Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective

Journal of Peptide Science

Volumn 12, Issue 12, 2006, Pages 790-795

  Ronga, Luisa ^a   Palladino, Pasquale ^a   Tizzano, Barbara ^a   Marasco, Daniela ^a   Benedetti, Ettore ^a   Ragone, Raffaele ^b   Rossi, Filomena ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

Amyloid; Anions; Cations; Counterions; Hofmeister series; Prion helix 2 derived peptides; Prion structure; Transmissible spongiform encephalopathies

Indexed keywords

ANION; CATION; PRION PROTEIN; PRION PROTEIN HELIX 2 DERIVATIVE; SODIUM CHLORIDE;

ALPHA HELIX; ARTICLE; BETA SHEET; HUMAN; IONIC STRENGTH; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; ELECTROSTATICS; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PRIONS; PROTEIN STRUCTURE, SECONDARY; SALTS; SULFATES;

EID: 33845662273     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.818     Document Type: Article

References (33)

1. Carrel RW, Lomas DA. Conformational disease. Lancet 1997; 350: 134-138.
2. Temussi PA, Masino L, Pastore A. From Alzheimer to Huntington: why is a structural understanding so difficult? EMBO J. 2003; 22: 355-361.
3. Swietnicki W, Petersen RB, Gambetti P, Surewicz WK. pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 1997; 272: 27517-27520.
4. Swietnicki W, Morillas M, Chen SG, Gambetti P, Surewicz WK. Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 2000; 39: 424-431.
5. Liemann S, Glockshuber R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 1999; 38: 3258-3267.
6. Hornemann S, Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 6010-6014.
7. Wildegger G, Liemann S, Glockshuber R. Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat. Struct. Biol. 1999; 6: 550-553.
8. Rezaei H, Marc D, Choiset Y, Takahashi M, Hoa GHB, Haertle T, Grosclaude J, Debey P. High yield purification and physicochemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 2000; 267: 2833-2839.
9. Zanusso G, Farinazzo A, Fiorini M, Gelati M, Castagna A, Righetti PG, Rizzuto N, Monaco S. pH-Dependent prion protein conformation in classical Creutzfeldt-Jakob disease. J. Biol. Chem. 2001; 276: 40 377-40 380.
10. Baskakov IV, Legname G, Prusiner SB, Cohen FE. Folding of prion protein to its native α-helical conformation is under kinetic control. J. Biol. Chem. 2001; 276: 19 687-19 690.
11. c helix 1 in the hydrophilic seeding of prion aggregates. Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 11 293-11 298.
12. Apetri AC, Surewicz WK. Atypical effect of salts on the thermodynamic stability of human prion protein. J. Biol. Chem. 2003; 278: 22 187-22 192.
13. Morillas M, Vanik DL, Surewicz WK. On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry 2001; 40: 6982-6987.
14. Nandi PK, Leclerc E, Marc D. Unusual property of prion protein unfolding in neutral salt solution. Biochemistry 2002; 41: 11017-11024.
15. Sc conversion process. J. Biol. Chem. 2003; 278: 50 175-50 181.
16. Tizzano B, Palladino P, De Capua A, Marasco D, Rossi F, Benedetti E, Pedone C, Ragone R, Ruvo M. The human prion protein alpha2 helix: a thermodynamic study of its conformational preferences. Proteins 2005; 59: 72-79.
17. Haire LF, Whyte SM, Vasisht N, Gill AC, Verma C, Dodson EJ, Dodson GG, Bayley PM. The crystal structure of the globular domain of sheep prion protein. J. Mol. Biol. 2004; 336: 1175-1183.
18. Brown DR, Guantieri V, Grasso G, Impellizzeri G, Pappalardo G, Rizzarelli E. Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region. J. Inorg. Biochem. 2004; 98: 133-143.
19. Brown DR, Qin K, Herms JW, Madlung A, Manson J, Strome R, Fraser PE, Kruck T, von Bohlen A, Schulz-Schaeffer W, Giese A, Westaway D, Kretzschmar H. The cellular prion protein binds copper in vivo. Nature 1997; 390: 684-687.
20. Millhauser GL. Copper binding in the prion protein. Acc. Chem. Res. 2004; 37: 79-85.
21. Cereghetti GM, Schweiger A, Glockshuber R, van Doorslaer S. Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases. Biophys. J. 2003; 84: 1985-1997.
22. Zuegg J, Gready JE. Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions. Biochemistry 1999; 38: 13862-13876.
23. Sc-dependent cell-free formation of protease-resistant prion protein. EMBO J. 2001; 20: 377-386.
24. Cordeiro, Y, Machado F, Juliano Neto L, Juliano MA, Brentani RR, Foguel D, Silva JL. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 2001; 276: 49 400-49 409.
25. Calzolai L, Zahn R. Influence of pH on NMR structure and stability of the human prion protein globular domain. J. Biol. Chem. 2003; 278: 35592-35596.
26. De Simone A, Dodson GG, Verma CS, Zagari A, Fraternali F. Prion and water: tight and dynamical hydration sites have a key role in structural stability. Proc. Natl. Acad. Sci. U.S.A. 2005; 102: 7535-7540.
27. Kawatake S, Nishimura Y, Sakaguchi S, Iwaki T, Doh-ura K. Surface plasmon resonance analysis for the screening of anti-prion compounds. Biol. Pharm. Bull. 2006; 29: 927-932.
28. Collins KD. Charge density-dependent strength of hydration and biological structure. Biophys. J. 1997; 72: 65-76.
29. Collins KD. Ions from the hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process. Methods 2004; 34: 300-311.
30. Niedz RP, Evens TJ. A solution to the problem of ion confounding in experimental biology. Nat. Methods 2006; 3: 417.
31. Chen YR, Huang HB, Chyan CL, Shiao MS, Lin TH, Chen YC. The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy. J. Biochem. (Tokyo) 2006; 139: 733-740.
32. Roberts MF. Organic compatible solutes of halotolerant and halophilic microorganisms. Saline Syst. 2005; 1: 1-30.
33. Arora A, Ha C, Park CB. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 2004; 564: 121-125.