Aggregation of Aβ(1-42) in the presence of short peptides: Conformational studies

Journal of Peptide Science

Volumn 14, Issue 6, 2008, Pages 731-741

  Laczkó, Ilona ^a   Vass, Elemér ^b   Soós, Katalin ^c   FüLöp, Livia ^c   Zarándi, Márta ^c   Penke, Botond ^c  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^c UNIVERSITY OF SZEGED   (Hungary)

Author keywords

amyloid; Alzheimer's disease; Circular dichroism; Fibrillogenesis; Infrared spectroscopy; Inhibitory pentapeptides

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; GLYCYLGLYCYLGLYCYLGLYCYLGLYCYLAMIDE; LEUCYLPROLYLPHENYLALANYLPHENYLALANYLASPARTYLHYDROXIDE; LEUCYLPROLYLTYROSYLPHENYLALANYLASPARTYLAMIDE; PENTAPEPTIDE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); PEPTIDE; PEPTIDE FRAGMENT;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONTROLLED STUDY; DRUG SCREENING; DRUG SYNTHESIS; INFRARED SPECTROSCOPY; INHIBITION KINETICS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; CHEMISTRY; SOLUBILITY;

AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN CONFORMATION; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 47249139209     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.990     Document Type: Article

References (41)

1. Clippingdale AB, Wade JD, Barrow CJ. The amyloid-beta peptide and its role in Alzheimer's disease. J. Pept. Sci. 2001; 7: 227-249.
2. Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006; 443: 774-779.
3. Bayer TA, Wirths O, Majtényi K, Hartmann T, Multhaup G, Beyreuther K, Czech C. Key factors in Alzheimer's disease: beta-amyloid precursor protein processing, metabolism and intraneuronal transport. Brain Pathol. 2001; 11: 1-11.
4. Dahlgren KN, Manelli AM, Stine WB, Baker LK, Krafft GA, LaDu MJ. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 2002; 277: 32046-32053.
5. Datki Z, Papp R. Zádori D, Soós K, Fülöp L, Juhász A, Laskay G, Hetényi C, Mihalik E, Zarádi M, Penke B. In vitro model of neurotoxicity of A beta 1-42 and neuroprotection by a pentapeptide: irreversible events during the first hour. Neurobiol. Dis. 2004; 17: 507-515.
6. Serpell LC. Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 2000; 1502: 16-30.
7. Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, Tycko R. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. U.S.A. 2002; 99: 16742-16747.
8. Rochet JC, Lansbury PT Jr. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 2000; 10: 60-68.
9. Deshpande A, Mina E, Glabe C, Busciglio J. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 2006; 26: 6011-6018.
10. Isaacs AM, Senn DB, Yuan ML, Shine JP, Yankner BA. Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium. J. Biol. Chem. 2006; 281: 27916-27923.
11. Butovsky O, Talpalar AE, Ben-Yaakov K, Schwartz M. Activation of microglia by aggregated beta-amyloid or lipopolysaccharide impairs MHC-II expression and renders them cytotoxic whereas IFN-gamma and IL-4 render them protective. Mol. Cell. Neurosci. 2005; 29: 381-393.
12. Rapoport M, Dawson HN, Binder LI, Vitek MP, Ferreira A. Tau is essential to beta-amyloid-induced neurotoxicity. Proc. Natl. Acad. Sci. U.S.A. 2002; 99: 6364-6369.
13. Szegedi V, Juhász G, Budai D, Penke B. Divergent effects of A beta 1-42 on ionotropic glutamate receptor-mediated responses in CA1 neurons in vivo. Brain Res. 2005; 1062: 120-126.
14. Chen GQ, Chen KS, Knox J, Inglis J, Bernard A, Martin SJ, Justice A, McConlogue L, Games D, Freedman SB, Morris RGM. A learning deficit related to age and beta-amyloid plaques in a mouse model of Alzheimer's disease. Nature 2000; 408: 975-979.
15. Oda T, Wals P, Osterburg HH, Johnson SA, Pasinetti GM, Morgan TE. Clusterin alters the aggregation of amyloid beta-peptide and forms slowly sedimentic A-beta complexes that cause oxidative stress. Exp. Neurol. 1995; 136: 22-31.
16. Lambert MP, Barlow AK, Chromy BA, Edwards C, Reed R, Liosatos M. Diffusible, nonfibrillar ligands derived from Abeta(1-42) are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 6448-6453.
17. Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Vasquez S, Vassilev PM. Amyloid beta-protein fibrillogenesis-structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 1999; 274: 25945-25952.
18. Cohen FE, Kelly JV. Therapeutic approaches to protein-misfolding diseases. Nature 2003; 426: 905-909.
19. Talaga P. Inhibitors of beta-amyloid aggregation: still an issue of structure and function? Drug Discov. Today: Therapeutic Strategies 2004; 1: 7-12.
20. Bieler S, Soto C. Beta-sheet breakers for Alzheimer's disease therapy. Curr. Drug Targets 2004; 5: 553-558.
21. Soto C, Sigurdsson EM, Morelli L, Kumar RA, Castano EM, Frangione B. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat. Med. 1998; 4: 822-826.
22. Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem. Biophys. Res. Commun. 1996; 226: 672-680.
23. Sato T, Kienlen-Campard P, Ahmed M, Liu W, Li HL, Elliott JI, Aimoto S, Constantinescu SN, Octave JN, Smith SO. Inhibitors of amyloid toxicity based on beta-sheet packing of A beta 40 and A beta 42. Biochemistry 2006; 45: 5503-5516.
24. Adessi C, Soto C. Beta-sheet breaker strategy for the treatment of Alzheimer's disease. Drug Dev. Res. 2002; 56: 184-193.
25. Sato C, Castano EM, Kumar RA, Beavis RC, Frangione B. Fibrillogenesis of synthetic amyloid-beta peptides is dependent on their initial secondary structure. Neurosci. Lett. 1995; 200: 105-108.
26. Zarándi M, Soós K, Fülöp L, Bozsó Z, Datki Z, Tóth GK, Penke B. Synthesis of Abeta(1-42) and its derivatives with improved efficiency. J. Pept. Sci. 2007; 13: 94-99.
27. Provencher W, Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 1981; 20: 33-37.
28. Jackson M, Mantsch HH. Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochim. Biophys. Acta 1992; 1118: 139-143.
29. Woody RW. Circular dichroism of peptides. In The Peptides, Vol. 7, Udenfriend S, Meienhofer J, Hruby VJ (eds). Academic Press: New York, 1985; 15-113.
30. Laczkó I, Hollósi M, Ürge L, Ugen KE, Weiner DB, Mantsch HH, Thurin J, Ötvös L Jr. Synthesis and conformational studies of N-glycosylated analogues of the HIV-1 principal neutralizing determinant. Biochemistry 1992; 31: 4282-4288.
31. Chou PY, Fasman GD. Empirical predictions of protein conformation. Annu. Rev. Biochem. 1978; 47: 251-276.
32. Gordon DJ, Sciarretta K, Meredith SC. Inhibition of beta-amyloid(40) fibrillogenesis and disassembly of beta-amyloid congeners containing N-methyl amino acids at alternate residues. Biochemistry 2001; 40: 8237-8245.
33. Zhang S, Rich A. Direct conversion of an oligopeptide from a beta-sheet to an alpha-helix: a model for amyloid formation. Proc. Natl. Acad. Sci U.S.A. 1997; 94: 23-28.
34. Manning MC, Illangasekare M, Woody RW. Circular dichroism studies of distorted alpha-helices, twisted beta-sheets and beta-turns. Biophys. Chem. 1988; 31: 77-86.
35. Surewicz KW, Mantsch HH. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 1988; 952: 115-130.
36. Zandomeneghi G, Krebs MRH, McCammon MG, Fandrich M. FTIR reveals structural differences between native beta-sheet and amyloid fibrils. Protein Sci. 2006; 13: 3314-3321.
37. Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA. pH-Dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 1991; 60: 1190-1201.
38. Kirkitadze MD, Condron MM, Teplow DB. Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. J. Mol. Biol. 2001; 312: 1103-1119.
39. Atwood CS, Moir RD, Huang X, Scarpa RC, Bacarra NM, Romano DM, Tanzi RE, Bush AI. Dramatic aggregation of Alzheimer A beta by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 1998; 273: 12817-12826.
40. Potempa LA, Kubak BM, Gewurz HJ. Effect of divalent metal-ions and pH upon the binding reactivity of human-serum amyloid P-component, a C-reactive protein homolog, for zymosan-preferential reactivity in the presence of copper and acidic pH. J. Biol. Chem. 1985; 260: 2142-2147.
41. Greenfield N, Fasman GD. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969; 8: 4108-4116.