Functionalization of peptides and proteins by Mukaiyama aldol reaction

Journal of the American Chemical Society

Volumn 132, Issue 28, 2010, Pages 9546-9548

  Alam, Jenefer ^a,b   Keller, Thomas H ^b   Loh, Teck Peng ^a  

^a Nanyang Technological University   (Singapore)

^b NOVARTIS INSTITUTE FOR TROPICAL DISEASES   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

C-C BOND FORMATION; CATALYST-FREE; CHEMICAL BIOLOGY; ENVIRONMENTALLY FRIENDLY CONDITION; FUNCTIONALIZATIONS; MUKAIYAMA ALDOL REACTION; N-TERMINALS; PROTEIN LABELING; SITE SELECTIVE;

ALDEHYDES; CONDENSATION REACTIONS; FUNCTIONAL GROUPS; PEPTIDES;

CHEMICAL BONDS;

ALDEHYDE DERIVATIVE; CARBON; MYOGLOBIN; WATER;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYST; CHEMICAL BOND; CIRCULAR DICHROISM; CONTROLLED STUDY; ELECTROSPRAY MASS SPECTROMETRY; ISOTOPE LABELING; MUKAIYAMA REACTION; PROTEIN FUNCTIONALIZATION; PROTEIN MODIFICATION; ULTRAVIOLET SPECTROSCOPY; VELOCITY;

ALDEHYDES; CHROMATOGRAPHY, LIQUID; KINETICS; PEPTIDES; PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 77954653618     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja102733a     Document Type: Article

References (18)

1. Sletten, E. M. and Bertozzi, C. R. Angew. Chem., Int. Ed. 2009, 48, 6974-6998
2. Link, A. J., Mock, M. L., and Tirrell, D. A. Curr. Opin. Biotechnol. 2003, 14, 603-609
3. Wang, L. and Schultz, P. G. Angew. Chem., Int. Ed. 2005, 44, 34-66
4. Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., Joshi, N. S., and Francis, M. B. Angew. Chem., Int. Ed. 2006, 45, 5307-5311
5. Kalia, J. and Raines, R. T. Curr. Org. Chem. 2010, 14, 138-147
6. Sasaki, T., Kodama, K., Hiroaki, S., Fukuzawa, S., and Tachibana, K. Bioorg. Med. Chem. Lett. 2008, 18, 4550-4553
7. Loh, T. P., Feng, L. C., and Wei, L. L. Tetrahedron 2000, 56, 7309-7312
8. Geoghegan, K. F. and Stroh, J. G. Bioconjugate Chem. 1992, 3, 138-146
9. Hong, S. H. and Grubbs, R. H. J. Am. Chem. Soc. 2006, 128, 3508-3509
10. Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., and Davis, B. G. I. J. Am. Chem. Soc. 2008, 130, 9642-9643
11. Wang, Q., Chan, T. R., Hilgraf, R., Fokin, V. V., Sharpless, K. B., and Finn, M. G. J. Am. Chem. Soc. 2003, 125, 3192-3193
12. Beatty, K. E., Xie, F., Wang, Q., and Tirrell, D. A. J. Am. Chem. Soc. 2005, 127, 14150-14151
13. Parveen, S. and Sahoo, S. K. Clin. Pharmacokinet. 2006, 45, 965-988
14. Refer to the Supporting Information.
15. Chi, E. Y., Krishnan, S., Randolph, T. W., and Carpenter, J. F. Pharm. Res. 2003, 20, 1325-1336
16. Khmelnitsky, Y. L., Mozhaev, V. V., Belova, A. B., Sergeeva, M. V., and Martinek, K. Eur. J. Biochem. 1991, 198, 31-41
17. The optimized conditions for the Mukaiyama aldol reaction with myoglobin use 190 equivalents of silyl ketene acetal. The greater efficiency of the reaction relative to that of the peptides (Table 1) is likely due to the greater excess of ketene acetal. We have shown that the yield of the Mukaiyama aldol reaction with peptides can be improved if a larger excess of ketene acetal is used (see the experimental conditions and comments in the Supporting Information).
18. Dunford, H. B. In Peroxidases in Chemistry and Biology; Everse, J., Everse, K. E., and Grisham, M. B., Eds.; CRC Press: Boca Raton, FL, 1991; Vol. II, pp 1 - 24.