메뉴 건너뛰기




Volumn 47, Issue 10, 2014, Pages 2878-2886

Fluorinated proteins: From design and synthesis to structure and stability

Author keywords

[No Author keywords available]

Indexed keywords

FLUORINE; PROTEIN;

EID: 84908082308     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar500125m     Document Type: Article
Times cited : (160)

References (41)
  • 1
    • 0033912062 scopus 로고    scopus 로고
    • Towards the Non-Stick Egg: Designing Fluorous Proteins
    • Marsh, E. N. G. Towards the Non-Stick Egg: Designing Fluorous Proteins Chem. Biol. 2000, 7, R153-R157
    • (2000) Chem. Biol. , vol.7 , pp. 153-R157
    • Marsh, E.N.G.1
  • 3
    • 0038372081 scopus 로고    scopus 로고
    • Fluorous Biphase Chemistry
    • Horvath, I. T. Fluorous Biphase Chemistry Acc. Chem. Res. 1998, 31, 641-650
    • (1998) Acc. Chem. Res. , vol.31 , pp. 641-650
    • Horvath, I.T.1
  • 4
    • 0034838165 scopus 로고    scopus 로고
    • Self-Association and Membrane-Binding Behavior of Melittins Containing Trifluoroleucine
    • Niemz, A.; Tirrell, D. A. Self-Association and Membrane-Binding Behavior of Melittins Containing Trifluoroleucine J. Am. Chem. Soc. 2001, 123, 7407-7413
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7407-7413
    • Niemz, A.1    Tirrell, D.A.2
  • 6
    • 7444241366 scopus 로고    scopus 로고
    • De Novo Design of Defined Helical Bundles in Membrane Environments
    • Bilgicer, B.; Kumar, K. De Novo Design of Defined Helical Bundles in Membrane Environments Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 15324-15329
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15324-15329
    • Bilgicer, B.1    Kumar, K.2
  • 7
    • 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.; Koksch, B. Fluorine in a Native Protein Environment-How the Spatial Demand and Polarity of Fluoroalkyl Groups Affect Protein Folding Angew. Chem., Int. Ed. 2006, 45, 4198-4203
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 4198-4203
    • Jackel, C.1    Salwiczek, M.2    Koksch, B.3
  • 9
    • 0041708049 scopus 로고    scopus 로고
    • Stereoelectronic Effects on Collagen Stability: The Dichotomy of 4-Fluoroproline Diastereomers
    • Hodges, J. A.; Raines, R. T. Stereoelectronic Effects on Collagen Stability: The Dichotomy of 4-Fluoroproline Diastereomers J. Am Chem Soc. 2003, 125, 9262-9263
    • (2003) J. Am Chem Soc. , vol.125 , pp. 9262-9263
    • Hodges, J.A.1    Raines, R.T.2
  • 11
    • 70349318199 scopus 로고    scopus 로고
    • Fluorine-A New Element in the Design of Membrane-Active Peptides
    • Marsh, E. N. G.; Buer, B. C.; Ramamoorthy, A. Fluorine-A New Element in the Design of Membrane-Active Peptides Mol. BioSyst. 2009, 5, 1143-1147
    • (2009) Mol. BioSyst. , vol.5 , pp. 1143-1147
    • Marsh, E.N.G.1    Buer, B.C.2    Ramamoorthy, A.3
  • 12
    • 79959927774 scopus 로고    scopus 로고
    • Using Fluorine Nuclear Magnetic Resonance to Probe Changes in the Structure and Dynamics of Membrane-Active Peptides Interacting with Lipid Bilayers
    • Suzuki, Y.; Buer, B. C.; Al-Hashimi, H. M.; Marsh, E. N. G. Using Fluorine Nuclear Magnetic Resonance To Probe Changes in the Structure and Dynamics of Membrane-Active Peptides Interacting with Lipid Bilayers Biochemistry 2011, 50, 5979-5987
    • (2011) Biochemistry , vol.50 , pp. 5979-5987
    • Suzuki, Y.1    Buer, B.C.2    Al-Hashimi, H.M.3    Marsh, E.N.G.4
  • 13
    • 77954755663 scopus 로고    scopus 로고
    • Using Fluorine Nuclear Magnetic Resonance to Probe the Interaction of Membrane-Active Peptides with the Lipid Bilayer
    • Buer, B. C.; Chugh, J.; Al-Hashimi, H. M.; Marsh, E. N. G. Using Fluorine Nuclear Magnetic Resonance to Probe the Interaction of Membrane-Active Peptides with the Lipid Bilayer Biochemistry 2010, 49, 5760-5765
    • (2010) Biochemistry , vol.49 , pp. 5760-5765
    • Buer, B.C.1    Chugh, J.2    Al-Hashimi, H.M.3    Marsh, E.N.G.4
  • 14
    • 84876420343 scopus 로고    scopus 로고
    • 19F NMR Reporter for Peptide-Membrane Interactions in Solution
    • 19F NMR Reporter for Peptide-Membrane Interactions in Solution J. Pept. Sci. 2013, 19, 308-314
    • (2013) J. Pept. Sci. , vol.19 , pp. 308-314
    • Buer, B.C.1    Levin, B.J.2    Marsh, E.N.G.3
  • 17
    • 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.; Marsh, E. N. G. A Short and Efficient Synthesis of l -5,5,5,5′,5′,5′-Hexafluoroleucine from N -Cbz- l -Serine Org. Lett. 2002, 4, 4281-4283
    • (2002) Org. Lett. , vol.4 , pp. 4281-4283
    • Anderson, J.T.1    Toogood, P.L.2    Marsh, E.N.G.3
  • 18
    • 0035799841 scopus 로고    scopus 로고
    • A Novel Synthesis of Enantiomerically Pure 5,5,5,5 ′,5 ′,5 ′-Hexafluoroleucine
    • Xing, X. C.; Fichera, A.; Kumar, K. A Novel Synthesis of Enantiomerically Pure 5,5,5,5 ′,5 ′,5 ′-Hexafluoroleucine Org. Lett. 2001, 3, 1285-1286
    • (2001) Org. Lett. , vol.3 , pp. 1285-1286
    • Xing, X.C.1    Fichera, A.2    Kumar, K.3
  • 19
    • 38349124527 scopus 로고    scopus 로고
    • Chemoenzymatic Synthesis of (S)-Hexafluoroleucine and (S)-Tetrafluoroleucine
    • Chiu, H.-P.; Cheng, R. P. Chemoenzymatic Synthesis of (S)-Hexafluoroleucine and (S)-Tetrafluoroleucine Org. Lett. 2007, 9, 5517-5520
    • (2007) Org. Lett. , vol.9 , pp. 5517-5520
    • Chiu, H.-P.1    Cheng, R.P.2
  • 20
    • 0037183472 scopus 로고    scopus 로고
    • Attenuation of the Editing Activity of the Escherichia coli Leucyl-tRNA Synthetase Allows Incorporation of Novel Amino Acids into Proteins in Vivo
    • Tang, Y.; Tirrell, D. A. Attenuation of the Editing Activity of the Escherichia coli Leucyl-tRNA Synthetase Allows Incorporation of Novel Amino Acids into Proteins in Vivo Biochemistry 2002, 41, 10635-10645
    • (2002) Biochemistry , vol.41 , pp. 10635-10645
    • Tang, Y.1    Tirrell, D.A.2
  • 21
    • 0029899119 scopus 로고    scopus 로고
    • Controlling Topology and Native-Like Behavior of de Novo- Designed Peptides: Design and Characterization of Antiparallel Four-Stranded Coiled Coils
    • Betz, S. F.; DeGrado, W. F. Controlling Topology and Native-Like Behavior of De Novo- Designed Peptides: Design and Characterization of Antiparallel Four-Stranded Coiled Coils Biochemistry 1996, 35, 6955-6962
    • (1996) Biochemistry , vol.35 , pp. 6955-6962
    • Betz, S.F.1    Degrado, W.F.2
  • 22
    • 0033694923 scopus 로고    scopus 로고
    • De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
    • Hill, R. B.; Raleigh, D. P.; Lombardi, A.; Degrado, W. F. De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function Acc. Chem. Res. 2000, 33, 745-754
    • (2000) Acc. Chem. Res. , vol.33 , pp. 745-754
    • Hill, R.B.1    Raleigh, D.P.2    Lombardi, A.3    Degrado, W.F.4
  • 23
    • 11144320703 scopus 로고    scopus 로고
    • Fluorous Effect in Proteins: De Novo Design and Characterization of a Four-Alpha-Helix Bundle Protein Containing Hexafluoroleucine
    • Lee, K.-H.; Lee, H.-Y.; Slutsky, M. S.; Anderson, J. T.; Marsh, E. N. G. Fluorous Effect in Proteins: De Novo Design and Characterization of a Four-Alpha-Helix Bundle Protein Containing Hexafluoroleucine Biochemistry 2004, 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
  • 24
    • 70449562250 scopus 로고    scopus 로고
    • Engineering Protein Stability and Specificity Using Fluorous Amino Acids: The Importance of Packing Effects
    • Buer, B. C.; de la Salud-Bea, R.; Al Hashimi, H. M.; Marsh, E. N. G. Engineering Protein Stability and Specificity Using Fluorous Amino Acids: The Importance of Packing Effects Biochemistry 2009, 48, 10810-10817
    • (2009) Biochemistry , vol.48 , pp. 10810-10817
    • Buer, B.C.1    De La Salud-Bea, R.2    Al Hashimi, H.M.3    Marsh, E.N.G.4
  • 25
    • 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.; Marsh, E. N. G. 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. 2006, 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
  • 26
    • 84864697431 scopus 로고    scopus 로고
    • Influence of Fluorination on the Thermodynamics of Protein Folding
    • Buer, B. C.; Levin, B. J.; Marsh, E. N. G. Influence of Fluorination on the Thermodynamics of Protein Folding J. Am. Chem. Soc. 2012, 134, 13027-13034
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 13027-13034
    • Buer, B.C.1    Levin, B.J.2    Marsh, E.N.G.3
  • 28
    • 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.; Curran, D. P. Fluorous Synthesis: A Fluorous-Phase Strategy for Improving Separation Efficiency in Organic Synthesis Science 1997, 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
  • 29
    • 0000992534 scopus 로고
    • The Solubility of Fluorocarbons
    • Scott, R. L. The Solubility of Fluorocarbons J. Am. Chem. Soc. 1948, 70, 4090-4093
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 4090-4093
    • Scott, R.L.1
  • 31
    • 84867674672 scopus 로고    scopus 로고
    • Comparison of the Structures and Stabilities of Coiled-Coil Proteins Containing Hexafluoroleucine and t -Butylalanine Provides Insight into the Stabilizing Effects of Highly Fluorinated Amino Acid Side-Chains
    • Buer, B. C.; Meagher, J. L.; Stuckey, J. A.; Marsh, E. N. G. Comparison of the Structures and Stabilities of Coiled-Coil Proteins Containing Hexafluoroleucine and t -Butylalanine Provides Insight into the Stabilizing Effects of Highly Fluorinated Amino Acid Side-Chains Protein Sci. 2012, 21, 1705-1715
    • (2012) Protein Sci. , vol.21 , pp. 1705-1715
    • Buer, B.C.1    Meagher, J.L.2    Stuckey, J.A.3    Marsh, E.N.G.4
  • 32
    • 0035965730 scopus 로고    scopus 로고
    • Programmed Self-Sorting of Coiled Coils with Leucine and Hexafluoroleucine Cores
    • Bilgicer, B.; Xing, X. C.; Kumar, K. Programmed Self-Sorting of Coiled Coils with Leucine and Hexafluoroleucine Cores J. Am. Chem. Soc. 2001, 123, 11815-11816
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11815-11816
    • Bilgicer, B.1    Xing, X.C.2    Kumar, K.3
  • 33
    • 0026567907 scopus 로고
    • Response of a Protein-Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic Effect
    • Eriksson, A. E.; Baase, W. A.; Zhang, X. J.; Heinz, D. W.; Blaber, M.; Baldwin, E. P.; Matthews, B. W. Response of a Protein-Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic Effect Science 1992, 255, 178-183
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 34
    • 0029002720 scopus 로고
    • The Hydrophobic Effect in Protein-Folding
    • Lins, L.; Brasseur, R. The Hydrophobic Effect in Protein-Folding FASEB J. 1995, 9, 535-540
    • (1995) FASEB J. , vol.9 , pp. 535-540
    • Lins, L.1    Brasseur, R.2
  • 35
    • 4544316921 scopus 로고    scopus 로고
    • The Polar Hydrophobicity of Fluorinated Compounds
    • Biffinger, J. C.; Kim, H. W.; DiMagno, S. G. The Polar Hydrophobicity of Fluorinated Compounds ChemBioChem. 2004, 5, 622-627
    • (2004) ChemBioChem. , vol.5 , pp. 622-627
    • Biffinger, J.C.1    Kim, H.W.2    Dimagno, S.G.3
  • 38
    • 48849093330 scopus 로고    scopus 로고
    • Using Fluorous Amino Acids to Modulate the Biological Activity of an Antimicrobial Peptide
    • Gottler, L. M.; Lee, H.-Y.; Shelburne, C. E.; Ramamoorthy, A.; Marsh, E. N. G. Using Fluorous Amino Acids To Modulate the Biological Activity of an Antimicrobial Peptide ChemBioChem. 2008, 9, 370-373
    • (2008) ChemBioChem. , vol.9 , pp. 370-373
    • Gottler, L.M.1    Lee, H.-Y.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.G.5
  • 39
    • 50849120027 scopus 로고    scopus 로고
    • Using Fluorous Amino Acids to Probe the Effects of Changing Hydrophobicity on the Physical and Biological Properties of the Beta-Hairpin Antimicrobial Peptide Protegrin-1
    • Gottler, L. M.; de la Salud Bea, R.; Shelburne, C. E.; Ramamoorthy, A.; Marsh, E. N. Using Fluorous Amino Acids To Probe the Effects of Changing Hydrophobicity on the Physical and Biological Properties of the Beta-Hairpin Antimicrobial Peptide Protegrin-1 Biochemistry 2008, 47, 9243-9250
    • (2008) Biochemistry , vol.47 , pp. 9243-9250
    • Gottler, L.M.1    De La Salud Bea, R.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 40


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.