Synthetic study of phosphopeptides related to heat shock protein FLSP27

Bioorganic and Medicinal Chemistry

Volumn 5, Issue 1, 1997, Pages 135-145

  Wakamiya, Tateaki ^a   Togashi, Ryusaku ^a   Nishida, Takatoshi ^a   Saruta, Kunio ^b   Yasuoka, Jun Ichi ^b   Kusumoto, Shoichi ^b   Aimoto, Saburo ^b   Kumagaye, Kumiko Yoshizawa ^c   Nakajima, Kiichiro ^c   Nagata, Kazuhiro ^d  

^a KINKI UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c Protein Research Foundation   (Japan)

^d KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; PHOSPHOPEPTIDE;

CONFERENCE PAPER; IN VITRO STUDY; PEPTIDE SYNTHESIS; REACTION ANALYSIS;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOPEPTIDES; SPECTROMETRY, MASS, FAST ATOM BOMBARDMENT;

EID: 0031013088     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(96)00208-8     Document Type: Conference Paper

References (50)

1. 1. Perich, J. W.; Johns, R. B. J. Org. Chem. 1983, 53, 4103; Aust. J. Chem. 1990, 43, 1609; 1991, 44, 397, 405, 1683.
2. 1. Perich, J. W.; Johns, R. B. J. Org. Chem. 1983, 53, 4103; Aust. J. Chem. 1990, 43, 1609; 1991, 44, 397, 405, 1683.
3. 1. Perich, J. W.; Johns, R. B. J. Org. Chem. 1983, 53, 4103; Aust. J. Chem. 1990, 43, 1609; 1991, 44, 397, 405, 1683.
4. 2. Perich, J. W.; Alewood, P. F.; Johns, R. B. Aust. J. Chem. 1991, 44, 233, 253; Perich, J. W.; Johns, R. B.; Reynolds, E. C. ibid 1992, 45, 385; Perich, J. W.; Kelly, D. P.; Reynolds, E. C. Int. J. Pept. Protein Res. 1992, 40, 81.
5. 2. Perich, J. W.; Alewood, P. F.; Johns, R. B. Aust. J. Chem. 1991, 44, 233, 253; Perich, J. W.; Johns, R. B.; Reynolds, E. C. ibid 1992, 45, 385; Perich, J. W.; Kelly, D. P.; Reynolds, E. C. Int. J. Pept. Protein Res. 1992, 40, 81.
6. 2. Perich, J. W.; Alewood, P. F.; Johns, R. B. Aust. J. Chem. 1991, 44, 233, 253; Perich, J. W.; Johns, R. B.; Reynolds, E. C. ibid 1992, 45, 385; Perich, J. W.; Kelly, D. P.; Reynolds, E. C. Int. J. Pept. Protein Res. 1992, 40, 81.
7. 3. Tsukamoto, M.; Kato, R.; Ishiguro, K.; Uchida, T.; Sato, K. Tetrahedron Lett. 1991, 32, 7083.
8. 4. Paquet, A.; Johns, M. Int. J. Pept. Protein Res. 1990, 36, 97; Paquet, A. ibid. 1992, 39, 82.
9. 4. Paquet, A.; Johns, M. Int. J. Pept. Protein Res. 1990, 36, 97; Paquet, A. ibid. 1992, 39, 82.
10. 5. Bannwarth, W.; Küng, E. Tetrahedron Lett. 1989, 30, 4219.
11. 6. Ueno, Y.; Suda, F.; Taya, Y.; Noyori, R.; Hayakawa, H.; Hata, T. Bioorg. Med. Chem. Lett. 1995, 5, 823.
12. 2 is restricted to peptides devoid of aromatic or sulfur-containing amino acids.
13. 8. Wakamiya, T.; Kawahara, M.; Kusumoto, S.; Imajoh-Ohmi, S.; Kanegasaki, S. In Peptide Chemistry 1991; Suzuki, A. Ed.; Protein Research Foundation: Osaka, 1992; pp 383-388.
14. 9. Wakamiya, T. Chem. Express 1992, 7, 577.
15. 10. Wakamiya, T.; Saruta, K.; Kusumoto, S.; Nakajima, K.; Yoshizawa-Kumagaye, K.; Imajoh-Ohmi, S.; Kanegasaki, S. Chem. Lett. 1993, 1401.
16. 11. Wakamiya, T.; Saruta, K.; Kusumoto, S.; Aimoto, S.; Yoshizawa-Kumagaye, K.; Nakajima, K. In Peptide Chemistry 1993, Okada, Y. Ed. Protein Research Foundation, Osaka, 1994; pp 17-20.
17. 12. Sato, K.; Ishiguro, K.; Omori, A.; Kim, J. I.; Uchida, T.; Saruta, K.; Wakamiya, T. In Peptide Chemistry 1993, Okada, Y. Ed.; Protein Research Foundation: Osaka, 1994; pp 109-112.
18. 13. Wakamiya, T.; Saruta, K.; Yasuoka, J.; Kusumoto, S. Bull. Chem. Soc. Jpn 1995, 68, 2699.
19. 14. Abbreviations used: Boc, tert-butoxycarbonyl; BOP, O-(benzotriazol-1-yl)tris(dimethylamino)phosphonium hexafluorophosphate; tBu: tert-butyl; CHA, cyclohexylamine; mCPBA, m-chloroperbenzoic acid; DCC, dicyclohexylcarbodiimide; DCHA, dicyclohexylamine; DIEA, diisopropylethylamine; DMF, N,N-dimethylformamide; DTT, dithiothreitol; EDT, ethanedithiol; Fmoc, 9-fluorenylmethoxycarbonyl; HATU, O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate; HOBt, 1-hydroxybenzotriazole; MTB, methylthiobenzene (thioanisole); NMP, N-methylpyrrolidone; Pac, phenacyl; Pmc, 2,2,5,7,8-pentamethylchroman-6-sulfonyl; iPr, isopropyl; PSer, phosphoserine; Tce, 2,2,2-trichloroethyl; TFA, trifluoroacetic acid; TFMSA, trifluoromethanesulfonic acid; Trt, triphenylmethyl (trityl).
20. 15. Fujii, N.; Funakoshi, S.; Sasaki, T.; Yajima, H. Chem. Pharm. Bull. 1977, 25, 3096; Fujii, N.; Otaka, A.; Ikemura, O.; Hatano, M.; Okamachi, A.; Funakoshi, S.; Sakurai, M.; Shioiri, T.; Yajima, H. Chem. Pharm. Bull. 1987, 35, 3447.
21. 15. Fujii, N.; Funakoshi, S.; Sasaki, T.; Yajima, H. Chem. Pharm. Bull. 1977, 25, 3096; Fujii, N.; Otaka, A.; Ikemura, O.; Hatano, M.; Okamachi, A.; Funakoshi, S.; Sakurai, M.; Shioiri, T.; Yajima, H. Chem. Pharm. Bull. 1987, 35, 3447. A hard acid treatment for removing all of the protecting groups and cleaving of peptides from the resin is generally carried out at 0 °C for 2 h.
22. 23
23. 23
24. 23
25. 23
26. 18. A part of this work was presented at the 33rd Japanese Peptide Symposium, Sapporo, October, 1995, and published in Peptide Chemistry 1995; Nishi, N. Ed.; Protein Research Foundation: Osaka, 1996; pp 17-20.
27. 19. Otaka et al. have recently reported the use of O-(dimethyloxyphosphinyl) β-hydroxy α-amino acid derivatives as building blocks for the Boc strategy: Otaka, A.; Miyoshi, K.; Roller, P. R.; Burke, T.; Tamamura, H.; Fujii, N. J. Chem. Soc. Chem. Commun. 1995, 387. Although the methyl group is removable by trimethylsilyl trifluoromethanesulfonate (TMSOTf) and additives in TFA, two-step deprotection protocol is required for the complete removal.
28. 20. Lacombe, J.-M.; Andriamanampisoa, F.; Pavia, A. A. Int. J. Pept. Protein Res. 1990, 36, 275.
29. 21. Fmoc-strategy is basically applicable to the synthesis of phosphotyrosine-containing peptides. Kitas, E. A.; Knorr, R.; Trzeciak, A.; Bannwarth, W. Helv. Chim. Acta 1991, 74, 1314; Bannwarth, W.; Kitas, E. A. Helv. Chim. Acta 1992, 75, 707.
30. 21. Fmoc-strategy is basically applicable to the synthesis of phosphotyrosine-containing peptides. Kitas, E. A.; Knorr, R.; Trzeciak, A.; Bannwarth, W. Helv. Chim. Acta 1991, 74, 1314; Bannwarth, W.; Kitas, E. A. Helv. Chim. Acta 1992, 75, 707.
31. 8,10 Furthermore, we suggest that the phosphoamino acid residue at the N-terminus is generally stable during base treatment after de-tert-butoxycarbonylation; in fact, we have never observed a side reaction due to the β-elimination of phosphate at this stage.
32. 23. Wakamiya, T.; Saruta, K.; Yasuoka, J.; Kusumoto, S. Chem. Lett. 1994, 1099; In Peptide Chemistry 1994; Ohno, M. Ed.; Protein Research Foundation: Osaka, 1995; pp 5-8.
33. 23. Wakamiya, T.; Saruta, K.; Yasuoka, J.; Kusumoto, S. Chem. Lett. 1994, 1099; In Peptide Chemistry 1994; Ohno, M. Ed.; Protein Research Foundation: Osaka, 1995; pp 5-8.
34. 24. Gaestel, M.; Schröder, W.; Benndorf, R.; Lipmann, C.; Buchner, K.; Hucho, F.; Erdmann, V. A.; Bielka, H. J. Biol. Chem. 1991, 266, 14721.
35. 25. Landry, J.; Lambert, H.; Zhou, M.; Lavoie, J. N.; Hickey, E.; Weber, L. A.; Anderson, C. W. J. Biol. Chem. 1992, 267, 794.
36. 26. Dreef, C. E.; Elie, C. J. J.; Hoogerhout, P.; van der Marel, G. A.; van Boom, J. H. Tetrahedron Lett. 1988, 29, 6513.
37. 27. Perich, J. W.; Johns, R. B. Aust. J. Chem. 1990, 43, 1623; 1991, 44, 389.
38. 27. Perich, J. W.; Johns, R. B. Aust. J. Chem. 1990, 43, 1623; 1991, 44, 389.
39. 3 ester is susceptible to the β-elimination of phosphate or the addition of HOBt to the Dha residue.
40. 11 Comparison of this result with that obtained by the use of 5a or 8 is currently undertaken.
41. 30. Wakamiya, T.; Nishida, T.; Togashi, R.; Saruta, K.; Yasuoka, J.; Kusumoto, S. Bull. Chem. Soc. Jpn 1996, 69, 465. Compound 10 was obtained in an 81% yield through four reaction steps from Fmoc-Ser-OH as follows: (1) esterification with PacBr; (2) phosphite-forming reaction with amidite 13 (3) oxidation with mCPBA to give Fmoc-Ser[PO(O-Bzl)(OTce)]-OPac; and (4) simultaneous removal of the Pac and Tce groups with Zn/AcOH. Fmoc-Thr[PO(OBzl)(OH)]-OH (11) was similarly prepared in an 86% yield.
42. 3SnH, and (5) selective cleavage of one of the O-phosphono-protecting groups with NaI. The overall yield of each derivative isolated as Na salt was of 37% (10) and 38% (11), respectively.
43. 32. King, D. S.; Fields, C. G.; Fields, G. B. Int. J. Pept. Protein Res. 1990, 36, 255.
44. α-allyloxycarbonyl (Alloc) derivative of phosphoamino acids was recently reported: Lacombe, J. M.; Andriamanampisoa, F.; Pavia, A. A. Int. J. Pept. Protein Res. 1990, 36, 275; Shapiro, G.; Büchler, D.; Dalvit, C.; Fernandez, C.; Gomez-Lor, B.; Pombo, E.; Stauss, U.; Swoboda, R. Bioorg. Med. Chem. Lett. 1996, 6, 409. More examinations may be required to establish a methodology for synthesizing phosphopeptides based on the Alloc or combined Alloc-Fmoc strategy.
45. α-allyloxycarbonyl (Alloc) derivative of phosphoamino acids was recently reported: Lacombe, J. M.; Andriamanampisoa, F.; Pavia, A. A. Int. J. Pept. Protein Res. 1990, 36, 275; Shapiro, G.; Büchler, D.; Dalvit, C.; Fernandez, C.; Gomez-Lor, B.; Pombo, E.; Stauss, U.; Swoboda, R. Bioorg. Med. Chem. Lett. 1996, 6, 409. More examinations may be required to establish a methodology for synthesizing phosphopeptides based on the Alloc or combined Alloc-Fmoc strategy.
46. 34. Dittmer, J. D.; Lester, R. L. J. Lipid Res. 1964, 5, 126.
47. 35. Shimidzu, T.; Yamana, K.; Maikuma, S. Tetrahedron Lett. 1984, 25, 4237.
48. 36. Tanaka, T.; Tamatsukuri, S.; Ikehara, M. Tetrahedron Lett. 1986, 27, 199.
49. 37. The presence of conformers can be suggested.
50. 38. The synthesis was carried out according to the standard protocol which is originally specified in the system software. Therefore, the synthetic result of each peptide mentioned in the present study is reproducible so far as we use the same software.