Fluorous effect in proteins: De novo design and characterization of a four-α-helix bundle protein containing hexafluoroleucine

Biochemistry

Volumn 43, Issue 51, 2004, Pages 16277-16284

  Lee, Kyung Hoon ^a   Lee, Hyang Yeol ^a   Slutsky, Morris M ^a   Anderson, James T ^a,b   Marsh, E Neil G ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b ATHERSYS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; HYDROPHOBICITY; THERMODYNAMIC STABILITY;

GUANIDINIUM CHLORIDES; HYDROPHOBIC CORES; LEUCINE; PEPTIDES;

PROTEINS;

AMINO ACID DERIVATIVE; FLUORINE; GUANIDINE; LEUCINE; PEPTIDE; PROTEIN; VALINE;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; FLUORESCENCE; GEL FILTRATION CHROMATOGRAPHY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS; ULTRACENTRIFUGATION;

CIRCULAR DICHROISM; GUANIDINE; LEUCINE; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; STAINING AND LABELING;

EID: 11144320703     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049086p     Document Type: Article

References (33)

1. Link, A. J., Mock, M. L., and Tirrell, D. A. (2003) Non-canonical amino acids in protein engineering, Curr. Opin. Biotechnol. 14, 603-609.
2. Yoder, N. C., and Kumar, K. (2002) Fluorinated amino acids in protein design and engineering, Chem. Soc. Rev. 31, 335-341.
3. Cotton, G. J., and Muir, T. W. (1999) Peptide ligation and its application to protein engineering, Chem. Biol. 6, R247-R256.
4. Holmgren, S. K., Taylor, K. M., Bretscher, L. E., and Raines, R. T. (1998) Code for collagen's stability deciphered, Nature 392, 666-667.
5. Bilgicer, B., Xing, X. C., and Kumar, K. (2001) Programmed self-sorting of coiled coils with leucine and hexafluoroleucine cores, J. Am. Chem. Soc. 123, 11815-11816.
6. Bilgicer, B., Fichera, A., and Kumar, K. (2001) A coiled coil with a fluorous core, J. Am. Chem. Soc. 123, 4393-4399.
7. Tang, Y., and Tirrell, D. A. (2001) Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host, J. Am. Chem. Soc. 123, 11089-11090.
8. Niemz, A., and Tirrell, D. A. (2001) Self-association and membrane-binding behavior of melittins containing trifluoroleucine, J. Am. Chem. Soc. 123, 7407-7413.
9. Tang, Y., Ghirlanda, G., Petka, W. A., Nakajima, T., DeGrado, W. F., and Tirrell, D. A. (2001) Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability, Angew. Chem., Int. Ed. 40, 1494.
10. Tang, Y., Ghirlanda, G., Vaidehi, N., Kua, J., Mainz, D. T., Goddard, W. A., DeGrado, W. F., and Tirrell, D. A. (2001) Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine, Biochemistry 40, 2790-2796.
11. Bilgicer, B., and Kumar, K. (2002) Synthesis and thermodynamic characterization of self-sorting coiled coils, Tetrahedron 58, 4105-4112.
12. Marsh, E. N. G. (2000) Towards the non-stick egg: Designing fluorous proteins, Chem. Biol. 7, R153-R157.
13. Luo, Z. Y., Zhang, Q. S., Oderaotoshi, Y., and Curran, D. P. (2001) Fluorous mixture synthesis: A fluorous-tagging strategy for the synthesis and separation of mixtures of organic compounds, Science 291, 1766-1769.
14. Dobbs, A. P., and Kimberley, M. R. (2002) Fluorous phase chemistry: A new industrial technology, J. Fluorine Chem. 118, 3-17.
15. Horng, J.-C., and Raleigh, D. P. (2003) φ values beyond the ribosomally encoded amino acids: Kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein, J. Am. Chem. Soc. 125, 9286-9287.
16. Anderson, J. T., Toogood, P. L., and Marsh, E. N. G. (2002) A short and efficient synthesis of L-5,5,5,5′,5′,5′-hexafluoroleucine from W-Cbz-L-serine, Org. Lett. 4, 4281-4283.
17. Schnolzer, M., Alewood, P., Jones, A., Alewood, D., and Kent, S. B. H. (1992) In situ neutralization in Boc-chemistry solid-phase peptide synthesis: Rapid, high yield assembly of difficult sequences, Int. J. Pept. Protein Res. 40, 180-193.
18. Harding, S. E., Rowe, A. J., and Horton, H. C. (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science, The Royal Society of Chemistry, Cambridge, U.K.
19. Cohn, E. J., and Edsall, J. T. (1943) Proteins, Amino Acids and Peptides as Ions and Dipolar Ions, Reinhold, New York.
20. Boice, J. A., Dieckmann, G. R., DeGrado, W. F., and Fairman, R. (1996) Thermodynamic analysis of a designed three-stranded coiled coil, Biochemistry 35, 14480-14485.
21. Wilce, M. C. J., Aguilar, M. I., and Hearn, M. T. W. (1995) Physicochemical basis of amino acid hydrophobicity scales: Evaluation of 4 new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides, Anal. Chem. 67, 1210-1219.
22. Fauchere, J.-L., and Pliska, V. (1983) Hydrophobic parameters, π, of amino acid side chains from the partitioning of N-acetylamino acid amides, Eur. J. Med. Chem. 18, 369-375.
23. Oakley, M. G., and Hollenbeck, J. J. (2001) The design of antiparallel coiled coils, Curr. Opin. Struct. Biol. 11, 450-457.
24. DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., and Lombardi, A. (1999) De novo design and structural characterization of proteins and metalloproteins, Annu. Rev. Biochem. 68, 779-819.
25. Bryson, J. W., Betz, S. F., Lu, H. S., Suich, D. J., Zhou, H. X. X., Oneil, K. T., and Degrade, W. F. (1995) Protein design: A hierarchical approach, Science 270, 935-941.
26. Betz, S. F., and DeGrado, W. F. (1996) Controlling topology and native-like behavior of de novo-designed peptides: Design and characterization of antiparallel four-stranded coiled coils, Biochemistry 35, 6955-6962.
27. Harbury, P. B., Zhang, T., Kim, P. S., and Alber, T. (1993) A switch between 2-stranded, 3-stranded and 4-stranded coiled coils in GCN4 leucine zipper mutants, Science 262, 1401-1407.
28. Rohl, C. A., Chakrabartty, A., and Baldwin, R. L. (1996) Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol, Protein Sci. 5, 2623-2637.
29. Bondi, A. (1964) van der Waals volumes and radii, J. Phys. Chem. 68, 441-451.
30. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991) Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers 31, 119-128.
31. Betz, S. F., Raleigh, D. P., and Degrade, W. F. (1993) De-novo protein design: From molten globules to native-like states, Curr. Opin. Struct. Biol. 3, 601-610.
32. Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure, Proteins: Struct., Funct., Genet. 6, 87-103.
33. Hill, R. B., and DeGrado, W. F. (2000) A polar, solvent-exposed residue can be essential for native protein structure, Struct. Folding Des. 8, 471-479.