Effect of one D-Leu residue on right-handed helical -L-Leu-Aib- peptides in the crystal state

Journal of Peptide Science

Volumn 17, Issue 6, 2011, Pages 420-426

  Demizu, Yosuke ^a   Doi, Mitsunobu ^b   Sato, Yukiko ^a   Tanaka, Masakazu ^c   Okuda, Haruhiro ^a   Kurihara, Masaaki ^a  

^a NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^b OSAKA MEDICAL COLLEGE   (Japan)

^c NAGASAKI UNIVERSITY   (Japan)

Author keywords

Amino acids; Conformation; Peptide; Secondary structure; X ray crystallographic analysis

Indexed keywords

LEUCINE; PEPTIDE DERIVATIVE;

ARTICLE; CRYSTAL STRUCTURE; DIASTEREOISOMER; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; LEUCINE; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; STEREOISOMERISM;

EID: 79955909466     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1332     Document Type: Article

References (39)

1. Schneider JP, Kelly JW. Template that induce α-helical, β-sheet, and loop conformations. Chem. Rev. 1995; 95: 2169-2187.
2. Venkatraman J, Shankaramma SC, Balaram P. Design of folded peptides. Chem. Rev. 2001; 101: 3131-3152.
3. Narita M, Honda S, Ueyama H. Conformational analysis of oligo-L-leucines containing only one D-amino acid residue. Bull. Chem. Soc. Jpn. 1987; 60: 4127-4131.
4. 4-OMe. Biopolymers 1989; 28: 193-201.
5. 2. J. Am. Chem. Soc. 1992; 114: 3182-3188.
6. Haque TS, Little JC, Gellman SH. Stereochemical requirements for β-hairpin formation: medel studies with four-residue peptides and depsipeptides. J. Am. Chem. Soc. 1996; 118: 6975-6985.
7. α type hexapeptide fold. Chem. Commun. 1997; 1379-1380.
8. Dhanasekaran M, Fabiola F, Pattabhi V, Durani S. A rationally designed turn-helix peptide. J. Am. Chem. Soc. 1999; 121: 5575-5576.
9. Karle IL, Hosahudya GN, Balaram P. Crystal structure of a hydrophobic 19-residue peptide helix containing three centrally located D-amino acids. Proc. Natl. Acad. Sci. U.S.A. 2003; 100: 13946-13951.
10. Jaun B, Tanaka M, Seiler P, Kuhnle FNM, Braun C, Seebach D. Studies on the conformation of Boc-protected (S)-(+)-isovaline homopeptide methyl esters in the solid state and in solution. Liebigs Ann. Recl. 1997; 1697-1710.
11. Karle IL. Controls exerted by the Aib residue: helix formation and helix reversal. Biopolymers (Pept. Sci.) 2001; 60: 351-365.
12. α-methylated peptide. Implications for folding of membrane proteins. J. Am. Chem. Soc. 2001; 123: 6678-6686.
13. Toniolo C, Crisma M, Formaggio F, Peggion C, Broxterman QB, Kaptein B. Molecular spacers for physicochemical investigations based on novel helical and extended peptide structures. Biopolymers (Pept. Sci.) 2004; 76: 162-176.
14. Crisma M, Formaggio F, Moretto A, Toniolo C. Peptide helices based on α-amino acids. Biopolymers (Pept. Sci.) 2006; 84: 3-12.
15. Aravinda S, Shamala N, Balaram P. Aib residues in peptaibiotics and synthetic sequences: analysis of nonhelical conformations. Chem. Biodivers. 2008; 5: 1238-1262.
16. 10-helical peptide. J. Am. Chem. Soc. 2008; 130: 12266-12267.
17. Oba M, Tanaka M, Kurihara M, Suemune H. Conformation of peptides containing (S-α-ethylleucine. Helv. Chim. Acta 2002; 85: 3197-3218.
18. 10-helical structure of peptide composed of diverse α-ethylated α, α-disubstituted α-amino acids. Chem. Eur. J. 2003; 9: 3082-3090.
19. Tanaka M, Demizu Y, Doi M, Kurihara M, Suemune H. Chiral centers in the side chains of α-amino acids control the helical screw sense of peptides. Angew. Chem. Int. Ed. 2004; 43: 5360-5363.
20. Royo S, Borggraeve WMD, Peggion C, Formaggio F, Crisma M, Jiménez Al, Cativiela C, Toniolo C. Turn and helical peptide handedness governed exclusively by side-chain chiral centers. J. Am. Chem. Soc. 2005; 127: 2036-2037.
21. Tanaka M, Anan K, Demizu Y, Kurihara M, Doi M, Suemune H. Side-chain chiral centers of amino acid and helical-screw handedness of its peptides. J. Am. Chem. Soc. 2005; 127: 11570-11571.
22. Tanaka M. Design and synthesis of chiral α, α-disubstituted α-amino acids and conformational study of their oligopeptides. Chem. Pharm. Bull. 2007; 55: 349-358.
23. Nagano M, Tanaka M, Doi M, Demizu Y, Kurihara M, Suemune H. Helical-screw directions of diastereoisomeric cyclic α-amino acid oligomers. Org. Lett. 2009; 11: 1135-1137.
24. 4/L-Val[L-(αMe)Val] in the crystal state. Biopolymers 1998; 46: 433-443.
25. Demizu Y, Yamagata N, Sato Y, Doi M, Tanaka M, Okuda H, Kurihara M. Controlling the helical screw sense of peptides with C-terminal L-valine. J. Pept. Sci. 2010; 16: 153-158.
26. Oba M, Demizu Y, Yamagata N, Sato Y, Doi M, Tanaka M, Suemune H, Okuda H, Kurihara M. Solid-state conformation of diastereomeric -Pro-Pro- sequences. Tetrahedron 2010; 66: 2293-2296.
27. Demizu Y, Tanaka M, Doi M, Kurihara M, Okuda H, Suemune H. Conformations of peptides containing a chiral cyclic α, α-disubstituted α-amino acid within the sequence of Aib residues. J. Pept. Sci. 2010; 16: 621-626.
28. 10-helix and α-helix of short peptides in the solid state. Chem. Pharm. Bull. 2007; 55: 840-842.
29. Demizu Y, Doi M, Sato Y, Tanaka M, Okuda H, Kurihara M. Three-dimensional control of diastereomeric Leu-Leu-Aib-Leu-Leu-Aib sequences in the solid state. J. Org. Chem. 2010; 75: 5234-5239.
30. Nagano M, Doi M, Kurihara M, Suemune H, Tanaka M. Stabilized α-helix-catalyzed enantioselective epoxidation of α, β-unsaturated ketones. Org. Lett. 2010; 12: 3564-3566.
31. Sheldrick GM. SHELXL 97. Program for Crystal Structure Refinement. University of Göttingen: Göttingen, 1997.
32. Beurskens PT, Admiraal G, Beurskens G, Bosman WP, de Gelder R, Israel R, Smits JMM. The DIRDIF-99 program system, technical report of the crystallography laboratory, University of Nijmegen: The Netherlands, 1994.
33. CCDC-770819 for 1, CCDC-770820 for 2, CCDC-770821 for 3, and CCDC-770822 for 4 contain the supplementary crystallographic data for this paper. These data can be obtained free of charge it via (or from the Cambridge Crystallographic Data Centre, 12, Union Road, Cambridge CB2 1EZ, UK; fax: (+44) 1223-336-033; or deposit@ccdc.cam.ac.uk).
34. 10-helix. Trends Biochem. Sci. 2000; 16: 350-353.
35. Steiner T. Donor and acceptor strengths in CHO hydrogen bonds quantified from crystallographic data of small solvent molecules. New J. Chem. 1998; 22: 1099-1103.
36. Desiraju GR. The CHO hydrogen bond in crystals. Acc. Chem. Res. 1991; 24: 290-296.
37. Venkatachalam CM. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers 1968; 6: 1425-1436.
38. Inai Y, Ishida Y, Tagawa K, Takasu A, Hirabayashi T. Noncovalent domino effect on helical screw sense of chiral peptides possessing C-terminal chiral residue. J. Am. Chem. Soc. 2002; 124: 2466-2473.
39. 88. J. Am. Chem. Soc. 2010; 132: 4548-4549.