Conformations of peptides containing a chiral cyclic α, α-disubstituted α-amino acid within the sequence of Aib residues

Journal of Peptide Science

Volumn 16, Issue 11, 2010, Pages 621-626

  Demizu, Yosuke ^a,b   Tanaka, Masakazu ^c   Doi, Mitsunobu ^d   Kurihara, Masaaki ^b   Okuda, Haruhiro ^b   Suemune, Hiroshi ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^c NAGASAKI UNIVERSITY   (Japan)

^d OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

aminoisobutyric acid; 310 helix; Chiral cyclic , disubstituted amino acid; Conformational analysis; X ray diffraction

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; ALPHA AMINO ACID;

ARTICLE; CHEMICAL ANALYSIS; CHIRALITY; INFRARED SPECTROMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON NUCLEAR MAGNETIC RESONANCE; SYNTHESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; AMINOISOBUTYRIC ACIDS; CRYSTALLOGRAPHY, X-RAY; CYCLOLEUCINE; HYDROGEN BONDING; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 78650446277     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1273     Document Type: Article

References (24)

1. Branden C, Tooze J. Introduction to Protein Structure. Garland: New York, 1991; 1-131.
2. Royo S, Borggraeve WMD, Peggion C, Formaggio F, Crisma M, Jiménez AI, Cativiela C, Toniolo C. Turn and helical peptide handedness governed exclusively by side-chain chiral centers. J. Am. Chem. Soc. 2005; 127: 2036-2037.
3. 4/L-Val[L-(αMe)Val] in solution. J. Chem. Soc. Perkin Trans. 2 1998; 1651-1657.
4. 4/L-Val[L-(αMe)Val] in the crystal state. Biopolymers 1998; 46: 433-443.
5. 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.
6. 10-helical peptide. J. Am. Chem. Soc. 2008; 130: 12266-12267.
7. 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.
8. 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.
9. 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.
10. 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.
11. 5-NHMe. Biopolymers 1986; 25: 1635-1644.
12. 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.
13. Karle IL, Balaram P. α-Helical peptide molecules containing Aib residues. Biochemistry 1990; 29: 6747-6756.
14. Heimgartner H. Synthons for α, α-disubstituted α-amino acids in heterocycle and peptide synthesis. Angew. Chem. Int. Ed. 1991; 30: 238-264.
15. 10-helix: from 3D-structural studies to applications as templates. J. Incl. Phenom. Macrocycl. Chem. 2005; 51: 121-136.
16. Oba M, Tanaka M, Kurihara M, Suemune H. Conformation of peptides containing (S)-α-ethylleucine. Helv. Chim. Acta 2002; 85: 3197-3218.
17. Altomare A, Cascarano G, Giacovazzo C, Guagliardi A, Burla M, Polidori G, Camalli M. Sir 92. J. Appl. Crystallogr. 1994; 27: 435.
18. Sheldrick GM. SHELXL 97. Program for Crystal Structure Refinement. University of Göttingen: Göttingen, 1997.
19. 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.
20. CCDC-763135 and -763137 contain the supplementary crystallographic data for this paper. These data can be obtained free of charge 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).
21. 10- and α-helixes and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy. Biochemistry 1991; 30: 6541-6548.
22. 10-helical structure of peptide foldamer composed of diverse α-ethylated α, α-disubstituted α-amino acids. Chem. Eur. J. 2003; 9: 3082-3090.
23. 10-helix. J. Am. Chem. Soc. 1996; 118: 2744-2745.
24. 10-helices in proteins. Proteins: Structure Funct. Genet. 2002; 48: 571-579.