Structural conversion rate changes of recombinant bovine prion by designed synthetic peptides

International Journal of Peptide Research and Therapeutics

Volumn 18, Issue 3, 2012, Pages 217-225

  Hirata, Akiyoshi ^a   Yajima, Shunsuke ^b   Yasuhara, Tadashi ^b   Nokihara, Kiyoshi ^a  

^a HiPep Laboratories   (Japan)

^b TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

Author keywords

Aggregation kinetics; Designed synthetic peptide; Prion protein related peptide; Recombinant bovine prion protein; Structural conversion

Indexed keywords

PRION PROTEIN; SYNTHETIC PEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; PEPTIDE MAPPING; PEPTIDE SYNTHESIS; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

BOVINAE;

EID: 84867330818     PISSN: 15733149     EISSN: 15733904     Source Type: Journal    
DOI: 10.1007/s10989-012-9294-z     Document Type: Article

References (32)

1. Abalos GC, Cruite JT, Bellon A, Hemmers S, Akagi J, Mastrianni JA, Williamson RA, Solforosi L (2008) Identifying key components of the PrPC-PrPSc replicative interface. J Biol Chem 283:34021-34028
2. Bocharova OV, Breydo L, Salnikov VV, Baskakov IV (2005) Copper(II) inhibits in vitro conversion of Prion protein into amyloid fibrils. Biochemistry 44:6776-6787
3. Boshuizen RS, Schulz V, Morbin M, Mazzoleni G, Meloen RH, Langedijk JP (2009) Heterologous stacking of prion protein peptides reveals structural details of fibrils and facilitates complete inhibition of fibril growth. J Biol Chem 284:12809-12820
4. Cheng H-M, Tsai TWT, Huang WYC, Lee H-K, Lian H-Y, Chou F-C, Mou Y, Chan JCC (2011) Steric zipper formed by hydrophobic peptide fragment of Syrian hamster prion protein. Biochemistry 50:6815-6823
5. De Gioia L, Selvaggini C, Ghibaudi E, Diomede L, Bugiani O, Forloni G, Tagliavini F, Salmona M (1994) Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J Biol Chem 269:7859-7862
6. Di Natale G, Impellizzeri G, Pappalardo G (2005a) Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study. Org Biomol Chem 3:490-497
7. Di Natale G, Grasso G, Impellizzeri G, La Mendola D, Micera G, Mihala N, Nagy Z, Osz K, Pappalardo G, Rigó V, Rizzarelli E, Sanna D, Sóvágó I (2005b) Copper(II) interaction with unstructured prion domain outside the octarepeat region: speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides. Inorg Chem 44:7214-7225
8. Dupiereux I, Zorzi W, Lins L, Brasseur R, Colson P, Heinen E, Elmoualij B (2005) Interaction of the 106-126 prion peptide with lipid membranes and potential implication for neurotoxicity. Biochem Biophys Res Commun 331:894-901
9. Evans KC, Berger EP, Cho CG, Weisgraber KH, Lans bury PT Jr (1995) Apolipoprotein E is a kinetic but not thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci USA 92:763-767
10. García-Martín F, Quintanar-Audelo M, García-Ramos Y, Cruz LJ, Gravel C, Furic R, Côté S, Tulla-Puche J, Albericio F (2006) ChemMatrix, a poly(ethylene glycol)-based support for the solid-phase synthesis of complex peptides. ChemMatrix, a poly(ethylene glycol)-based support for the solid-phase synthesis of complex peptides. J Comb Chem 8:213-220
11. Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sóvá gó I (2005) Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues. Chemistry 12:537-547
12. Haris PI, Chapman D (1995) The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 37: 251-263
13. Kawasaki T, Ohyama T, Hirata A, Nokihara K (2010) Fingerprintdetection of sugar-binding proteins generated by labeled structured glycopeptides arrays. Bull Chem Soc Jpn 83:799-801
14. Kuroda Y, Maeda Y, Sawa S, Shibata K, Miyamoto K, Nakagawa T (2003) Effects of detergents on the secondary structures of prion protein peptides as studied by CD spectroscopy. J Pept Sci 9: 212-220
15. López GF, Zahn R, Riek R, Wüthrich K (2000) NMR structure of the bovine prion protein. Proc Natl Acad Sci 97:145-150
16. Miyazato N, Hirata A, Kawakami H, Kawahira N, Ohyama T, Nokihara K (2008) Efficient solid-phase synthesis and purification of b-Amyloid peptides by improved protocols with a novel HPLC column. In: Aimoto S, Ono S (eds) Peptide science 2007. Japanese Peptide Society, pp 143-146
17. Natalello A, Prokorov VV, Tagliavini F, Morbin M, Forloni G, Beeg M, Manzoni C, Colombo L, Gobbi M, Salmona M, Doglia SM (2008) Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways. J Mol Biol 381:1349-1361
18. Nokihara K, Nagawa Y, Hong S-P, Nakanishi H (1997) Efficient solid-phase synthesis of a large peptide by a single coupling protocol with a single step of HPLC purification. Lett Pept Sci 4:141-146
19. Nokihara K, Yasuhara T, Nakata Y, Lerner EA, Wray V (2007) Chemical synthesis of Maxadilan, a non-mammalian potent vasodilatory peptide consisting of 61 amino acids with two disulfide bridges, and its related peptides. Int J Pept Res Ther 13:377-386
20. Nokihara K, Ohyama T, Ono N, Kawakami H, Kawahira N, Kodama Y, Miyazato N, Suzuki K, Miyajima M, Sogon T, Hirata A, Kawasaki T, Takebayashi Y, Oka Y (2008) Development of peptide arrays as sensor elements and novel chip-materials focusing on practical bio-chip production. In: Aimoto S, Ono S (eds) Peptide science 2007. Japanese Peptide Society, pp 106-108
21. Prusiner SB (1997) Prion diseases and the BSE crisis. Science 278:245-250
22. Rehders D, Claasen B, Redecke L, Buschke A, Reibe C, Jehmlich N, von Bergen M, Betzel C, Meyer B (2009) Peptide NMHRYPNQ of the cellular prion protein (PrPC) inhibits aggregation and is a potential key for understanding prion-prion interaction. J Mol Biol 392:198-207
23. Ronga L, Palladino P, Ragone R, Benedetti E, Rossi F (2009) A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein a2-helix. J Pept Sci 15:30-35
24. Satheeshkumar KS, Jayakumar R (2003) Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein. Biophys J 85:473-483
25. Satheeshkumar KS, Murali J, Jayakumar R (2004) Assemblages of prion fragments: novel model systems for understanding amyloid toxicity. J Struct Biol 148:176-193
26. Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AO, Riekel C, Eisenberg D (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447:453-457
27. Soto C, Kascsak RJ, Saborío GP, Aucouturier P, Wisniewski T, Prelli F, Kascsak R, Mendez E, Harris DA, Ironside J, Tagliavini F, Carp RI, Frangione B (2000) Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 355:192-197
28. Tycko R, Savtchenko R, Ostapchenko VG, Makarava N, Baskako IV (2010) The a-helical C-Terminal domain of full-length recombinant PrP converts to an in-register parallel b-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry 49:9488-9497
29. Walsh P, Simonetti K, Sharpe S (2009) Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure 17:417-426
30. Winsor CP (1932) The Gompertz curve as a growth curve. Proc Natl Acad Sci USA 18:1-8
31. Wray V, Kakoschke C, Nokihara K, Naruse S (1993) Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy. Biochemistry 32:5832-5841
32. Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S (2003) CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC?PrPSc conversion process. J Biol Chem 278:50175-50181