Site-specific structure of Aβ(25-35) peptide: Isotope-assisted vibrational circular dichroism study

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 308-316

  Shanmugam, Ganesh ^a,b   Polavarapu, Prasad L ^a  

^a VANDERBILT UNIVERSITY   (United States)

^b CENTRAL LEATHER RESEARCH INSTITUTE   (India)

Author keywords

Amyloid; Beta sheet; Circular dichroism; Infrared; Isotope; Vibrational

Indexed keywords

ALANINE; AMIDE; AMYLOID BETA PROTEIN[25-35]; CARBON 13; CARBONYL DERIVATIVE; GLYCINE; ISOTOPE; LEUCINE;

ABSORPTION SPECTROSCOPY; ALZHEIMER DISEASE; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; ISOTOPE ASSISTED INFRARED VIBRATIONAL CIRCULAR DICHROISM; ISOTOPE DILUTION ASSAY; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; CIRCULAR DICHROISM; HUMANS; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84871716940     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.010     Document Type: Article

References (45)

1. C.M. Dobson Protein-misfolding diseases: getting out of shape Nature 418 2002 729 730
2. J. Kang, H.G. Lemaire, A.K. Unterbeck, J.M. Salbanum, K.H. Grezeschik, G. Multhaup, K. Beyreuther, and B. Muller-Hill The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 325 1987 733 736
3. C. Haass, E.H. Koo, A. Mellon, A.Y. Hunag, and D.J. Selkoe Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments Nature 357 1992 500
4. E.D. Eanes, and G.G. Glenner X-ray diffraction studies on amyloid filaments J. Histochem. Cytochem. 16 1968 673 677
5. D.A. Kirschner, C. Abraham, and D.J. Selkoe X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation Proc. Natl. Acad. Sci. U. S. A. 83 1986 503 507
6. T. Luhrs, C. Ritter, M. Adrian, D. Riek-Loher, B. Bohrmann, H. Dobeli, D. Schubert, and R. Riek 3D structure of Alzheimer's amyloid-β(1-42) fibrils Proc. Natl. Acad. Sci. U. S. A. 102 2005 17342 17347
7. A.T. Petkova, Y. Ishii, J.J. Balbach, O.N. Antzutkin, R.D. Leapman, F. Delaglio, and R. Tycko A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR Proc. Natl. Acad. Sci. U. S. A. 99 2002 16742 16747
8. K.J. Halverson, I. Sucholeiki, T.T. Ashburn, and P.T. Lansbury Location of β-sheet-forming sequences in amyloid proteins by FTIR J. Am. Chem. Soc. 113 1991 6701 6703
9. P.T. Lansbury, P.R. Costa, J.M. Griffiths, E.J. Simon, M. Auger, K.J. Halverson, D.A. Kocisko, Z.S. Hendsch, T.T. Ashburn, R.G.S. Spencer, B. Tidor, and R.G. Griffin Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide Nat. Struct. Biol. 2 1995 990 998
10. J.J. Balbach, Y. Ishii, O.N. Antzutkin, R.D. Leapman, N.W. Rizzo, F. Dyda, J. Reed, and R. Tycko Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR Biochemistry 39 2000 13748 13759
11. A.T. Petkova, G. Buntkowsky, F. Dyda, R.D. Leapman, E.-M. Yau, and R. Tycko Solid state NMR reveals a pH-dependent antiparallel β-sheet registry in fibrils formed by a β-amyloid peptide J. Mol. Biol. 335 2004 247 260
12. T.L.S. Benzinger, D.M. Gregory, T.S. Burkoth, H. Miller-Auer, D.G. Lynn, R.E. Botto, and S.C. Meredith Propagating structure of Alzheimer's β-amyloid (10-35) is parallel β-sheet with residues in exact register Proc. Natl. Acad. Sci. U. S. A. 95 1998 13407 13412
13. O.N. Antzutkin, J.J. Balbach, R.D. Leapman, N.W. Rizzo, J. Reed, and R. Tycko Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils Proc. Natl. Acad. Sci. U. S. A. 97 2000 13045 13050
14. J.J. Balbach, A.T. Petkova, N.A. Oyler, O.N. Antzutkin, D.J. Gordon, S.C. Meredith, and R. Tycko Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance Biophys. J. 83 2002 1205 1216
15. M. Török, S. Milton, R. Kayed, P. Wu, T. McIntire, C.G. Glabe, and R. Langen Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling J. Biol. Chem. 277 2002 40810 40815
16. G. Forloni, R. Chiesa, S. Smiroldo, L. Verga, M. Salmona, F. Tagliavini, and N. Angeretti Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35 Neuroreport 4 1993 523 526
17. B.A. Yankner, L.K. Duffy, and D.A. Kirschner Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides Science 250 1990 279 282
18. N.W. Kowall, M.F. Beal, J. Busciglio, L.K. Duffy, and B.A. Yankner An in vivo model for the neurodegenerative effects of β amyloid and protection by substance P Proc. Natl. Acad. Sci. U. S. A. 88 1991 7247 7251
19. E. Terzi, G. Holzemann, and J. Seelig Alzheimer β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes Biochemistry 33 1994 7434 7441
20. T. Kohno, K. Kobayashi, T. Maeda, K. Sato, and A. Takashima Three-dimensional structures of the amyloid β-peptide (25-35) in membrane-mimicking environment Biochemistry 35 1996 16094 16104
21. M. Del Mar Martinez-Senac, J. Villalain, and J.C. Gomez-Fernandez Structure of the Alzheimer β-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles Eur. J. Biochem. 265 1999 744 753
22. A.M. D'Ursi, M.R. Armenante, R. Guerrini, S. Salvadori, G. Sorrentino, and D. Picone Solution structure of amyloid β-peptide (25-35) in different media J. Med. Chem. 47 2004 4231 4238
23. G. Shanmugam, and P.L. Polavarapu Structure of Aβ(25-35) peptide in different environments Biophys. J. 87 2004 622 630
24. J. He, A.G. Petrovic, S.V. Dzyuba, N. Berova, K. Nakanishi, and P.L. Polavarapu Spectroscopic investigation of Ginkgo biloba terpene trilactones and their interaction with amyloid peptide Aβ(25-35) Spectrochim. Acta A Mol. Biomol. Spectrosc. 335 2008 712 722
25. J.H. Ippel, A. Olofsson, J. Schleucher, E. Lundgren, and S.S. Wijmenga Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 99 2002 8648 8653
26. G. Shanmugam, and P.L. Polavarapu Isotope-assisted vibrational circular dichroism investigations of amyloid β peptide fragment, Aβ(16-22) J. Struct. Biol. 176 2011 212 219
27. S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38 1986 181 364
28. W.C. Chan, and P.D. White Fmoc Solid Phase Peptide Synthesis. A Practical Approach 2000 Oxford University Press Oxford, UK
29. L.A. Nafie Dual polarization modulation: a real-time, spectral-multiplex separation of circular dichroism from linear birefringence spectral intensities Appl. Spectrosc. 54 2000 1634 1645
30. 13C isotope labeling of hydrophobic peptides. Origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures J. Am. Chem. Soc. 122 2000 677 683
31. 13C isotopically labeled peptide β-sheets comes from extended, multiple-stranded structures. An ab initio study J. Am. Chem. Soc. 123 2001 6142 6150
32. S.M. Decatur Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy Acc. Chem. Res. 39 2006 169 175
33. M.R. Nilsson Techniques to study amyloid fibril formation in vitro Methods 34 2004 151 160
34. J. Kubelka, and T.A. Keiderling Differentiation of β-sheet-forming structures: ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets J. Am. Chem. Soc. 123 2001 12048 12058
35. D. Kurouski, R.A. Lombardi, R.K. Dukor, I.K. Lednev, and L.A. Nafie Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism Chem. Commun. 46 2010 7154 7156
36. T.J. Measey, K.B. Smith, S.M. Decatur, L. Zhao, G. Yang, and R. Schweitzer-Stenner Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal J. Am. Chem. Soc. 131 2009 18218 18219
37. A.C. Sen, and T.A. Keiderling Vibrational circular-dichroism of polypeptides. III. Film studies of several α-helical and β-sheet polypeptides Biopolymers 23 1984 1533 1545
38. T.J. Measey, and R. Schweitzer-Stenner Vibrational circular dichroism as a probe of fibrillogenesis: the origin of the anomalous intensity enhancement of amyloid-like fibrils J. Am. Chem. Soc. 133 2011 1066 1076
39. R. Schweitzer-Stenner, and Simulated IR Isotropic and anisotropic Raman, and vibrational circular dichroism amide I band profiles of stacked β-sheets J. Phys. Chem. B 116 2012 4141 4153
40. V.P. Gupta, and T.A. Keiderling Vibrational CD of the amide-II band in some model polypeptides and proteins Biopolymers 32 1992 239 248
41. P. Bour, J. Kubelka, and T.A. Keiderling Simulations of oligopeptide vibrational CD: effects of isotopic labeling Biopolymers 53 2000 380 395
42. 13C isotopic labeling on infrared spectra J. Phys. Chem. B 205 2005 5348 5357
43. R. Huang, J. Kubelka, W. Barber-Armstrong, R.A.G.D. Silva, S.M. Decatur, and T.A. Keiderling Nature of vibrational coupling in helical peptides: an isotopic labeling study J. Am. Chem. Soc. 126 2004 2346 2354
44. G. Wei, A.I. Jewettb, and J.-E. Shea Structural diversity of dimers of the Alzheimer amyloid-β(25-35) peptide and polymorphism of the resulting fibrils Phys. Chem. Chem. Phys. 12 2010 3622 3629
45. B. Ma, and R. Nussinov The stability of monomeric intermediates controls amyloid formation: Aβ25-35 and its N27Q mutant Biophys. J. 90 2006 3365 3374