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Volumn 47, Issue 15, 2008, Pages 4484-4490

The fluorous effect in proteins: Properties of α4F 6, a 4-α-helix bundle protein with a fluorocarbon core

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; HELIX BUNDLE PROTEIN; HEXAFLUOROLEUCINE SIDE CHAIN; SELF-SEGREGATING BEHAVIOR;

EID: 42049094611     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702476f     Document Type: Article
Times cited : (47)

References (40)
  • 1
    • 0027432004 scopus 로고
    • Synthesis of Chiral and Bioactive Fluoroorganic Compounds
    • Resnati, G. (1993) Synthesis of Chiral and Bioactive Fluoroorganic Compounds. Tetrahedron 49, 9385-9445.
    • (1993) Tetrahedron , vol.49 , pp. 9385-9445
    • Resnati, G.1
  • 2
    • 0028116495 scopus 로고
    • Facile Catalyst Separation Without Water-Fluorous Biphase Hydroformylation of Olefins
    • Horvath, I. T., and Rabai, J. (1994) Facile Catalyst Separation Without Water-Fluorous Biphase Hydroformylation of Olefins. Science 266, 72-75.
    • (1994) Science , vol.266 , pp. 72-75
    • Horvath, I.T.1    Rabai, J.2
  • 3
    • 0033912062 scopus 로고    scopus 로고
    • Towards the non-stick egg: Designing fluorous proteins
    • Marsh, E. N. G. (2000) Towards the non-stick egg: designing fluorous proteins. Chem. Biol. 7, R153-R157.
    • (2000) Chem. Biol , vol.7
    • Marsh, E.N.G.1
  • 4
    • 0035793878 scopus 로고    scopus 로고
    • Fluorous mixture synthesis: A fluorous-tagging strategy for the synthesis and separation of mixtures of organic compounds
    • 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.
    • (2001) Science , vol.291 , pp. 1766-1769
    • Luo, Z.Y.1    Zhang, Q.S.2    Oderaotoshi, Y.3    Curran, D.P.4
  • 5
    • 33751408183 scopus 로고    scopus 로고
    • Bioorthogonal noncovalent chemistry: Fluorous phases in chemical biology
    • Yoder, N. C., Yuksel, D., Dafik, L., and Kumar, K. (2006) Bioorthogonal noncovalent chemistry: fluorous phases in chemical biology. Curr. Opin. Chem. Biol. 10, 576-583.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 576-583
    • Yoder, N.C.1    Yuksel, D.2    Dafik, L.3    Kumar, K.4
  • 6
    • 0000992534 scopus 로고
    • The solubility of fluorocarbons
    • Scott, R. L. (1948) The solubility of fluorocarbons. J. Am. Chem. Soc. 70, 4090-4093.
    • (1948) J. Am. Chem. Soc , vol.70 , pp. 4090-4093
    • Scott, R.L.1
  • 7
    • 33947438481 scopus 로고
    • Liquid-Liquid Solubility of Perfluoromethylcyclohexane with Benzene, Carbon Tetrachloride, Chlorobenzene, Chloroform and Toluene
    • Hildebrand, J. H., and Cochran, D. R. F. (1949) Liquid-Liquid Solubility of Perfluoromethylcyclohexane with Benzene, Carbon Tetrachloride, Chlorobenzene, Chloroform and Toluene. J. Am. Chem. Soc. 71, 22-25.
    • (1949) J. Am. Chem. Soc , vol.71 , pp. 22-25
    • Hildebrand, J.H.1    Cochran, D.R.F.2
  • 8
    • 0036430153 scopus 로고    scopus 로고
    • Fluorinated amino acids in protein design and engineering
    • Yoder, N. C., and Kumar, K. (2002) Fluorinated amino acids in protein design and engineering. Chem. Soc. Rev. 31, 335-341.
    • (2002) Chem. Soc. Rev , vol.31 , pp. 335-341
    • Yoder, N.C.1    Kumar, K.2
  • 9
    • 27644457086 scopus 로고    scopus 로고
    • Fluorine in peptide design and protein engineering
    • Jackel, C., and Koksch, B. (2005) Fluorine in peptide design and protein engineering. Eur. J. Org. Chem., 4483-4487.
    • (2005) Eur. J. Org. Chem , pp. 4483-4487
    • Jackel, C.1    Koksch, B.2
  • 10
    • 33746593245 scopus 로고    scopus 로고
    • How C-alpha-fluoroalkyl amino acids and peptides interact with enzymes: Studies concerning the influence on proteolytic stability, enzymatic resolution and peptide coupling
    • Smits, R., and Koksch, B. (2006) How C-alpha-fluoroalkyl amino acids and peptides interact with enzymes: Studies concerning the influence on proteolytic stability, enzymatic resolution and peptide coupling. Curr. Top. Med. Chem. 6, 1483-1498.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1483-1498
    • Smits, R.1    Koksch, B.2
  • 11
    • 0034817253 scopus 로고    scopus 로고
    • A coiled coil with a fluorous core
    • Bilgicer, B., Fichera, A., and Kumar, K. (2001) A coiled coil with a fluorous core. J. Am. Chem. Soc. 123, 4393-4399.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 4393-4399
    • Bilgicer, B.1    Fichera, A.2    Kumar, K.3
  • 12
    • 0035965730 scopus 로고    scopus 로고
    • Programmed self-sorting of coiled coils with leucine and hexafluoroleucine cores
    • 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.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 11815-11816
    • Bilgicer, B.1    Xing, X.C.2    Kumar, K.3
  • 13
    • 0034838165 scopus 로고    scopus 로고
    • Self-association and membrane-binding behavior of melittins containing trifluoroleucine
    • Niemz, A., and Tirrell, D. A. (2001) Self-association and membrane-binding behavior of melittins containing trifluoroleucine. J. Am. Chem. Soc. 123, 7407-7413.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 7407-7413
    • Niemz, A.1    Tirrell, D.A.2
  • 14
    • 0035901630 scopus 로고    scopus 로고
    • Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability
    • 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.
    • (2001) Angew. Chem., Int. Ed , vol.40 , pp. 1494
    • Tang, Y.1    Ghirlanda, G.2    Petka, W.A.3    Nakajima, T.4    DeGrado, W.F.5    Tirrell, D.A.6
  • 16
    • 0038276996 scopus 로고    scopus 로고
    • Incorporation of trifluoroisoleucine into proteins in vivo
    • Wang, P., Tang, Y., and Tirrell, D. A. (2003) Incorporation of trifluoroisoleucine into proteins in vivo. J. Am. Chem. Soc. 125, 6900-6906.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6900-6906
    • Wang, P.1    Tang, Y.2    Tirrell, D.A.3
  • 17
    • 7444241366 scopus 로고    scopus 로고
    • De novo design of defined helical bundles in membrane environments
    • Bilgicer, B., and Kumar, K. (2004) De novo design of defined helical bundles in membrane environments. Proc. Natl. Acad. Sci. U.S.A. 101, 15324-15329.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15324-15329
    • Bilgicer, B.1    Kumar, K.2
  • 18
    • 0035823858 scopus 로고    scopus 로고
    • Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host
    • 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.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 19
    • 0037071153 scopus 로고    scopus 로고
    • Synthesis and thermodynamic characterization of self-sorting coiled coils
    • Bilgicer, B., and Kumar, K. (2002) Synthesis and thermodynamic characterization of self-sorting coiled coils. Tetrahedron 58, 4105-4112.
    • (2002) Tetrahedron , vol.58 , pp. 4105-4112
    • Bilgicer, B.1    Kumar, K.2
  • 20
    • 11144320703 scopus 로고    scopus 로고
    • Fluorous effect in proteins: De novo design and characterization of a four-α helix bundle protein containing hexafluoroleucine
    • Lee, K.-H., Lee, H.-Y., Slutsky, M. S., Anderson, J. T., and Marsh, E. N. G. (2004) Fluorous effect in proteins: De novo design and characterization of a four-α helix bundle protein containing hexafluoroleucine. Biochemistry 43, 16277-16284.
    • (2004) Biochemistry , vol.43 , pp. 16277-16284
    • Lee, K.-H.1    Lee, H.-Y.2    Slutsky, M.S.3    Anderson, J.T.4    Marsh, E.N.G.5
  • 21
    • 30744471668 scopus 로고    scopus 로고
    • Modulating protein structure with fluorous amino acids: Increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine
    • Lee, H. Y., Lee, K. H., Al-Hashimi, H. M., and Marsh; E. N. G. (2006) Modulating protein structure with fluorous amino acids: Increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine. J. Am. Chem. Soc. 128, 337-343.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 337-343
    • Lee, H.Y.1    Lee, K.H.2    Al-Hashimi, H.M.3    Marsh, E.N.G.4
  • 22
    • 33746302557 scopus 로고    scopus 로고
    • Fluorinated interfaces drive self-association of transmembrane alpha helices in lipid bilayers
    • Naarmann, N., Bilgicer, B., Meng, H., Kumar, K., and Steinem, C. (2006) Fluorinated interfaces drive self-association of transmembrane alpha helices in lipid bilayers. Angew. Chem., Int. Ed. 45, 2588-2591.
    • (2006) Angew. Chem., Int. Ed , vol.45 , pp. 2588-2591
    • Naarmann, N.1    Bilgicer, B.2    Meng, H.3    Kumar, K.4    Steinem, C.5
  • 24
    • 33746320232 scopus 로고    scopus 로고
    • Fluorine in a native protein environment - How the spatial demand and polarity of fluoroalkyl groups affect protein folding
    • Jackel, C., Salwiczek, M., and Koksch, B. (2006) Fluorine in a native protein environment - How the spatial demand and polarity of fluoroalkyl groups affect protein folding. Angew. Chem., Int. Ed. 45, 4198-4203.
    • (2006) Angew. Chem., Int. Ed , vol.45 , pp. 4198-4203
    • Jackel, C.1    Salwiczek, M.2    Koksch, B.3
  • 25
    • 0037191625 scopus 로고    scopus 로고
    • A short and efficient synthesis of L-5,5,5,5′,5′,5′- hexafluoroleucine from N-Cbz-L-serine
    • 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 N-Cbz-L-serine. Org. Lett. 4, 4281-4283.
    • (2002) Org. Lett , vol.4 , pp. 4281-4283
    • Anderson, J.T.1    Toogood, P.L.2    Marsh, E.N.G.3
  • 27
    • 0023385987 scopus 로고
    • Rules for Optimization of Biocatalysis in Organic-Solvents
    • Laane, C., Boeren, S., Vos, K., and Veeger, C. (1987) Rules for Optimization of Biocatalysis in Organic-Solvents. Biotechnol. Bioeng. 30, 81-87.
    • (1987) Biotechnol. Bioeng , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 30
    • 33845454071 scopus 로고    scopus 로고
    • Interactions of hexafluoro-2-propanol with the Trp-cage peptide
    • Chatterjee, C., and Gerig, J. T. (2006) Interactions of hexafluoro-2-propanol with the Trp-cage peptide. Biochemistry 45, 14665-14674.
    • (2006) Biochemistry , vol.45 , pp. 14665-14674
    • Chatterjee, C.1    Gerig, J.T.2
  • 31
    • 25844479815 scopus 로고    scopus 로고
    • Effect of hexafluoroisopropanol alcohol on the structure of melittin: A molecular dynamics simulation study
    • Roccatano, D., Fioroni, M., Zacharias, M., and Colombo, G. (2005) Effect of hexafluoroisopropanol alcohol on the structure of melittin: A molecular dynamics simulation study. Protein Sci. 14, 2582-2589.
    • (2005) Protein Sci , vol.14 , pp. 2582-2589
    • Roccatano, D.1    Fioroni, M.2    Zacharias, M.3    Colombo, G.4
  • 32
    • 0032894467 scopus 로고    scopus 로고
    • Molecular simulation of the effects of alcohols on peptide structure
    • Dwyer, D. S. (1999) Molecular simulation of the effects of alcohols on peptide structure. Biopolymers 49, 635-645.
    • (1999) Biopolymers , vol.49 , pp. 635-645
    • Dwyer, D.S.1
  • 33
    • 0031029886 scopus 로고    scopus 로고
    • Fluorous synthesis: A fluorous-phase strategy for improving separation efficiency in organic synthesis
    • Studer, A., Hadida, S., Ferritto, R., Kim, S. Y., Jeger, P., Wipf, P., and Curran, D. P. (1997) Fluorous synthesis: A fluorous-phase strategy for improving separation efficiency in organic synthesis. Science 275, 823-826.
    • (1997) Science , vol.275 , pp. 823-826
    • Studer, A.1    Hadida, S.2    Ferritto, R.3    Kim, S.Y.4    Jeger, P.5    Wipf, P.6    Curran, D.P.7
  • 34
    • 0000648758 scopus 로고
    • Fluorine NMR of Proteins
    • Gerig, J. T. (1994) Fluorine NMR of Proteins. Prog. NMR Spectrosc. 26, 293-370.
    • (1994) Prog. NMR Spectrosc , vol.26 , pp. 293-370
    • Gerig, J.T.1
  • 35
    • 0028103622 scopus 로고
    • Origins of Fluorine Chemical-Shifts in Proteins
    • Chambers, S. E., Lau, E. Y., and Gerig, J. T. (1994) Origins of Fluorine Chemical-Shifts in Proteins. J. Am. Chem. Soc. 116, 3603-3604.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 3603-3604
    • Chambers, S.E.1    Lau, E.Y.2    Gerig, J.T.3
  • 36
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • Griebenow, K., and Klibanov, A. M. (1996) On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J. Am. Chem. Soc. 118, 11695-11700.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 37
    • 0034237189 scopus 로고    scopus 로고
    • Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition
    • Arroyo, M., Torres-Guzman, R., de la Mata, I., Castillon, M. P., and Acebal, C. (2000) Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition. Enzyme Microb. Technol. 27, 122-126.
    • (2000) Enzyme Microb. Technol , vol.27 , pp. 122-126
    • Arroyo, M.1    Torres-Guzman, R.2    de la Mata, I.3    Castillon, M.P.4    Acebal, C.5
  • 38
    • 0025882622 scopus 로고
    • Denaturation Capacity - a New Quantitative Criterion for Selection of Organic-Solvents as Reaction Media in Biocatalysis
    • Khmelnitsky, Y. L., Mozhaev, V. V., Belova, A. B., Sergeeva, M. V., and Martinek, K. (1991) Denaturation Capacity - a New Quantitative Criterion for Selection of Organic-Solvents as Reaction Media in Biocatalysis. Eur. J. Biochem. 198, 31-41.
    • (1991) Eur. J. Biochem , vol.198 , pp. 31-41
    • Khmelnitsky, Y.L.1    Mozhaev, V.V.2    Belova, A.B.3    Sergeeva, M.V.4    Martinek, K.5
  • 39
    • 37849047198 scopus 로고    scopus 로고
    • Antimicrobial Activity and Protease Stability of Peptides Containing Fluorinated Amino Acids
    • Meng, H., and Kumar, K. (2007) Antimicrobial Activity and Protease Stability of Peptides Containing Fluorinated Amino Acids. J. Am. Chem. Soc. 129, 15615-15622.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15615-15622
    • Meng, H.1    Kumar, K.2
  • 40
    • 48849093330 scopus 로고    scopus 로고
    • Using Fluorous Amino Acids to Modulate the Biological Activity of an Antimicrobial Peptide
    • in press
    • Gottler, L. M., Lee, H.-Y., Shelburne, C. E., Ramamoorthy, A., and Marsh, E. N. G. (2008) Using Fluorous Amino Acids to Modulate the Biological Activity of an Antimicrobial Peptide. ChemBioChem (in press).
    • (2008) ChemBioChem
    • Gottler, L.M.1    Lee, H.-Y.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.