Collect. Czech. Chem. Commun.
2002, 67, 1533-1559
https://doi.org/10.1135/cccc20021533
Peptide Synthesis with α-(Difluoromethyl)-Substituted α-Amino Acids
Thomas Michela, Beate Kokschb, Sergei N. Osipovc, Alexander S. Golubevc, Joachim Sielerd and Klaus Burgerb,*
a Jenapharm, Otto-Schott-Strasse 15, D-07745 Jena, Germany
b Department of Organic Chemistry, University of Leipzig, Johannisallee 29, D-04103 Leipzig, Germany
c Institute of Organoelement Compounds, Russian Academy of Sciences, Vavilov str. 28, GSP-1, V-334, 117813 Moscow, Russia
d Department of Inorganic Chemistry, University of Leipzig, Linnéstrasse 3, D-04103 Leipzig, Germany
References
1a. Macromolecules 1991, 24, 4004.
< C., Benedetti E.: https://doi.org/10.1021/ma00014a006>
1b. Int. J. Pept. Protein Res. 1988, 32, 544.
< G. R., Clark J. D., Dundar J. B., Jr., Smith G. D., Zabrocki J., Redlinski A. S., Leplavy M. T.: https://doi.org/10.1111/j.1399-3011.1988.tb01386.x>
2a. ACS Symp. Ser. 1996, 639, 42.
< B., Sewald N., Jakubke H.-D., Burger K.: https://doi.org/10.1021/bk-1996-0639.ch003>
2b. Sewald N., Burger K. in: Fluorine-Containing Amino Acids: Synthesis and Properties (V. P. Kukhar and V. A. Soloshonok, Eds), p. 139. John Wiley & Sons, Chichester 1995.
3. J. Fluorine Chem. 1994, 69, 199.
< V. P.: https://doi.org/10.1016/0022-1139(94)03131-2>
4a. Shimohigashi Y. in: Opioid Peptides, Medicinal Chemistry (R. S. Rapaka, G. Barnett and R. L. Hawks, Eds), p. 65. NIDA Research Monograph 69, NIDA-DHHS, U.S. Government Printing Office, Rockville 1986.
4b. Biopolymers 1997, 43, 219.
< V. J., Li G., Haskell-Luevano C., Shenderovich M.: https://doi.org/10.1002/(SICI)1097-0282(1997)43:3<219::AID-BIP3>3.0.CO;2-Y>
5. Tetrahedron Lett. 2000, 923.
< T., Nose T., Matsushima A., Okada K., Asai D., Yamauchi Y., Shirasu N., Honda T., Shigehiro, Shimohigashi Y.: https://doi.org/10.1016/S0040-4039(99)02191-7>
6. Tetrahedron 1995, 51, 8665.
< M., Umezawa Y., Hirota M., Takeuchi Y.: https://doi.org/10.1016/0040-4020(94)01066-9>
7a. J. Org. Chem. 1995, 60, 1626.
< J. A., McLoughlin J. I.: https://doi.org/10.1021/jo00111a021>
7b. Angew. Chem. 1999, 111, 3105.
< W., Melandri S., Moreschini P., Favero P. G.: https://doi.org/10.1002/(SICI)1521-3757(19991004)111:19<3105::AID-ANGE3105>3.0.CO;2-O>
8a. Tetrahedron 1996, 52, 12613.
< J. A. K., Hoy V. J., O’Hagan D., Smith G. T.: https://doi.org/10.1016/0040-4020(96)00749-1>
8b. Chem. Commun. 1997, 645.
< D., Rzepa H. S.: https://doi.org/10.1039/a604140j>
8c. Chem. Eur. 1997, 3, 89.
< J. F., Taylor R.: https://doi.org/10.1002/chem.19970030115>
9a. Kontakte Darmstadt 1988, 1, 17.
S., Bonitz D., Gassen G., Papandrikopoulou A., Weber M., Weiler H., Wollny E.:
9b. J. Mol. Struct. 1995, 339, 57.
< K., Hofmann H.-J.: https://doi.org/10.1016/0166-1280(95)04195-C>
9c. J. Peptide Sci. 1997, 3, 157.
< B., Sewald N., Hofmann H.-J., Burger K., Jakubke H.-D.: https://doi.org/10.1002/(SICI)1099-1387(199705)3:3<157::AID-PSC94>3.0.CO;2-W>
9d. Koksch B.: Ph.D. Thesis. University of Leipzig, Leipzig 1995.
10a. For a review see: Gerig J. T. in: Biological Magnetic Resonance (L. S. Berliner and J. Reuben, Eds), Vol. 1, p. 139. Plenum Press, New York 1978.
10b. Methods Enzymol. 1989, 177, 3.
< J. T.: https://doi.org/10.1016/0076-6879(89)77003-8>
10c. Biopolymers 1991, 31, 845.
< D. H., Gerig J. T.: https://doi.org/10.1002/bip.360310705>
10d. J. Org. Chem. 1992, 57, 5630.
< M., Patel H. H., Scheuring J., Bacher A.: https://doi.org/10.1021/jo00047a015>
11a. Z. Naturforsch., B: Chem. Sci. 1991, 46, 361.
< K., Höss E., Gaa K., Sewald N., Schierlinger C.: https://doi.org/10.1515/znb-1991-0316>
11b. Chem.-Ztg. 1991, 114, 101.
K., Gaa K.:
11c. Synthesis 1990, 115.
< K., Sewald N., https://doi.org/10.1055/s-1990-26803>
11d. Bull. Acad. Sci. USSR, Chem. Sect. (Engl.) 1986, 1256.
S. N., Chkanikov N. D., Kolomiets A. F., Fokin A. V.:
11e. Russ. Chem. Rev. 1992, 61, 798.
< S. N., Kolomiets A. F., Fokin A. V.: https://doi.org/10.1070/RC1992v061n08ABEH000999>
12a. Synlett 1994, 751.
< K., Hollweck W.: https://doi.org/10.1055/s-1994-22997>
12b. Amino Acids 1995, 8, 187.
< N., Hollweck W., Mütze K., Schierlinger C., Seymour L. C., Gaa K., Burger K., Koksch B., Jakubke H.-D.: https://doi.org/10.1007/BF00806491>
12c. J. Prakt. Chem. 1995, 337, 391.
< W., Burger K.: https://doi.org/10.1002/prac.19953370183>
12d. Liebigs Ann. Chem. 1997, 2549.
< W., Sewald N., Michel T., Burger K.: https://doi.org/10.1002/jlac.199719971219>
13. Tetrahedron: Asymmetry 1994, 5, 1051.
< N., Seymour L. C., Burger K., Osipov S. N., Kolomiets A. F., Fokin A. V.: https://doi.org/10.1016/0957-4166(94)80055-3>
13b. Tetrahedron: Asymmetry 1994, 5, 2009.
< P., Capelli S., Meille S. V., Viani F., Zanda M., Kukhar V. P., Soloshonok V. A.: https://doi.org/10.1016/S0957-4166(00)86276-X>
14. J. Am. Chem. Soc. 1992, 114, 3535.
< D. G., Lauhon C. T., Nyfeler R., Fässler A., Bartlett P. A.: https://doi.org/10.1021/ja00035a058>
15. J. Org. Chem. 1996, 61, 7521.
< S. N., Golubev A. S., Sewald N., Michel T., Kolomiets A. F., Fokin A. V., Burger K.: https://doi.org/10.1021/jo9608331>
16. J. Prakt. Chem. 1991, 325, 321.
K., Mütze K., Hollweck W., Koksch B., Kuhl P., Jakubke H.-D., Riede J., Schier A.:
17. Hollweck W.: Ph.D. Thesis. Technical University Munich, Munich 1994.
18a. Int. J. Pept. Protein Res. 1993, 41, 587.
< N. L., Lee Y. C., Chen F. M. F.: https://doi.org/10.1111/j.1399-3011.1993.tb00481.x>
18b. Michel T.: Ph.D. Thesis. University of Leipzig, Leipzig 1998.
19. Can. J. Chem. 1984, 62, 1335.
N. L., Chen F. M. F.:
20. For a review on the origin and nature of the gem-dimethyl effect, see: Synthesis 1995, 1205.
< P. G., Weller D. J.: https://doi.org/10.1055/s-1995-4099>
21a. Int. J. Pept. Protein Res. 1981, 18, 459.
< S. S., Tam J. P., Wang B. S. H., Merrifield R. B.: https://doi.org/10.1111/j.1399-3011.1981.tb03007.x>
21b. Int. J. Pept. Protein Res. 1994, 44, 399.
< N. L.: https://doi.org/10.1111/j.1399-3011.1994.tb01025.x>
21c. Anal. Chem. 1996, 68, 2361.
< D., Wiesmüller K. H., Scholl D., Kuhn R.: https://doi.org/10.1021/ac9511511>
22. Tetrahedron Lett. 1996, 39, 241.
< L. A., Ionescu D., El-Faham A., Henklein P., Wenschuh H., Beyermann M., Bienert M.: https://doi.org/10.1016/S0040-4039(97)10504-4>
23. J. Org. Chem. 1991, 56, 2635.
< L. A., Chao H. G., Beyermann M., Bienert M.: https://doi.org/10.1021/jo00008a012>
24a. For a review on amino acid halides see: J. Org. Chem. 1996, 61, 268.
< L. A., Beyermann M., Wenschuh H., Bienert M.: https://doi.org/10.1021/jo950912x>
24b. J. Org. Chem. 1991, 56, 2635.
< L. A., Chao H. G., Beyermann M., Bienert M.: https://doi.org/10.1021/jo00008a012>
25a. Chromatographia 1987, 23, 83.
< S., Bayer E., Frank H.: https://doi.org/10.1007/BF02312877>
25b. Angew. Chem. 1957, 69, 640.
< E., Reuter K. H., Born J.: https://doi.org/10.1002/ange.19570692009>
25c. J. Chromatogr. 1968, 37, 398.
< C. W., Zumwalt R. W., Wall L. L.: https://doi.org/10.1016/S0021-9673(01)99136-8>
26. J. Chromatogr. Sci. 1977, 9, 141.
H., Nicholson G. J., Bayer E.:
27. We are grateful to the Peptide Service Group of the Max Planck Institute for Infection Biology for performing the racemization test.
28. J. Org. Chem. 1990, 112, 9651.
L. A., Sadat-Aalaee D., Chao H. G., DeSelms R. H.:
29. Lett. Pept. Sci. 1995, 2, 285.
< C., Wenschuh H., Beyermann M., Forner K., Carpino L. A., Bienert M.: https://doi.org/10.1007/BF00142240>
30. J. Org. Chem. 1990, 112, 2611.
L. A., Sadat-Aalaee D., Chao H. G., DeSelms R. H.:
31a. J. Org. Chem. 1986, 51, 3732.
< L. A., Cohen B. J., Stephens K. E. J., Sadat-Aalaee S. Y., Tien H.-J., Langridge D. C.: https://doi.org/10.1021/jo00369a042>
31b. J. Org. Chem. 1991, 56, 2635.
< L. A., Chao H. G., Beyermann M., Bienert M.: https://doi.org/10.1021/jo00008a012>
32. J. Am. Chem. Soc. 1995, 117, 5401.
A., Carpino L. A.:
33. Acta Crystallogr., Sect. A: Cryst. Phys., Diffr., Theor. Gen. Crystallogr. 1977, 33, 216.
< A., Perini B.: https://doi.org/10.1107/S0567739477000448>
34. Koksch B., Jakubke H.-D., Wenschuh H., Dietmeier K., Starostin A., Woolley A., Dathe M., Müller G., Gussmann M., Hofmann H.-J., Burger K.: Peptides 1998, Proc. 25th Eur. Pept. Symp. (S. Bajusz and F. Hudecz, Eds), p. 476. ESCOM, Leiden 1999.
35. Sheldrick G. M.: SADABS, Program for Empirical Absorption Correction. University of Göttingen, Göttingen 1996.
36. Sheldrick G. M.: SHELXS97, Program for Crystal Structure Solution and Refinement. University of Göttingen, Göttingen 1997.