Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-trifluoroleucine and (2S,4S)-5,5,5-trifluoroleucine

ChemBioChem

Volumn 10, Issue 1, 2009, Pages 84-86

  Montclare, Jin Kim ^b   Son, Soojin ^a   Clark, Ginevra A ^c   Kumar, Krishna ^c,d   Tirrell, David A ^a  

^a California Institute of Technology   (United States)

^b POLYTECHNIC UNIVERSITY   (United States)

^c TUFTS UNIVERSITY   (United States)

^d TUFTS MEDICAL CENTER   (United States)

Author keywords

Biosynthesis; Noncanonical amino acids; Protein engineering; Stereochemical control; Thermostability

Indexed keywords

5,5,5 TRIFLUOROLEUCINE; AMINO ACID DERIVATIVE; HETERODIMER; HOMODIMER; LEUCINE TRANSFER RNA LIGASE; UNCLASSIFIED DRUG; 5',5',5' TRIFLUOROLEUCINE; 5',5',5'-TRIFLUOROLEUCINE; DRUG DERIVATIVE; LEUCINE; PEPTIDE;

AMINO ACID ANALYSIS; ARTICLE; CIRCULAR DICHROISM; FLUORINATION; IN VITRO STUDY; INCUBATION TIME; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; RNA TRANSLATION; SPECTROSCOPY; STEREOCHEMISTRY; STEREOISOMERISM; STRUCTURE ANALYSIS; THERMOSTABILITY; AMINO ACID SEQUENCE; CHEMISTRY; DIMERIZATION; ESCHERICHIA COLI; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; TEMPERATURE;

AMINO ACID SEQUENCE; DIMERIZATION; ESCHERICHIA COLI; KINETICS; LEUCINE; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS; PEPTIDES; PROTEIN STABILITY; STEREOISOMERISM; TEMPERATURE;

EID: 59649103752     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200800164     Document Type: Article

References (35)

1. a) A. J. Link, M. L. Mock, D. A. Tirrell, Curr. Opin. Biotechnol. 2003, 14, 603-609;
2. b) R. E. Connor, D. A. Tirrrell, Polym. Rev. 2007, 47, 9-28; N. Budisa, Angew. Chem. 2004, 116, 6586-6624; Angew. Chem. Int. Ed. 2004, 43, 6426-6463.
3. a) T. L. Hendrickson, V. de Crecy-Lagard, P. Schimmel, Annu. Rev. Biochem. 2004, 73, 147-176;
4. b) L. Wang, P. G. Schultz, Angew. Chem. 2005, 117, 34-68; Angew. Chem. Int. Ed. 2005, 44, 34-66.
5. a) B. Bilgicer, K. Kumar, J. Chem. Educ. 2003, 80, 1275-1281;
6. b) C. Jäckel, B. Koksch, Eur. J. Org. Chem. 2005, 4483-4503.
7. O. M. Rennert, H. S. Anker, Biochemistry 1963, 2, 471-476.
8. E. Neil, G. Marsh, Chem. Biol. 2000, 7, R153-R157.
9. Y. Tang, G. Ghirlanda, W. A. Petka, T. Nakajima, W. F. DeGrado, D. A. Tirrell, Angew. Chem. 2001, 113, 1542-1544; Angew. Chem. Int. Ed. 2001, 40, 1494-1496.
10. B. Bilgicer, A. Fichera, K. Kumar, J. Am. Chem. Soc. 2001, 123, 4393-4399.
11. Y. Tang, G. Ghirlanda, N. Vaidehi, J. Kua, D. T. Mainz, W. A. Goddard, W. F. DeGrado, D. A. Tirrell, Biochemistry 2001, 40, 2790-2796.
12. a) T. Panchenko, W. W. Zhu, J. K. Montclare, Biotechnol. Bioeng. 2006, 94, 921-930;
13. b) J. K. Montclare, D. A. Tirrell, Angew. Chem. 2006, 118, 4630-4633; Angew. Chem. Int. Ed. 2006, 45, 4518-4521; c) N. Voloshchuk, M. X. Lee, I. C. Tanrikulu, J. K. Montclare, Bioorg. Med. Chem. Lett. 2007, 17, 5907-5911.
14. S. Cusack, A. Yaremchuk, M. Tukalo, EMBO J. 2000, 19, 2351-2361.
15. R. B. Loftfield, Biochem. J. 1963, 89, 82-92.
16. J. Flossdorf, M. R. Kula, Eur. J. Biochem. 1973, 36, 534-540.
17. R. B. Loftfield, E. A. Eigner, Biochim. Biophys. Acta 1966, 130, 426-448.
18. H. Polet, M. E. Conrad, Proc. Soc. Exp. Biol. Med. 1969, 130, 581-586.
19. M. L. Mock, T. Michon, J. C. M. van Hest, D. A. Tirrell, ChemBioChem 2006, 7, 83-87.
20. P. Wang, A. Fichera, K. Kumar, D. A. Tirrell, Angew. Chem. 2004, 116, 3750-3752; Angew. Chem. Int. Ed. 2004, 43, 3664-3666.
21. E. K. O'Shea, J. D. Klemm, P. S. Kim, T. Alber, Science 1991, 254, 539-544.
22. W. A. Petka, J. L. Harden, K. P. McGrath, D. Wirtz, D. A. Tirrell, Science 1998, 281, 389-392.
23. a) Y. Tang, D. A. Tirrell, J. Am. Chem. Soc. 2001, 123, 11089-11090;
24. b) S. Son, I. C. Tanrikulu, D. A. Tirrell, ChemBioChem 2006, 7, 1251-1257.
25. a) C. Jäckel, W. Seufert, S. Thust, B. Koksch, ChemBioChem 2004, 5, 717-720;
26. b) C. Jäckel, M. Salwiczek, B. Koksch, Angew. Chem. 2006, 118, 4305-4309; Angew. Chem. Int. Ed. 2006, 45, 4198-4203.
27. K. L. Kiick, R. Weberskirch, D. A. Tirrell, FEBS Lett. 2001, 502, 25-30.
28. The software CDNN was employed to calculate the percent helical content from the CD wavelength data. This program is available at: http:// bioinformatik.biochemtech.uni-halle.de/
29. Protein concentrations were determined by using the Bradford assay (BioRad, Hercules, CA, USA).
30. a) K. H. Lee, H. Y. Lee, M. M. Slutsky, J. T. Anderson, E. N. G. Marsh, Biochemistry 2004, 43, 16277-16284;
31. b) H. Y. Lee, K. H. Lee, H. M. Al-Hashimi, E. N. G. Marsh, J. Am. Chem. Soc. 2006, 128, 337-343;
32. c) L. M. Gottler, R. de La Salud-Bea, E. N. G. Marsh, Biochemistry 2008, 47, 4484-4490.
33. X. Xing, A. Fichera, K. Kumar, J. Org. Chem. 2002, 67, 1722-1725.
34. K. Weinges, E. Kromm, Liebigs Ann. Chem. 1985, 90-102.
35. S. Yamada, C. Hongo, R. Yoshioka, I. Chibata, J. Org. Chem. 1983, 48, 843-846.