Methyl dynamics of the amyloid-β peptides Aβ40 and Aβ42

Biochemical and Biophysical Research Communications

Volumn 362, Issue 2, 2007, Pages 410-414

  Yan, Yilin ^a   Liu, Jiajing ^a   McCallum, Scott A ^a   Yang, Daiwen ^b   Wang, Chunyu ^a  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

A ; Alzheimer's disease; Methyl dynamics; NMR spectroscopy; Protein dynamics

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; METHYL GROUP;

ARTICLE; CLUSTER ANALYSIS; DYNAMICS; HYDROPHOBICITY; INFORMATION PROCESSING; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

AMYLOID BETA-PROTEIN; HYDROPHOBICITY; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 34548324280     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.07.198     Document Type: Article

References (24)

1. Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81 (2001) 741-766
2. Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E., and Ball M.J. β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 90 (1993) 10836-10840
3. Jarrett J.T., Berger E.P., and Lansbury Jr. P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
4. Jarrett J.T., Berger E.P., and Lansbury Jr. P.T. The C-terminus of the beta protein is critical in amyloidogenesis. Ann. NY Acad. Sci. 695 (1993) 144-148
5. El-Agnaf O.M., Mahil D.S., Patel B.P., and Austen B.M. Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease. Biochem. Biophys. Res. Commun. 273 (2000) 1003-1007
6. Bitan G., Kirkitadze M.D., Lomakin A., Vollers S.S., Benedek G.B., and Teplow D.B. Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. USA 100 (2003) 330-335
7. Bitan G., Vollers S.S., and Teplow D.B. Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization. J. Biol. Chem. 278 (2003) 34882-34889
8. Zhang Y., McLaughlin R., Goodyer C., and LeBlanc A. Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156 (2002) 519-529
9. Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
10. Yan Y., and Wang C. Abeta42 is More Rigid than Abeta40 at the C Terminus: Implications for Abeta Aggregation and Toxicity. J. Mol. Biol. 364 (2006) 853-862
11. Lim K.H., Collver H.H., Le Y.T., Nagchowdhuri P., and Kenney J.M. Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Biochem. Biophys. Res. Commun. 353 (2007) 443-449
12. Riek R., Guntert P., Dobeli H., Wipf B., and Wuthrich K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer's peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox). Eur. J. Biochem. 268 (2001) 5930-5936
13. Zheng Y., and Yang D. Measurement of dipolar cross-correlation in methylene groups in uniformly 13C-, 15N-labeled proteins. J. Biomol. NMR 28 (2004) 103-116
14. Houben K., and Boelens R. Side chain dynamics monitored by 13C-13C cross-relaxation. J. Biomol. NMR 29 (2004) 151-166
15. Lee A.L., Kinnear S.A., and Wand A.J. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat. Struct. Biol. 7 (2000) 72-77
16. Ishima R., and Torchia D.A. Protein dynamics from NMR. Nat. Struct. Biol. 7 (2000) 740-743
17. Kim W., and Hecht M.H. Sequence determinants of enhanced amyloidogenicity of Alzheimer's A{beta}42 peptide relative to A{beta}40. J. Biol. Chem. 280 (2005) 35069-35076
18. Hou L., Shao H., Zhang Y., Li H., Menon N.K., Neuhaus E.B., Brewer J.M., Byeon I.J., Ray D.G., Vitek M.P., Iwashita T., Makula R.A., Przybyla A.B., and Zagorski M.G. Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc. 126 (2004) 1992-2005
19. Zhang X., Sui X., and Yang D. Probing methyl dynamics from 13C autocorrelated and cross-correlated relaxation. J. Am. Chem. Soc. 128 (2006) 5073-5081
20. Sgourakis N.G., Yan Y., McCallum S.A., Wang C., and Garcia A.E. The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD/NMR study. J. Mol. Biol. 368 (2007) 1448-1457
21. Choy W.Y., Shortle D., and Kay L.E. Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta. J. Am. Chem. Soc. 125 (2003) 1748-1758
22. Soto C., Castano E.M., Frangione B., and Inestrosa N.C. The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J. Biol. Chem. 270 (1995) 3063-3067
23. Christopeit T., Hortschansky P., Schroeckh V., Guhrs K., Zandomeneghi G., and Fandrich M. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's beta-amyloid peptide. Protein Sci. 14 (2005) 2125-2131
24. Chen Y.R., and Glabe C.G. Distinct early folding and aggregation properties of Alzheimer's amyloid-beta peptides Abeta40 and Abeta42: stable trimer or tetramer formation by Abeta42. J. Biol. Chem. 281 (2006) 24414-24422