Novel consecutive β- and γ-turn mimetics composed of α-aminooxy tripeptides

Organic Letters

Volumn 5, Issue 7, 2003, Pages 971-974

  Baek, Bong Hyeon ^a   Lee, Myung Ryul ^a   Kim, Kwang Yon ^a   Cho, Ung In ^a   Boo, Doo Wan ^a   Shin, Injae ^a  

^a Yonsei University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

TRIPEPTIDE DERIVATIVE; PEPTIDE;

AB INITIO CALCULATION; ARTICLE; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; MOLECULAR MIMICRY; PROTEIN SECONDARY STRUCTURE; SYNTHESIS;

DIMERIZATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR MIMICRY; MOLECULAR STRUCTURE; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0042730264     PISSN: 15237060     EISSN: None     Source Type: Journal    
DOI: 10.1021/ol020233q     Document Type: Article

References (24)

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5. Peptides forming γ-turn conformation: (a) Levian-Teitelbaum, D.; Kolodny, N.; Chorev, M.; Selinger, Z.; Gilon, C. Biopolymers 1989, 28, 51. (b) Raghothama, S.; Ramakrishnan, C.; Balasubramanian, D.; Balaram, P. Biopolymers 1989, 28, 573. (c) Milon, A.; Miyazawa, T.; Higashijima, T. Biochemistry 1990, 29, 65. (d) Walse, B.; Kihlberg, J.; Drakenberg, T. Eur. J. Biochem. 1998, 252, 428.
6. Peptides forming γ-turn conformation: (a) Levian-Teitelbaum, D.; Kolodny, N.; Chorev, M.; Selinger, Z.; Gilon, C. Biopolymers 1989, 28, 51. (b) Raghothama, S.; Ramakrishnan, C.; Balasubramanian, D.; Balaram, P. Biopolymers 1989, 28, 573. (c) Milon, A.; Miyazawa, T.; Higashijima, T. Biochemistry 1990, 29, 65. (d) Walse, B.; Kihlberg, J.; Drakenberg, T. Eur. J. Biochem. 1998, 252, 428.
7. Peptides forming γ-turn conformation: (a) Levian-Teitelbaum, D.; Kolodny, N.; Chorev, M.; Selinger, Z.; Gilon, C. Biopolymers 1989, 28, 51. (b) Raghothama, S.; Ramakrishnan, C.; Balasubramanian, D.; Balaram, P. Biopolymers 1989, 28, 573. (c) Milon, A.; Miyazawa, T.; Higashijima, T. Biochemistry 1990, 29, 65. (d) Walse, B.; Kihlberg, J.; Drakenberg, T. Eur. J. Biochem. 1998, 252, 428.
8. Peptides forming γ-turn conformation: (a) Levian-Teitelbaum, D.; Kolodny, N.; Chorev, M.; Selinger, Z.; Gilon, C. Biopolymers 1989, 28, 51. (b) Raghothama, S.; Ramakrishnan, C.; Balasubramanian, D.; Balaram, P. Biopolymers 1989, 28, 573. (c) Milon, A.; Miyazawa, T.; Higashijima, T. Biochemistry 1990, 29, 65. (d) Walse, B.; Kihlberg, J.; Drakenberg, T. Eur. J. Biochem. 1998, 252, 428.
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13. For γ-turn mimetics, see: (a) Schmidt, B.; Lindman, S.; Tong, W.; Lindeberg, G.; Gogoll, A.; Lai, Z.; Thörnwall, M.; Synnergren, B.; Nilsson, A.; Welch, C. J.; Sohtell, M.; Westerlund, C.; Nyberg, F.; Karlén, A.; Hallberg, A. J. Med. Chem. 1997, 40, 903. (b) Brickmann, K.; Yuan, Z.; Sethson, I.; Somfai, P.; Kihlberg, J. Chem. Eur. J. 1999, 5, 2241. (c) Jiménez, A. I.; Cativiela, C.; Marraud, M. Tetrahedron Lett. 2000, 41, 2000.
14. For γ-turn mimetics, see: (a) Schmidt, B.; Lindman, S.; Tong, W.; Lindeberg, G.; Gogoll, A.; Lai, Z.; Thörnwall, M.; Synnergren, B.; Nilsson, A.; Welch, C. J.; Sohtell, M.; Westerlund, C.; Nyberg, F.; Karlén, A.; Hallberg, A. J. Med. Chem. 1997, 40, 903. (b) Brickmann, K.; Yuan, Z.; Sethson, I.; Somfai, P.; Kihlberg, J. Chem. Eur. J. 1999, 5, 2241. (c) Jiménez, A. I.; Cativiela, C.; Marraud, M. Tetrahedron Lett. 2000, 41, 2000.
15. Yang, D.; Li, B.; Ng, F.-F.; Yan, Y.-L.; Qu, J.; Wu, Y.-D. J. Org. Chem. 2001, 66, 7303 and references are therein.
16. Because we liked to incorporate trimers into peptides to construct novel hybrid peptidomimetics with well-defined folded structures, we prepared the trimers containing a NHMe group instead of a NHOMe group at the C-terminus.
17. The six-membered cyclic α-aminooxy acid was called oxanipecotic acid instead of tetrahydro-1,2-oxazine-6-carboxylic acid because it is a nipecotic acid analogue. Shin, I.; Lee, M-r.; Lee, J.; Jung, M.; Lee, W.; Yoon, J. J. Org. Chem. 2000, 65, 7667.
18. The chemical shifts of hydrogen-bonded oxyamide NHs appear at > 10 ppm. See ref 8.
19. 3.
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22. 6. This indicates that the amide NH group is intramolecularly hydrogen-bonded to adopt eight-membered hydrogen bond as suggested by Yang and co-workers. See ref 8.
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24. The optimized structure has the lowest energy at 298 K among 12 conformers found along dihedral angles of backbone.