Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-I

FEBS Letters

Volumn 586, Issue 13, 2012, Pages 1754-1758

  Wong, Yuan Qi ^a   Binger, Katrina J ^a,b   Howlett, Geoffrey J ^a   Griffin, Michael D W ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

Aggregation; ApoA I; Peptide; Protein misfolding

Indexed keywords

AMYLOID; AMYLOID FIBRIL FORMING PEPTIDE; APOLIPOPROTEIN A1; APOLIPOPROTEIN A1[46-59]; PEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; ATHEROSCLEROTIC PLAQUE; CRYSTAL STRUCTURE; FAMILIAL AMYLOIDOSIS; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

AMYLOID; AMYLOIDOSIS, FAMILIAL; APOLIPOPROTEIN A-I; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 84862489906     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.007     Document Type: Article

References (20)

1. Rye, K.A. and Barter, P.J. (2004) Formation and metabolism of prebetamigrating, lipid-poor apolipoprotein A-I. Arterioscler. Thromb. Vasc. Biol. 24, 421-428.
2. Tall, A.R. (2008) Cholesterol efflux pathways and other potential mechanisms involved in the athero-protective effect of high density lipoproteins. J. Intern. Med. 263, 256-273.
3. Gursky, O., Mei, X. and Atkinson, D. (2012) The crystal structure of the Cterminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment. Biochemistry 51, 10-18.
4. Rowczenio, D. et al. (2011) Amyloidogenicity and clinical phenotype associated with five novel mutations in apolipoprotein A-I. Am. J. Pathol. 179, 1978-1987.
5. Rocken, C., Tautenhahn, J., Buhling, F., Sachwitz, D., Vockler, S., Goette, A. and Burger, T. (2006) Prevalence and pathology of amyloid in atherosclerotic arteries. Arterioscler. Thromb. Vasc. Biol. 26, 676-677.
6. Wong, Y.Q., Binger, K.J., Howlett, G.J. and Griffin, M.D.W. (2010) Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proc. Natl. Acad. Sci. USA 107, 1977-1982.
7. Zehender, F., Ziegler, A., Schonfeld, H.J. and Seelig, J. (2012) Thermodynamics of protein self-association and unfolding. The case of apolipoprotein a-I. Biochemistry 51, 1269-1280.
8. Gursky, O. and Atkinson, D. (1996) Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. Proc. Natl. Acad. Sci. USA 93, 2991-2995. (Pubitemid 26114351)
9. Hatters, D.M. and Howlett, G.J. (2002) The structural basis for amyloid formation by plasma apolipoproteins: a review. Eur. Biophys. J. 31, 2-8.
10. Sawaya, M.R. et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447, 453-457. (Pubitemid 46816731)
11. Giasson, B.I., Murray, I.V., Trojanowski, J.Q. and Lee, V.M. (2001) A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 276, 2380-2386.
12. Jones, S., Manning, J., Kad, N.M. and Radford, S.E. (2003) Amyloid-forming peptides from beta2-microglobulin-insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 325, 249-257. (Pubitemid 36062686)
13. Westermark, P., Engstrom, U., Johnson, K.H., Westermark, G.T. and Betsholtz, C. (1990) Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc. Natl. Acad. Sci. USA 87, 5036-5040.
14. Todorova, N., Hung, A., Maaser, S.M., Griffin, M.D.W., Karas, J., Howlett, G.J. and Yarovsky, I. (2010) Effects of mutation on the amyloidogenic propensity of apolipoprotein C-II(60-70) peptide. Phys. Chem. Chem. Phys. 12, 14762-14774.
15. Teoh, C.L. et al. (2011) A structural model for apolipoprotein C-II amyloid fibrils: experimental characterization and molecular dynamics simulations. J. Mol. Biol. 405, 1246-1266.
16. Makin, O.S., Sikorski, P. and Serpell, L.C. (2006) Diffraction to study protein and peptide assemblies. Curr. Opin. Chem. Biol. 10, 417-422. (Pubitemid 44375062)
17. Maurer-Stroh, S. et al. (2010) Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat. Methods 7, 237-242.
18. Ohhashi, Y., Ito, K., Toyama, B.H., Weissman, J.S. and Tanaka, M. (2010) Differences in prion strain conformations result from non-native interactions in a nucleus. Nat. Chem. Biol. 6, 225-230.
19. Tjernberg, L.O., Callaway, D.J., Tjernberg, A., Hahne, S., Lilliehook, C., Terenius, L., Thyberg, J. and Nordstedt, C. (1999) A molecular model of Alzheimer amyloid beta-peptide fibril formation. J. Biol. Chem. 274, 12619-12625.
20. Mei, X. and Atkinson, D. (2011) Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization. J. Biol. Chem. 286, 38570-38582.