. 2004, 279, 18169
18. Karr, J. W., Akintoye, H., Kaupp, L. J., and Szalai, V. A. Biochemistry 2005, 44, 5478
19. Karr, J. W. and Szalai, V. A. J. Am. Chem. Soc. 2007, 129, 3796
20. Atamna, H. and Frey II, W. H. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 11153
21. Atamna, H., Liu, J., and Ames, B. N. J. Biol. Chem. 2001, 276, 48410
22. Kimpara, T., Takeda, A., Yamguchi, T., Arai, H., Okita, N., Takase, S., Sasaki, H., and Itoyama, Y. Neurobiol. Aging 2000, 21, 551
23. Schipper, H. M., Cisse, S., and Stopa, E. G. Ann. Neurol. 1995, 37, 758
24. Steffens, G. C., Biewald, R., and Buse, G. Eur. J. Biochem. 1987, 164, 295
25. Atamna, H. and Boyle, K. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 3381
26. Atamna, H., Frey, W. H., II, and Ko, N. Arch. Biochem. Biophys. 2009, 487, 59
27. Holland, V. R., Saunders, B. C., Rose, F. L., and Walpole, A. L. Tetrahedron 1974, 30, 3299
28. Beers, R. F., Jr. and Sizer, I. W. Science 1954, 120, 32
29. Note that due to the low resolution of the data at 77 K we cannot accurately determine the E / D parameter. However, the data show changes that can be used for diagnostic purposes.
30. Rotilio, G., Calabrese, L., GIacometti, G. M., and Brunori, M. Biochim. Biophys. Acta 1971, 236, 234
31. Peisach, J., Blumberg, W. E., Wittenberg, B. A., Wittenberg, J. B., and Kampa, L. Proc. Natl. Acad. Sci. U.S.A. 1969, 63, 934
32. Blumberg, W. E., Peisach, J., Wittenberg, B. A., and Wittenberg, J. B. J. Biol. Chem. 1968, 243, 1854
33. perp = 6 EPR excited state.
34. Rodriguez -Lopez, J. N., Smith, A. T., and Thornley, R. N. F. J. BIol. Chem. 1996, 271, 4023
35. Henriksen, A., Smith, A. T., and Gajhede, M. J. Biol. Chem. 1999, 274, 35005
36. Murthy, M. R. N., Reid, T. J., III, Sicignano, A., Tanaka, N., and Rossmann, M. G. J. Mol. Biol. 1981, 152, 465
37. Note that EPR data on the high- and low-pH heme-Aβ complexes show increased rhombicity in the low-pH form.
38. Teale, F. W. J. Biochim. Biophys. Acta 1959, 35, 543
39. Redaelli, C., Monzani, E., Santagostini, L., Casella, L., Sanangalantoni, A. M., Pierattelli, R., and Banci, L. ChemBioChem 2002, 3, 226
40. Ikeda-Saito, M., Horill, H., Andersson, L. A., Prince, R. C., Pickering, I. J., George, G. H., Sanders, C. R., Lutz, R. S., McKelvey, E. J., and Mattera, R. J. Biol. Chem. 1992, 267, 22843
41. Vaughan, D. W. and Peters, A. J. Neuropathol. Exp. Neurol. 1981, 40, 472