Conversion of Aβ42 into a Folded Soluble Native-like Protein using a Semi-random Library of Amphipathic Helices

Journal of Molecular Biology

Volumn 396, Issue 5, 2010, Pages 1284-1294

  Arslan, Pharhad Eli ^a   Mulligan, Vikram Khipple ^a   Ho, Sylvia ^a   Chakrabartty, Avijit ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Alzheimer's disease; Amyloid; Genetic screen; Protein aggregation; Semi random libraries

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; HYBRID PROTEIN; YELLOW FLUORESCENT PROTEIN; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); GREEN FLUORESCENT PROTEIN; PEPTIDE; PEPTIDE FRAGMENT; PEPTIDE LIBRARY; PRIMER DNA;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; MOLECULAR LIBRARY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SOLUBILIZATION; CHEMICAL STRUCTURE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; HUMAN; IN VITRO STUDY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PH; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; SOLUBILITY; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PROTEIN; BASE SEQUENCE; DNA PRIMERS; ESCHERICHIA COLI; GREEN FLUORESCENT PROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE LIBRARY; PEPTIDES; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

EID: 77649274599     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.12.019     Document Type: Article

References (25)

1. Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
2. Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416:535-539.
3. Gong Y., Chang L., Viola K.L., Lacor P.N., Lambert M.P., Finch C.E., et al. Alzheimer's disease-affected brain: presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl Acad. Sci. USA 2003, 100:10417-10422.
4. Schenk D., Barbour R., Dunn W., Gordon G., Grajeda H., Guido T., et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999, 400:173-177.
5. Citron M. Strategies for disease modification in Alzheimer's disease. Nat. Rev. Neurosci. 2004, 5:677-685.
6. Wolozin B. Cholesterol and the biology of Alzheimer's disease. Neuron 2004, 41:7-10.
7. Yan Q., Zhang J., Liu H., Babu-Khan S., Vassar R., Biere A.L., et al. Anti-inflammatory drug therapy alters β-amyloid processing and deposition in an animal model of Alzheimer's disease. J. Neurosci. 2003, 23:7504-7509.
8. Wong G.T., Manfra D., Poulet F.M., Zhang Q., Josien H., Bara T., et al. Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J. Biol. Chem. 2004, 279:12876-12882.
9. Sunde M., Serpell L.C., Bartlam M., Fraser P.E., Pepys M.B., Blake C.C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 1997, 273:729-739.
10. Wang J., Gulich S., Bradford C., Ramirez-Alvarado M., Regan L. A twisted four-sheeted model for an amyloid fibril. Structure 2005, 13:1279-1288.
11. Chakrabartty A., Baldwin R.L. Stability of α-helices. Adv. Protein Chem. 1995, 46:141-176.
12. Roy S., Hecht M.H. Cooperative thermal denaturation of proteins designed by binary patterning of polar and nonpolar amino acids. Biochemistry 2000, 39:4603-4607.
13. Wurth C., Guimard N.K., Hecht M.H. Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis. J. Mol. Biol. 2002, 319:1279-1290.
14. Kim W., Hecht M.H. Sequence determinants of enhanced amyloidogenicity of Alzheimer Aβ42 peptide relative to Aβ40. J. Biol. Chem. 2005, 280:35069-35076.
15. Nagai T., Ibata K., Park E.S., Kubota M., Mikoshiba K., Miyawaki A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20:87-90.
16. LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993, 2:404-410.
17. Guo M., Gorman P.M., Rico M., Chakrabartty A., Laurents D.V. Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides. FEBS Lett. 2005, 579:3574-3578.
18. Padmanabhan S., Laurents D.V., Fernandez A.M., Elias-Arnanz M., Ruiz-Sanz J., Mateo P.L., et al. Thermodynamic analysis of the structural stability of phage 434 Cro protein. Biochemistry 1999, 38:15536-15547.
19. Bateman D.A., Chakrabartty A. Two distinct conformations of Aβ aggregates on the surface of living PC12 cells. Biophys. J. 2009, 96:4260-4267.
20. Frost D., Gorman P.M., Yip C.M., Chakrabartty A. Co-incorporation of Aβ40 and Aβ42 to form mixed pre-fibrillar aggregates. Eur. J. Biochem. 2003, 270:654-663.
21. Gorman P.M., Yip C.M., Fraser P.E., Chakrabartty A. Alternate aggregation pathways of the Alzheimer β-amyloid peptide: Aβ association kinetics at endosomal pH. J. Mol. Biol. 2003, 325:743-757.
22. Arslan P.E., Chakrabartty A. Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method. Biochem. Cell Biol. 2009, 87:631-639.
23. DeMattos R.B., Bales K.R., Cummins D.J., Dodart J.C., Paul S.M., Holtzman D.M. Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc. Natl Acad. Sci. USA 2001, 98:8850-8855.
24. Gronwall C., Jonsson A., Lindstrom S., Gunneriusson E., Stahl S., Herne N. Selection and characterization of Affibody ligands binding to Alzheimer amyloid β peptides. J. Biotechnol. 2007, 128:162-183.
25. Hoyer W., Gronwall C., Jonsson A., Stahl S., Hard T. Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation. Proc. Natl Acad. Sci. USA 2008, 105:5099-5104.