Acid-Stable Ester Linkers for the Solid-Phase Synthesis of Immobilized Peptides
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- Keywords
- diketopiperazines, esters, peptides, protecting groups, solid-phase synthesis,
- MeSH
- Esters chemical synthesis chemistry MeSH
- Immobilized Proteins chemical synthesis MeSH
- Indicators and Reagents chemical synthesis chemistry MeSH
- Peptides chemical synthesis MeSH
- Solid-Phase Synthesis Techniques methods MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Esters MeSH
- Immobilized Proteins MeSH
- Indicators and Reagents MeSH
- Peptides MeSH
A series of N-terminally Fmoc-protected linkers of the general formula Fmoc-X-CO-O-Y-COOH have been prepared, where X is -NH-CH2 -CH2 - or -p-(aminomethyl)phenyl- and Y is -(CH2 )n - (n is 1 or 4) or -p-(methyl)phenyl-. These linkers can easily be covalently attached via their C-terminal carboxyl group to a resin bearing a free amino group. After cleavage of the N-terminal Fmoc group, the linkers can be extended by standard solid-phase peptide synthesis techniques. These ester linkers are acid-stable and resistant to the base-mediated diketopiperazine formation that often occurs during the synthesis of ester-bound peptides; they are stable at neutral pH in aqueous buffers for days but can be effectively cleaved with 0.1 m NaOH or aq. ammonia within minutes or hours, respectively. These properties make these ester handles well suited for use as linkers for the solid-phase peptide synthesis of immobilized peptides when the stable on-resin immobilization of the peptides and the testing of their biological properties in aqueous buffers at neutral pH are necessary.
See more in PubMed
M. Wilchek, T. Miron, J. Kohn, Methods Enzymol. 1984, 104, 3-55;
M. Urh, D. Simpson, K. Zhao, Methods Enzymol. 2009, 463, 417-438.
J. Taunton, C. A. Hassig, S. L. Schreiber, Science 1996, 272, 408-411;
M. Collinsova, C. Castro, T. A. Garrow, A. Yiotakis, V. Dive, J. Jiracek, Chem. Biol. 2003, 10, 113-122;
S. E. Ong, X. Y. Li, M. Schenone, S. L. Schreiber, S. A. Carr, Methods Mol. Biol. 2012, 803, 129-140.
K. S. Lam, M. Lebl, V. Krchnak, Chem. Rev. 1997, 97, 411-448;
R. W. Liu, X. C. Li, K. S. Lam, Curr. Opin. Chem. Biol. 2017, 38, 117-126;
T. Kodadek, P. J. McEnaney, Chem. Commun. 2016, 52, 6038-6059;
T. Kodadek, N. G. Paciaroni, M. Balzarini, P. Dickson, Chem. Commun. 2019, 55, 13330-13341;
Z. P. Gates, A. A. Vinogradov, A. J. Quartararo, A. Bandyopadhyay, Z.-N. Choo, E D. Evans, K. H. Halloran, A. J. Mijalis, S. K. Mong, M. D. Simon, E. A. Standley, E. D. Styduhar, S. Z. Tasker, F. Touti, J. M. Weber, J. L. Wilson, T. F. Jamison, B. L. Pentelute, Proc. Natl. Acad. Sci. USA 2018, 115, E5298-E5306;
P. Dickson, T. Kodadek, Org. Biomol. Chem. 2019, 17, 4676-4688;
T. M. Doran, P. Dickson, J. M. Ndungu, P. Ge, I. Suponitsky-Kroyter, H. An, T. Kodadek, Methods Enzymol. 2019, 622, 91-127.
M. Lebl, V. Krchnak, Methods Enzymol. 1997, 289, 336-392.
G. B. Fields, R. L. Noble, Int. J. Pept. Protein Res. 1990, 35, 161-214.
I. W. James, Tetrahedron 1999, 55, 4855-4946;
F. Guillier, D. Orain, M. Bradley, Chem. Rev. 2000, 100, 2091-2157.
R. J. T. Mikkelsen, K. E. Grier, K. T. Mortensen, T. E. Nielsen, K. Qvortrup, ACS Comb. Sci. 2018, 20, 377-399;
M. Rinnova, M. Novakova, V. Kasicka, J. Jiracek, J. Pept. Sci. 2000, 6, 355-365.
J. U. Peters, S. Blechert, Synlett 1997, 348-350.
M. Gongora-Benitez, J. Tulla-Puche, F. Albericio, Acs Comb Sci 2013, 15, 217-228;
N. Jung, M. Wiehn, S. Brase, Top. Curr. Chem. 2007, 278, 1-88.
E. Atherton, M. J. Gait, R. C. Sheppard, B. J. Williams, Bioorg. Chem. 1979, 8, 351-370;
A. M. Bray, N. J. Maeji, A. G. Jhingran, R. M. Valerio, Tetrahedron Lett. 1991, 32, 6163-6166;
A. M. Bray, A. G. Jhingran, R. M. Valerio, N. J. Maeji, J. Org. Chem. 1994, 59, 2197-2203;
S. C. Story, J. V. Aldrich, Int. J. Pept. Protein Res. 1992, 39, 87-92.
S. M. Dankwardt, Synlett 1998, 761-761;
B. Blankemeyermenge, M. Nimtz, R. Frank, Tetrahedron Lett. 1990, 31, 1701-1704.
J. W. van Nispen, J. P. Polderdijk, H. M. Greven, Recl. Trav. Chim. Pays-Bas 1985, 104, 99-100.
E. Atherton, N. L. Benoiton, E. Brown, R. C. Sheppard, B. J. Williams, J. Chem. Soc. Chem. Commun. 1981, 336-337;
P. Sieber, Tetrahedron Lett. 1987, 28, 6147-6150.
B. F. Gisin, R. B. Merrifield, J. Am. Chem. Soc. 1972, 94, 3102-3106.
R. M. Valerio, M. Benstead, A. M. Bray, R. A. Campbell, N. J. Maeji, Anal. Biochem. 1991, 197, 168-177.
J. Picha, B. Fabre, M. Budesinsky, J. Hajduch, M. Abdellaoui, J. Jiracek, Eur. J. Org. Chem. 2018, 5180-5192.
M. Rothe, J. Mazánek, Liebigs Ann. Chem. 1974, 439-459;
E. Giralt, R. Eritja, E. Pedroso, Tetrahedron Lett. 1981, 22, 3779-3782;
E. Pedroso, A. Grandas, M. A. Saralegui, E. Giralt, C. Granier, J. Vanrietschoten, Tetrahedron 1982, 38, 1183-1192;
E. Pedroso, A. Grandas, X. Delasheras, R. Eritja, E. Giralt, Tetrahedron Lett. 1986, 27, 743-746.
