Identification of distinct physiochemical properties of toxic prefibrillar species formed by Aβ peptide variants

Biochemical and Biophysical Research Communications

Volumn 420, Issue 4, 2012, Pages 895-900

  Göransson, Anna Lena ^a   Nilsson, Peter K R ^a   Kågedal, Katarina ^a   Brorsson, Ann Christin ^a  

^a LINKÖPING UNIVERSITY   (Sweden)

Author keywords

Alzheimer's disease; Amyloid peptide; Cell toxicity; Fluorescence spectroscopy; Protein aggregation

Indexed keywords

8 ANILINO 1 NAPTHALENESULFONATE; AMYLOID BETA PROTEIN; FLUORESCENT DYE; PENTAMER FORMYL THIOPHENE ACETIC ACID; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; CYTOTOXICITY; DROSOPHILA; FLUORESCENCE SPECTROSCOPY; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; IN VITRO STUDY; IN VIVO STUDY; NERVE DEGENERATION; NEUROBLASTOMA CELL; NEUROTOXICITY; PREFIBRILLAR SPECIES; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY;

ACETIC ACIDS; ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANILINO NAPHTHALENESULFONATES; CELL LINE; FLUORESCENT DYES; HUMANS; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; THIOPHENES;

EID: 84859817796     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.097     Document Type: Article

References (15)

1. Dobson C.M. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2001, 356:133-145.
2. Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
3. Wolfe M.S., Guenette S.Y. APP at a glance. J. Cell Sci. 2007, 120:3157-3161.
4. Luheshi L.M., Tartaglia G.G., Brorsson A.-C., et al. Systematic in vivo analysis of the intrinsic determinants of amyloid β pathogenicity. PLoS Biol. 2007, 5:e290.
5. Kumar-Singh S., Theuns J., Van Broeck B., et al. Mean age-of-onset of familial Alzheimer disease caused by presenilin mutations correlates with both increased Aβ42 and decreased Aβ40. Hum. Mutat. 2006, 27:686-695.
6. Walsh D.M., Lomakin A., Benedek G.B., et al. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 1997, 272:22364-22372.
7. Cleary J.P., Walsh D.M., Hofmeister J.J., et al. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat. Neurosci. 2005, 8:79-84.
8. Nilsberth C., Westlind-Danielsson A., Eckman C.B., et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nat. Neurosci. 2001, 4:887-893.
9. Brorsson A.-C., Bolognesi B., Tartaglia G.G., et al. Intrinsic determinants of neurotoxic aggregate formation by the amyloid β peptide. Biophys. J. 2010, 98:1677-1684.
10. LeVine H., Ronald W. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999, 274-284.
11. Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites. J. Mol. Biol. 1965, 13:482-495.
12. Hammarström P., Simon R., Nyström S., et al. A fluorescent pentameric thiophene derivative detects in vitro-formed prefibrillar protein aggregates. Biochemistry 2010, 49:6838-6845.
13. Xue W.-F., Hellewell A.L., Gosal W.S., et al. Fibril fragmentation enhances amyloid cytotoxicity. J. Biol. Chem. 2009, 284:34272-34282.
14. Bolognesi B., Kumita J.R., Barros T.P., et al. ANS binding reveals common features of cytotoxic amyloid species. ACS Chem. Biol. 2010, 5:735-740.
15. Campioni S., Mannini B., Zampagni M., et al. A causative link between the structure of aberrant protein oligomers and their toxicity. Nat. Chem. Biol. 2010, 6:140-147.