Disruption of the β-sheet structure of a protected pentapeptide, related to the β-amyloid sequence 17-21, induced by a single, helicogenic Cα-tetrasubstituted α-amino acid

Journal of Peptide Science

Volumn 9, Issue 7, 2003, Pages 461-466

  Formaggio, Fernando ^a   Bettio, Andrea ^a   Moretto, Vittorio ^a   Crisma, Marco ^a   Toniolo, Claudio ^a   Broxterman, Quirinus B ^b  

^a UNIVERSITY OF PADOVA   (Italy)

^b DSM RESEARCH   (Netherlands)

Author keywords

sheet breaker; sheet structure; Amyloid related sequence; C tetrasubstituted amino acid; Helix inducer; Infrared absorption; Nuclear magnetic resonance

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; ALPHA AMINO ACID; AMYLOID BETA PROTEIN; ORGANIC SOLVENT; PENTAPEPTIDE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CHEMICAL MODEL; CONTROLLED STUDY; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SUBSTITUTION; AMINOISOBUTYRIC ACIDS; AMYLOID BETA-PROTEIN; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0041629184     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.503     Document Type: Article

References (23)

1. Toniolo C, Bonora GM, Marchiori F, Borin G. An infrared absorption method to titrate quantitatively the extent of self-association in peptides. J. Am. Chem. Soc. 1984; 106: 1455-1457.
2. α-protected C-terminal sequences of substance P. Biopolymers 1986; 25: 281-289.
3. Karle IL, Balaram P. Structural characteristics of α-helical peptide molecules containing Aib residues. Biochemistry 1990; 29: 6747-6756.
4. α-tetrasubstitution). Biopolymers (Pept. Sci.) 2001; 60: 396-419.
5. Toniolo C, Bonora GM, Mutter M, Rajasekharan Pillai VN. Linear oligopeptides.78. The effect of the insertion of a proline residue on the solution conformation of host peptides. Makromol. Chem. 1981; 182: 2007-2014.
6. Narita M, Isokawa S, Doi M, Wakita R. The ability of the proline residue to promote successive intramolecular hydrogen bonds in oligopeptides. Bull. Chem. Soc. Jpn 1986; 59: 3547-3552.
7. n oligopeptides. Macromolecules 1989; 22: 2939-2944.
8. Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer's amyloidosis. by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Común. 1996; 226: 672-680.
9. Tjernberg LO, Lilliehöök Ch, Callaway DJE, Näslund J, Hahne S, Thyberg J, Terenius L, Nordstedt Ch. Controlling amyloid β-peptide fibril formation with protease-stable ligands. J. Biol. Chem. 1997; 272: 12601-12605.
10. Findeis MA. Approaches to discovery and characterization of inhibitors of amyloid β-peptide polymerization. Biochim. Biophys. Acta 2000; 1502: 76-84.
11. Kapurniotu A. Amyloidogenicity and cytotoxicity of islet amyloid polypeptide. Biopolymers (Pept. Sci.) 2001; 60: 438-459.
12. Hughes E, Burke RM, Doig AJ. Inhibition of toxicity in the β-amyloid peptide fragment β-(25-35) using N-methylated derivatives. A general strategy to prevent amyloid formation. J. Biol. Chem. 2000; 275: 25109-25115.
13. Janek K, Rothemund S, Gast K, Beyermann M, Zipper J, Fabian H, Bienert M, Krause E. In Peptides 2000, Martinez J, Fehrentz J-A (eds). EDK: Paris, 2001; 483-484.
14. Körtvelyesi T, Hetenyi C, Penke B. In Peptides 2000, Martinez J, Fehrentz J-A (eds). EDK: Paris, 2001: 493-494.
15. Gordon DJ, Sciarretta KL, Meredith SC. Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid congeners containing N-methyl amino acids at alternate residues. Biochemistry 2001: 40: 8237-8245.
16. Rijkers DTS, Höppener JWM, Posthuma G, Lips CJM, Liskamp RMJ. Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and α-hydroxy acid residue containing peptides. Chem. Eur. J. 2002; 8: 4285-4291.
17. Carpino LA. 1-Hydroxy-7-azabenzotriazole. An efficent peptide coupling additive. J. Am. Chem. Soc. 1993; 115: 4397-4398.
18. Tatzelt J, Prusiner SB, Welch WJ. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 1996; 15: 6363-6373.
19. Szabo Z, Kiss G, Soos K, Zarandi M, Penke B. In Peptides 1998, Bajusz S, Hudecz F (eds). Akademiai Kiadó: Budapest, 1999; 386-387.
20. 10- and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy. Biochemistry 1991; 30: 6541-6548.
21. Kopple KD, Ohnishi M, Go A. Conformations of cyclic peptides. IV. Nuclear magnetic resonance studies of cyclopentaglycyl-L-leucyl and cyclodiglycyl-L-hystidyl-diglycyl-L-tyrosyl. Biochemistry 1969: 8: 4087-4095.
22. Kopple KD, Schamper TJ. Proton magnetic resonance line broadening produced by association with a nitroxide radical in studies of amide and peptide conformation. J. Am. Chem. Soc. 1972; 94: 3644-3646.
23. α,α-disubstituted glycine. Incorporation into model peptides and preferred conformation. J. Pept.