Improved Fmoc-based solid-phase synthesis of homologous peptide fragments of human and mouse prion proteins

Journal of Peptide Science

Volumn 17, Issue 1, 2011, Pages 32-38

  Grillo Bosch, Dolors ^a,b   Rabanal, Francesc ^b   Giralt, Ernest ^a,b  

^a INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^b UNIVERSITY OF BARCELONA   (Spain)

Author keywords

Aggregation; Difficult sequence; PEGA resin; Prion protein

Indexed keywords

FLUORENYLMETHYLOXYCARBONYL CHLORIDE; MACROGOL DERIVATIVE; PEPTIDE FRAGMENT; PRION PROTEIN; RESIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; HUMAN; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; SEQUENCE ANALYSIS; SOLID PHASE SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; FLUORENES; HUMANS; MICE; MICROSCOPY, ELECTRON, TRANSMISSION; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; POLYETHYLENE GLYCOLS; PRIONS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 78650247534     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1293     Document Type: Article

References (50)

1. Lloyd-Williams PA, Albericio F, Giralt E. Chemical Approaches to the Synthesis of Peptides and Proteins. CRC Press: Boca Raton, New York, 1997.
2. Merrifield RB. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963; 85: 2149-2154.
3. Kent SBH. Difficult sequences in stepwise peptide synthesis: common molecular origins in solution and solid phase? Pept.: Struct. Funct., Proc. Am. Pept. Symp. 9th 1985; 407-414.
4. Live DH, Kent SBH. Correlation of coupling rates with physicochemical properties of resin-bound peptides in solid phase synthesis. Pept.: Struct. Funct., Proc. Am. Pept. Symp, 8th 1983; 65-68.
5. Ludwick AG, Jelinski LW, Live D, Kintanar A, Dumais JJ. Association of peptide chains during Merrifield solid-phase peptide synthesis. A deuterium NMR study. J. Am. Chem. Soc. 1986; 108: 6493-6496.
6. Mutter M, Oppliger H, Zier A. Solubilizing protecting groups in peptide synthesis. Effect of side-chain-attached polyethylene glycol derivatives upon beta-sheet formation of model peptides. Makromol. Chem., Rapid Commun. 1992; 13: 151-157.
7. Pudelko M, Kihlberg J, Elofsson M. Application of gel-phase 19F NMR spectroscopy for optimization of solid-phase synthesis of a hydrophobic peptide from the signal sequence of the mucin MUC1. J. Pept. Sci. 2007; 13: 354-361.
8. Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003; 81: 678-699.
9. Sunde M, Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 1997; 50: 123-159.
10. Tycko R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 2006; 39: 1-55.
11. Sohma Y, Hayashi Y, Kimura M, Chiyomori Y, Taniguchi A, Sasaki M, Kimura T, Kiso Y. The 'O-acyl isopeptide method' for the synthesis of difficult sequence-containing peptides: application to the synthesis of Alzheimer's disease-related amyloid beta peptide (A-beta) 1-42. J. Pept. Sci. 2005; 11: 441-451.
12. Garcia-Martin F, Quintanar-Audelo M, Garcia-Ramos Y, Cruz LJ, Gravel C, Furic R, Cote S, Tulla-Puche J, Albericio F. ChemMatrix, a poly(ethylene glycol)-based support for the solid-phase synthesis of complex peptides. J. Comb. Chem. 2006; 8: 213-220.
13. Hope J. Prions and neurodegenerative diseases. Curr. Opin. Genet. Dev. 2000; 10: 568-574.
14. Cummings JL. The Neuropsychiatry of Alzheimer's Disease and Related Dementias. Martin Dunitz Ltd., Taylor and Francis group: London, 2003.
15. Soto C, Estrada Lisbell D. Protein misfolding and neurodegeneration. Arch. Neurol. 2008; 65: 184-189.
16. Huang Z, Gabriel JM, Baldwin MA, Fletterick RJ, Prusiner SB, Cohen FE. Proposed three-dimensional structure for the cellular prion protein. Proc. Natl. Acad. Sci. USA 1994; 91: 7139-7143.
17. Schatzl HM, Da Costa M, Taylor L, Cohen FE, Prusiner SB. Prion protein gene variation among primates. J. Mol. Biol. 1995; 245: 362-374.
18. Forloni G, Tagliavini F, Bugiani O, Salmona M. Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides. Prog. Neurobiol. 1996; 49: 287-315.
19. Brown DR. Prion protein peptides: optimal toxicity and peptide blockade of toxicity. Mol. Cell. Neurosci 2000; 15: 66-78.
20. Kourie JI, Culverson A. Prion peptide fragment PrP[106-126] forms distinct cation channel types. J. Neurosci. Res. 2000; 62: 120-133.
21. Kanapathipillai M, Ku SH, Girigoswami K, Park CB. Small stress molecules inhibit aggregation and neurotoxicity of prion peptide 106-126. Biochem. Bioph. Res. Co. 2008; 365: 808-813.
22. De Gioia L, Selvaggini C, Ghibaudi E, Diomede L, Bugiani O, Forloni G, Tagliavini F, Salmona M. Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J. Biol. Chem. 1994; 269: 7859-7862.
23. Tagliavini F, Prelli F, Verga L, Giaccone G, Sarma R, Gorevic P, Ghetti B, Passerini F, Ghibaudi E, Forloni G, Salmona M, Bugiani O, Frangione B. Synthetic peptide homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA 1993; 90: 9678-9682.
24. Selvaggini C, De Gioia L, Cantu L, Ghibaudi E, Diomede L, Passerini F, Forloni G, Bugiani O, Tagliavini F, Salmona M. Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Bioph. Res. Co. 1993; 194: 1380-1386.
25. Forloni G, Angeretti N, Chiesa R, Monzani E, Salmona M, Bugiani O, Tagliavini F. Neurotoxicity of a prion protein fragment. Nature 1993; 362: 543-546.
26. Jobling MF, Barrow CJ, White AR, Masters CL, Collins SJ, Cappai R. The synthesis and spectroscopic analysis of the neurotoxic prion peptide 106-126: comparative use of manual Boc and Fmoc chemistry Lett. Pept. Sci. 1999; 6: 129-134.
27. Hyde C, Johnson T, Owen D, Quibell M, Sheppard RC. Some 'difficult sequences' made easy. A study of interchain association in solid-phase peptide synthesis. Int. J. Pept. Protein Res. 1994; 43: 431-440.
28. Florio T, Paludi D, Villa V, Principe DR, Corsaro A, Millo E, Damonte G, D'Arrigo C, Russo C, Schettini G, Aceto A. Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J. Neurochem. 2003; 85: 62-72.
29. Cardona V, Eberle I, Barthélémy S, Beythien J, Doerner B, Schneeberger P, Keyte J, White P. Application of Dmb-dipeptides in the Fmoc SPPS of difficult and aspartimide-prone sequences. Int. J. Pept. Res. Therapeut. 2008; 14: 285-292.
30. Bagley CJ, Otteson KM, May BL, McCurdy SN, Pierce L, Ballard FJ, Wallace JC. Synthesis of insulin-like growth factor I using N-methyl pyrrolidinone as the coupling solvent and trifluoromethane sulfonic acid cleavage from the resin. Int. J. Pept. Prot. Res. 1990; 36: 356-361.
31. Varanda LM, Miranda MTM. Solid-phase peptide synthesis at elevated temperatures: a search for an optimized synthesis condition of unsulfated cholecystokinin-12. J. Pept. Res. 1997; 50: 102-108.
32. Auzanneau F-I, Meldal M, Bock K. Synthesis, characterization and biocompatibility of PEGA resins. J. Pept. Sci. 1995; 1: 31-44.
33. Renil M, Meldal M. Synthesis and application of a PEGA polymeric support for high capacity continuous flow solid-phase peptide synthesis. Tetrahedron Lett. 1995; 36: 4647-4650.
34. Renil M, Ferreras M, Delaisse JM, Foged NT, Meldal M. PEGA supports for combinatorial peptide synthesis and solid-phase enzymic library assays. J. Pept. Sci. 1998; 4: 195-210.
35. Kaiser E, Colescott RL, Bossinger CD, Cook PI. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970; 34: 595-598.
36. Vazquez J, Qushair G, Albericio F. Qualitative colorimetric tests for solid phase synthesis. Methods Enzymol. 2003; 369: 21-35.
37. Fields CG, Macdonald RL, Otteson KM, Noble RL. HBTU activation for automated Fmoc solid-phase peptide synthesis. Pept. Res. 1991; 4: 95-101.
38. Garcia-Martin F, White P, Steinauer R, Cote S, Tulla-Puche J, Albericio F. The synergy of ChemMatrix resin and pseudoproline building blocks renders RANTES, a complex aggregated chemokine. Biopolymers 2006; 84: 566-575.
39. Cremer G-A, Tariq H, Delmas AF. Combining a polar resin and a pseudo-proline to optimize the solid-phase synthesis of a 'difficult sequence'. J. Pept. Sci. 2006; 12: 437-442.
40. Pastor JJ, Granados G, Carulla N, Rabanal F, Giralt E. Redesign of protein domains using one-bead-one-compound combinatorial chemistry. J. Am. Chem. Soc. 2007; 129: 14922-14932.
41. Atherton ES, Sheppard RC. Solid Phase Peptide Synthesis: a Practical Approach. IRL Press: Oxford, 1989.
42. Rabanal F. Base/nucleophile-labile resins (Francesc Rabanal). In The Power of Functional Resins in Organic Synthesis, 1st edn, Tulla-Puche J, Albericio F (eds). Wiley VCH Verlag GmbH & Co KGaA: Weinheim, Germany, 2008; 417-436.
43. Kinter M, Sherman NE. Protein Sequencing and Identification using Tandem Mass Spectrometry. Wiley-Interscience: New York, 2000.
44. Sreerama N, Woody RW. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 2004; 383: 318-351.
45. Greenfield NJ. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protocols 2007; 1: 2876-2890.
46. Whitmore L, Wallace BA. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008; 89: 392-400.
47. Linden R, Martins VR, Prado MAM, Cammarota M, Izquierdo I, Brentani RR. Physiology of the prion protein. Physiol. Rev. 2008; 88: 673-728.
48. Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002; 418: 291.
49. Walsh P, Yau J, Simonetti K, Sharpe S. Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP (106-126). Biochemistry 2009; 48: 5779-5781.
50. Walsh P, Simonetti K, Sharpe S. Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure 2009; 17: 417-426.