The interaction of β-amyloid protein fragment (12-28) with lipid environments

Protein Science

Volumn 6, Issue 3, 1997, Pages 666-675

  Fletcher, Terry G ^a   Keire, David A ^a  

^a CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

Author keywords

Alzheimer's disease; amyloid; beta amyloid protein; dodecylphosphocholine; micelles; NMR; sodium dodecylsulfate

Indexed keywords

AMYLOID BETA PROTEIN; DODECYL SULFATE SODIUM; LIPID; PROTEIN;

ALZHEIMER DISEASE; ARTICLE; IONIC STRENGTH; MICELLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

EID: 0030983767     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060316     Document Type: Article

References (47)

1. Barrow CJ, Yasuda A, Kenny PTM, Zagorski MG. 1992. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectra. J Mol Biol 225:1075-1093.
2. Bothner-By AA, Stephens RL, Lee J-M, Warren CD, Jeanloz RW. 1984. Structure determination of a tetrasacchride: Transient nuclear overhauser effects in the rotating frame. J Amer Chem Soc 106:811-813.
3. Braunschweiler L, Ernst RR. 1983. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J Magn Res 53:521-528.
4. Brunger AT. 1992. X-PLOR: Version 3.1, a system for X-ray crystallography and NMR. New Haven, Connecticut: Yale University Press.
5. Chen Y-H, Yang JT, Chau KH. 1974. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochem 13:3350-3359.
6. Clements A, Allsop D, Walsh DM, Williams CH. 1996. Aggregation and metal-binding properties of mutant forms of the amyloid aβ peptide of Alzheimer's disease. J Neurochem 66:740-747.
7. Esler WP, Stimson ER, Ghilardi JR, Lu Y, Felix AM, Vinters HV, Mantyh PW, Lee JP, Maggio JE. 1996. Point substitution in the central hydrophobic cluster of human β-amyloid congener disrupts peptide folding and abolishes plaque competence. Biochem 35:13914-13921.
8. Evans KC, Berger EP, Cho C-G, Weisgraber KH, Lansbury PTJ. 1995. Apolipoprotein E is a kinetic but not thermodynamic inhibitor of amyloid formation: implications for the pathogenisis and treatment of Alzheimer's disease. Proc Natl Acad Sci USA 92:763-767.
9. Flood JF, Morely JE, Roberts E. 1991. Amnestic effects in mice of four synthetic peptide homologous to amyloid β-protein in patients with Alzheimer's disease. Proc Natl Acad Sci USA 88:3363-3366.
10. Flood JF, Morley JE, Roberts E. 1994. An amyloid β-protein fragment, Aβ[12-28], equipotently impairs post-training memory processing when injected into different limbic system structures. Brain Res 663:271-276.
11. Fraser PE, Levesque L, McLachlan DR. 1994. Alzheimer Aβ amyloid forms an inhibitory neuronal substrate. J Neurochem 62:1227-1230.
12. Fraser PE, Nguyen JT, Surewiez WK, Kirschner DA. 1991. pH Dependent structural transitions of alzheimer amyloid peptides. Biophys J 60:1190-1201.
13. Glenner GG, Wong CW. 1984. Alzheimer's disease: Initial report of the purification and characteristics of novel cerebrovascular amyloid protein. Biochem Biophys Res Comm 122:885-890.
14. Hayter JB, Penfold J. 1981. Self-consistent structural and dynamic study of concentrated micelle solutions. J Chem Soc Faraday Trans 77:1851-1863.
15. Hendriks L, van Duijin CM, Cras P, Cruts M, van Hul W, van Harskamp F, Warren A, McInnis MG, Antonarakis SE, Martin JJ, Hofman A, van Broeckhoven C. 1992. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β-amyloid precursor protein gene. Nature Genet 1:218-221.
16. Hilbich C, Kister-Woike B, Reed J, Masters CL, Beyreuther K. 1991. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J Mol Biol 218:149-163.
17. Hilbich C, Kister-Woike B, Reed S, Masters CL, Beyreuther K. 1992. Substitution of hydrophobic amino acids reduces the amyloidicity of Alzheimer's disease βA4 peptides. J Mol Biol 228:460-473.
18. Iversen LL, Mortishire-Smith RJ, Pollack SJ, Shearman MS. 1995. The toxicity in vitro of β-amyloid protein. Biochem J 311:1-16.
19. Jeener J, Meier BH, Bachmann P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71:4546-4553.
20. Keire DA, Fletcher TG. 1996. The conformation of substance P in lipid environments. Biophys J 70:1716-1727.
21. Kosik K, Coleman P, eds. 1992. Is β-amyloid neurotoxic? Neurobiol Aging 13:535-627.
22. Lauterwein J, Bosch C, Brown LR, Wuthrich K. 1979. Physiochemical studies of the protein-lipid interactions in mellittin-containing micelles. Biochim Biophys Acta 556:244-264.
23. 1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence. Biochem 34:5191-5200.
24. Levy E, Carman MD, Fernandez-Madrid IJ, Power MD, Lieberberg I, van Duinen SG, Bots GTAM, Luyendijk W, Frangione B. 1990. Mutation of the Alzhiemer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248:1124-1126.
25. Masters CL, Simms G, Weinmann NA, Multhaup G, McDonald BL, Beyreuther K. 1985. Amyloid plaque protein in Alzheimer's disease and Down's syndrome. Proc Natl Sci Acad USA 82:4245-4249.
26. 2+ homeostasis in Alzheimer's disease. Trends Neurosci 16:409-414.
27. Mattson MP, Rydel RE. 1992. β-Amyloid Precursor Protein and Alzheimer's disease: The peptide plot thickens. Neurobiol Aging 13:617-621.
28. Naslund J, Schierhorn A, Hellman U, Lannfelt L, Roses AD, Tjernberg LO, Silberring J, Gandy SE, Winblad B, Greengard P, Norsted C, Terenius L. 1994. Relative abundance of Alzheimer's Aβ amyloid peptide variants in Alzheimer's disease and normal aging. Proc Natl Acad Sci USA 91:8378-8382.
29. Nigles M, Clore GM, Gronenbom AM. 1988. Determination of three-dimensional structures of proteins from the interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett 2:317-324.
30. Nitsch RM, Blusztajn JK, Pittas AG, Slack BE, Growdon JH, Wurtman RJ. 1992. Evidence for a membrane defect in Alzheimer disease brain. Proc Natl Acad Sci USA 89:1671-1675.
31. O'Neil JD, Sykes BD. 1989. NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide. Biochemistry 28:699-707.
32. 1H NMR spectra of proteins via double quantum filtering. Biochem Biophys Res Comm 117:419-485.
33. Rodgers W, Glaser M. 1993. Distribution of proteins and lipids in the erythrocyte membrane. Biochem 32:12591-12598.
34. Sargent DF, Schwyzer R. 1986. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc Natl Acad Sci USA 85:5774-5778.
35. States DJ, Haberkorn RA, Ruben DJ. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Res 48:286-292.
36. Svennerholm L, Gottfries C. 1994. Membrane lipids, selectively diminished in Alzheimer's brains, suggest synapse loss as a primary event in early-onset form (Type I) and demylination in late-onset form (Type II). J Neurochem 62:1039-1047.
37. Talafous J, Marcinowski KJ, Klopman G, Zagorski MG. 1994. Solution structure of residues 1-28 of the amyloid β-peptide. Biochem 33:7788-7796.
38. Terzi E, Holzmann G, Seelig J. 1995. Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J Mol Biol 252:633-642.
39. van den Hooven HW, Spronk CAEM, van de Kamp M, Konings RNH, Hilbers CW, van de Ven FJ. 1996. Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulfate. Eur J Biochem 235:394-403.
40. Wood JW, Wetzel R, Martin JD, Hurle MR. 1995. Prolines and amyloidogenicity of Alzheimer's peptide β/A4. Biochem 34:724-730.
41. Woody RW. 1995. Circular Dichroism. In: Methods in Enzymology. New York: Academic Press. 246:34-71.
42. Woolley GA, Deber CM. 1987. Peptides in membranes: Lipid-induced secondary structure of substance P. Biopolymers 26:S109-S121.
43. Wright PE, Dyson HJ, Lemer RA. 1988. Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding. Biochem 27:7167-7175.
44. Wuthrich K. 1986. NMR of Proteins and nucleic acids. New York: John Wiley and Sons.
45. Wuthrich K, Billeter M, Braun W. 1983. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurement of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J Mol Biol 169:949-961.
46. Yang L, Glaser M. 1995. Membrane domains containing phosphatidylserine and substrate can be important for activation of protein kinase C. Biochem 34:1500-1506.
47. Zagorski MG, Barrow CJ. 1992. NMR studies of amyloid β-peptides: Proton assignments, secondary structure, and mechanism of an α-helix to β-sheet conversion for a homologous, 28-residue, N-terminal fragment. Biochem 31:5621-5631.