Circular dichroism and aggregation studies of amyloid β (11-28) fragment and its variants

Acta Biochimica Polonica

Volumn 52, Issue 2, 2005, Pages 425-431

  Juszczyk, Paulina ^a   Kołodziejczyk, Aleksandra S ^a   Grzonka, Zbigniew ^a  

^a UNIVERSITY OF GDA SK   (Poland)

Author keywords

Aggregation studies; Alzheimer's disease; Amyloid ; Circular dichroism (CD); Secondary structure studies; Thioflavine T assay

Indexed keywords

EID: 23644448737     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2005_3455     Document Type: Article

References (38)

1. Atherton E, Sheppard RC (1989) Solid Phase Peptide Synthesis: a Practical Approach. Oxford University Press, Oxford.
2. Buck M (1998) Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q Rev Biophys 31: 297-355.
3. Castano EM, Ghiso J, Prelli F, Gorevic PD, Migheli A, Frangione B (1986) In vitro formation of amyloid fibril from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein. Biochem Biophys Res Commun 141: 782-790.
4. Fezoui Y, Teplow DB (2002) Kinetic studies of amyloid β-protein fibril assembly. J Biol Chem 277: 36948-36954.
5. Flood JF, Morey JE, Roberts E (1994) An amyloid β-protein fragment, Aβ (12-28), equipotently impairs post-training memory processing when injected into different limbic structures. Brain Res 663: 271-276.
6. Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA (1991) pH-Dependent structural transition of Alzheimer amyloid peptides. Biophys J 60: 1190-1201.
7. Grabowski TJ, Cho HS, Vonsattel JP, Rebeck GW, Greenberg SM (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann Neurol 49: 697-705.
8. Hendriks L, van Duijn CM, Cruts M, Van Hul W, van Harskamp F, Warren A, McInnis MG, Antonarakis SE, Martin JJ (1992) Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta amyloid precursor protein gene. Nat Genet 1: 218-221.
9. Huang TH, Fraser PE, Chakrabartty A (1997) Fibrillogenesis of Alzheimer Ab peptides studied by fluorescence energy transfer. J Mol Biol 26: 214-224.
10. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
11. Kirkitadze MD., Condron MM., Teplow DB (2001) Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis, J Mol Biol 312: 1103-1119.
12. Klein WL, Krafft GA, Finch CE (2001) Targeting small Aβ oligomers: the solution to an Alzheimer's conundrum. Trends Neurosci 24: 219-224.
13. LeVine H III (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution, Protein Sci 2: 404-410.
14. Levy E, Carman MD, Fernandez-Madrid IJ, Power MD, Lieberburg, van Duinan SG, Bots AM, Luyendijk W, Frangione B (1990) Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248: 1124-1126.
15. Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red. Proc Nat Acad Sci USA 91: 12243-12247.
16. Melchor JP, McVoy L, Van Nostrand WE (2000) Charge alteration of E22 enhance the pathogenic properties of the amyloid beta-protein. J Neurochem 74: 2209-2212.
17. Miravalle L, Tokudo T, Chiavle R, Giaccone G, Bugiani C, Tagliavini F, Frangione B, Ghiso J (2000) Substitutions at codon 22 of Alzheimer's Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J Biol Chem 275: 271110-271116.
18. Monro OR, Mackic JB, Yamada S, Segal MB, Ghiso J, Maurer C, Calero M, Frangione B, Zlokovic BV (2002) Substitution at codon 22 reduces clearance of Alzheimer's amyloid-beta peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood. Neurobiol Aging 23: 405-412.
19. Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T (2003) Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy. J Biol Chem 278: 46179-46187.
20. Nilsberth C, Westlind-Danielsson A, Eckman CB, Condron MM, Axelman K, Forsell C, Steenh C, et al. (2001) The Arctic APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nat Neurosci 4: 887-893.
21. Paivio A, Jarvet J, Graslund A, Lannfelt L, Westlind-Danielsson A (2004) Unique physicochemical profile of β-amyloid peptide variant Aβ 1-40 E22G protofibrils: conceivable neuropathogenn in Arctic mutant carriers. J Mol Biol 339: 145-159.
22. Rabanal F, Tussel JM, Sastre L, Quintero MR, Cruz M, Grillo D, Pons M, Albericio F, Serratosa J, Giralt E (2002) Structural, kinetic and cytotoxicity aspects of 12-28 β-amyloid protein fragment: a reappraisal. J Peptide Sci 8: 578-588.
23. Rossi G, Macchi G, Porro M, Giaccone G, Bugiani M, Scarpini E, Scarlato G, Molini GE, Sasanelli F, Bugiani O, Tagliavini F (1998) Fatal familial insomnia: genetic, neuropathologic and biochemical study of a patient from a new Italian kindred. Neurology 50: 688-692.
24. 16-22 peptide assembly. Structure 12: 1-20.
25. Selkoe DJ (1993) Physiological production of the β-amyloid protein and the machanism of Alzheimer's disease. Trends Neurosci 16: 403-409.
26. Selkoe DJ (2001) Alzheimer's disease: genes, proteins and therapy. Physiol Rev 81: 741-766.
27. Serpell LC (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 1502: 16-30.
28. Soto C (1999) Alzheimer's and prion disease as disorders of protein conformation: implication for the design of novel therapeutic approaches. J Mol Med 77: 412-18.
29. Sreerama N, Woody R (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of Contin, Selcon and CDSSTR methods with an expanded reference set. Anal Biochem 287: 252-260.
30. Stenh C, Nilsberth C, Hammarback J, Engvall B, Naslund J, Lannfelt L (2002) The Arctic mutations interferes with processing of the amyloid precursor protein. Neuroreport 13: 1857-1860.
31. Stine WB, Dahlgren KN, Krafft GA, LaDu MJ (2003) In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem 278: 11612-11622.
32. Tsubuki S, Takaki Y, Saido TC (2003) Dutch, Flemish, Italian and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation. Lancet 361: 1957-1958.
33. Van Nostrand WE, Metchor JP, Cho HS, Greenberg SM, Rebeck GW (2001) Pathogenic effects of D23N Iowa mutant amyloid β-protein. J Biol Chem 276: 32860-32866.
34. Vieira EP, Hermel H, Mohwald M (2003) Change and stabilization of the amyloid-β (1-40) secondary structure by fluorocompounds. Biochim Biophys Acta 1645: 6-14.
35. Walsh DM, Klyubin I, Foldeeva JV, Rowan MJ, Selkoe DJ (2002) Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition. Biochem Soc Trans 30: 552-557.
36. Wang Z, Natte R, Berliner JA, van Duinen SG, Vinters M (2000) Toxicity of Dutch (E22Q) nad Flemish (A21G) mutant amyloid beta proteins to human cerebral microvessel and aortic smooth muscle cells. Stroke 31: 534-538.
37. Yoshiike Y, Chui D, Akagi T, Tanaka N, Takashima A (2003) Specific compositions of amyloid-β peptides as the determinant of toxic β-aggregation. J Biol Chem 278: 23648-23655.
38. Zagorski M, Barrow CJ (1992) NMR studies of amyloid β-peptides: proton assignments, secondary structure and machanism of an α-helix → β-sheet conversion for a homologous, 28-residue N-terminal fragment. Biochemistry 31: 5621-5631.