Role of aromatic interactions in amyloid formation by peptides derived from human amylin

Biochemistry

Volumn 43, Issue 50, 2004, Pages 15901-15908

  Tracz, Sylvia M ^a   Abedini, Andisheh ^a   Driscoll, Miles ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; SCANNING; SUBSTITUTION REACTIONS;

AMYLOID FORMATION; AROMATIC-AROMATIC INTERACTIONS; HUMAN AMYLIN;

POLYPEPTIDES;

ALANINE; AMYLIN; AMYLOID; LEUCINE; PHENYLALANINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; PH; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOID; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PHENYLALANINE; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 10844254749     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048812l     Document Type: Article

References (41)

1. Sipe, J. D. (1994) Amyloidosis, Crit. Rev. Clin. Lab. Sci. 31, 325-354.
2. Lorenzo, A., Razzaboni, B., Weir, G. C., and Yankner, B. A. (1994) Pancreatic islet cell toxicity of Amylin associated with type II diabetes mellitus, Nature 368, 756-760.
3. Harper, J. D., and Lansbury, P. T., (1997) Models of amyloid seeding in Alzheimer's and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
4. Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology, Cell 93, 337-348.
5. Westermark, P., Wilander, E., Hayden, D. W., O'Brian, T. D., and Johnson, K. H. (1987) Amyloid fibrils in human insulinoma and islets of langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells, Proc. Natl. Acad. Sci. U.S.A. 84, 3881-3885.
6. Simmons, L. K., May, P. C., Tomaselli, K. J., Rydel, R. E., Fuson, K. S., Brigham, E. F., Wright, S., Lieberburg, I., Becker, G. W., Brems, D. N., and Li, W. Y. (1994) Secondary structure of amyloid β-peptide correlates with neurotoxic activity in vitro, Mol. Pharm. 45, 373-379.
7. Kapurniotu A. (2001) Amyloidogenicity and cytotoxicity of islet amyloid polypeptide, Biopolymers 60, 438-459.
8. Clark, A., Lewis, C. E., Willis, A. C., Cooper, G. J. S., Morris, J. F., Reid, K. B. M., and Turner, R. C. (1987) Islet amyloid formed from diabetes-associated peptide may be pathogenic in type II diabetes, Lancet 2, 231-234.
9. Cooper, G. J. S., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., and Reid, K. B. M. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type II diabetic patients, Proc. Natl. Acad. Sci. U.S.A. 84, 8628-8632.
10. Lopez de la Paz, M., and Serrano, L. (2004) Sequence determinants of amyloid fibril formation, Proc. Natl. Acad. Sci. U.S.A. 101, 87-92.
11. Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates, Nature 424, 805-808.
12. Mazor, Y., Gilead, S., Benhar, I., and Gazit, E. (2002) Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide, J. Mol. Biol. 322, 1013-1024.
13. 2-microglobulin-Insights into the mechanism of fibril formation in vitro, J. Mol. Biol. 325, 249-257.
14. Broome, B. M., and Hecht, M. H. (2000) Nature disfavors sequences of alternating polar and nonpolar amino acids: Implications for amyloidogenesis, J. Mol. Biol. 296, 961-968.
15. Burley, S. K., and Petsko, G. A. (1988) Weakly polar interactions in proteins, Adv. Protein Chem. 39, 125-189.
16. Azriel, R., and Gazit, E. (2001) Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide, J. Biol. Chem. 276, 34156-34161.
17. Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils, FASEB J. 16, 77-83.
18. Reches, M., Porat, Y., and Gazit, E. (2002) Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin, J. Biol. Chem. 277, 35475-35480.
19. Westermark, P., and Wilander, E. (1978) Influence of amyloid deposits on islet volume in maturity onset diabetes-mellitus, Diabetologia 15, 417-421.
20. Kruger, D. F., Gatcomb, P. M., and Owen, S. K. (1999) Clinical implications of amylin and amylin deficiency, Diabetes Educ. 25, 389-397.
21. Kahn, S. E., Andrikopoulos, S., and Verchere, C. B. (1999) Islet amyloid: A long recognized but underappreciated pathological feature of type II diabetes, Diabetes 48, 241-246.
22. Jaikaran, E., and Clark, A. (2001) Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology, Biochim. Biophys. Acta 1537, 179-203.
23. 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. U.S.A. 87, 5036-5040.
24. Moriarty, D. P., and Raleigh, D. P. (1999) Effects of sequential proline substitution on amyloid formation by human Amylin 20-29, Biochemistry 38, 1811-1818.
25. Ashburn, T. T., and Lansbury, P. T. (1993) Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation - Peptide models of pancreatic amyloid, J. Am. Chem. Soc. 115, 11012-11013.
26. Ashburn, T. T., Auger, M., and Lansbury, P. T. (1992) The structural basis of pancreatic amyloid formation: Isotope-edited spectroscopy in the solid state, J. Am. Chem. Soc. 114, 790-791.
27. Nilsson, M. R., and Raleigh, D. P. (1999) Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. J. Mol. Biol. 294, 1375-1385.
28. Jaikaran, E. T., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A., and Fraser, P. E. (2001) Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis, J. Mol. Biol. 308, 515-525.
29. Goldsbury, C., Goldie, K., Pellaud, J., Seeling, J., Frey, P., Muller, S. A., Kistler, J., Cooper, G. J. S., and Aebi, U. (2000) Amyloid fibril formation from full-length and fragments of amylin, J. Struct. Biol. 130, 352-362.
30. Tenidis, K., Waldner, M., Bernhagen, J., Fischle, W., Bergmann, M., Weber, M., Merkle, M. L., Voelter, W., Brunner, H., and Kapurniotu, A. (2000) Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties, J. Mol. Biol. 295, 1055-1071.
31. Zanuy, D., Ma, B., and Nussinov, R. (2003) Short peptide amyloid organization: Stabilities and conformations of the islet amyloid peptide NFGAIL, Biophys. J. 84, 1884-1894.
32. Zanuy, D., and Nussinov, R. (2003) The sequence dependence of fiber organization: A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29, J. Mol. Biol. 329, 565-584.
33. Zanuy, D., Porat, Y., Gazit, E., and Nussinov, R. (2004) Peptide sequence and amyloid formation: Molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs, Structure 12, 439-455.
34. Nilsson, M. R., and Raleigh, D. P. (2001) Low levels of asparagine deamidation can have dramatic effects on the aggregation of amyloidogenic peptides: Implications for the study of amyloid formation, Protein Sci. 11, 342-349.
35. Driscoll, M. E. (2001) Amyloid Formation by Amylin. M.S. Thesis. State University of New York at Stony Brook.
36. Chou, P. Y., and Fasman, G. D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence, Adv. Eniymol. 47, 45-148.
37. Williams, R. W., Chang, A., Juretic, D., and Loughran, S. (1987) Secondary structure predictions and medium range interactions, Biochim. Biophys. Acta 916, 200-204.
38. Smith, C. K., and Regan, L. (1997) Construction and design of β-sheets, Acc. Chem. Res. 30, 153-161.
39. Creighton, T. E. (1993) Proteins: Structures and Molecular Properties, 2nd ed., W. H. Freeman and Co., New York.
40. Tjernberg, L., Hosia, W., Bark, N., Thyberg, J., and Johansson, J. (2002) Charge attraction and β-propensity are necessary for amyloid fibril formation from tetrapeptides, J. Biol. Chem. 277, 43243-43246.
41. 16-22 amyloid peptides into antiparallel β sheets, Structure 11, 295-307.