메뉴 건너뛰기




Volumn 46, Issue 4, 2013, Pages 907-915

Exploring and exploiting polar-π interactions with fluorinated aromatic amino acids

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; PEPTIDE; PROTEIN;

EID: 84876208474     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar300086n     Document Type: Article
Times cited : (109)

References (55)
  • 1
    • 70449518081 scopus 로고    scopus 로고
    • A new paradigm for protein design and biological self-assembly
    • Akcay, G.; Kumar, K. A new paradigm for protein design and biological self-assembly J. Fluorine Chem. 2009, 130, 1178-1182
    • (2009) J. Fluorine Chem. , vol.130 , pp. 1178-1182
    • Akcay, G.1    Kumar, K.2
  • 2
    • 70349318199 scopus 로고    scopus 로고
    • Fluorine - A new element in the design of membrane-active peptides
    • Marsh, E. N.; 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.1    Buer, B.C.2    Ramamoorthy, A.3
  • 3
    • 84857536069 scopus 로고    scopus 로고
    • Fluorinated amino acids: Compatibility with native protein structures and effects on protein-protein interactions
    • Salwiczek, M.; Nyakatura, E. K.; Gerling, U. I.; Ye, S.; Koksch, B. Fluorinated amino acids: compatibility with native protein structures and effects on protein-protein interactions Chem. Soc. Rev. 2012, 41, 2135-2171
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 2135-2171
    • Salwiczek, M.1    Nyakatura, E.K.2    Gerling, U.I.3    Ye, S.4    Koksch, B.5
  • 4
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • Muralidharan, V.; Muir, T. W. Protein ligation: an enabling technology for the biophysical analysis of proteins Nat. Methods 2006, 3, 429-438
    • (2006) Nat. Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 5
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C. C.; Schultz, P. G. Adding new chemistries to the genetic code Annu. Rev. Biochem. 2010, 79, 413-444
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 6
    • 80053467272 scopus 로고    scopus 로고
    • Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase
    • Minnihan, E. C.; Young, D. D.; Schultz, P. G.; Stubbe, J. Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase J. Am. Chem. Soc. 2011, 133, 15942-15945
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15942-15945
    • Minnihan, E.C.1    Young, D.D.2    Schultz, P.G.3    Stubbe, J.4
  • 8
    • 84856713970 scopus 로고    scopus 로고
    • Quasiracemic crystallization as a tool to assess the accommodation of noncanonical amino residues in nativelike protein conformations
    • Mortenson, D. E.; Satyshur, K. A.; Guzei, I. A.; Forest, K. T.; Gellman, S. H. Quasiracemic crystallization as a tool to assess the accommodation of noncanonical amino residues in nativelike protein conformations J. Am. Chem. Soc. 2012, 134, 2473-2476
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2473-2476
    • Mortenson, D.E.1    Satyshur, K.A.2    Guzei, I.A.3    Forest, K.T.4    Gellman, S.H.5
  • 10
    • 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.; Tirrell, D. A. Fluorinated coiled-coil proteins prepared in vivo display enhanced thermal and chemical stability Angew. Chem., Int. Ed. 2001, 40, 1494-1496
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 1494-1496
    • Tang, Y.1    Ghirlanda, G.2    Petka, W.A.3    Nakajima, T.4    Degrado, W.F.5    Tirrell, D.A.6
  • 12
    • 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. M.; Anderson, J. T.; Marsh, E. N. 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.M.3    Anderson, J.T.4    Marsh, E.N.5
  • 13
    • 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
  • 14
    • 0035965730 scopus 로고    scopus 로고
    • Programmed self-sorting of coiled coils with leucine and hexafluoroleucine cores
    • Bilgicer, B.; Xing, X.; 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.2    Kumar, K.3
  • 15
    • 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
  • 16
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • Meyer, E. A.; Castellano, R. K.; Diederich, F. Interactions with aromatic rings in chemical and biological recognition Angew. Chem., Int. Ed. 2003, 42, 1210-1250
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 17
    • 33748232054 scopus 로고
    • Structure of the lowest temperature phase of the solid benzene hexafluorobenzene adduct
    • Williams, J. H.; Cockcroft, J. K.; Fitch, A. N. Structure of the lowest temperature phase of the solid benzene hexafluorobenzene adduct Angew. Chem., Int. Ed. 1992, 31, 1655-1657
    • (1992) Angew. Chem., Int. Ed. , vol.31 , pp. 1655-1657
    • Williams, J.H.1    Cockcroft, J.K.2    Fitch, A.N.3
  • 18
    • 33748212084 scopus 로고
    • Polar interactions between stacked π-systems in fluorinated 1,8-Diarylnaphthalenes - Importance of quadrupole-moments in molecular recognition
    • Cozzi, F.; Ponzini, F.; Annunziata, R.; Cinquini, M.; Siegel, J. S. Polar interactions between stacked π-systems in fluorinated 1,8- Diarylnaphthalenes-Importance of quadrupole-moments in molecular recognition Angew. Chem., Int. Ed. 1995, 34, 1019-1020
    • (1995) Angew. Chem., Int. Ed. , vol.34 , pp. 1019-1020
    • Cozzi, F.1    Ponzini, F.2    Annunziata, R.3    Cinquini, M.4    Siegel, J.S.5
  • 19
    • 0001227655 scopus 로고
    • The nature of π-π Interactions
    • Hunter, C. A.; Sanders, J. K. M. The nature of π-π interactions J. Am. Chem. Soc. 1990, 112, 5525-5534
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, J.K.M.2
  • 20
    • 67749097785 scopus 로고    scopus 로고
    • Substituent effects in cation/π interactions and electrostatic potentials above the centers of substituted benzenes are due primarily to through-space effects of the substituents
    • Wheeler, S. E.; Houk, K. N. Substituent effects in cation/π interactions and electrostatic potentials above the centers of substituted benzenes are due primarily to through-space effects of the substituents J. Am. Chem. Soc. 2009, 131, 3126-3127
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3126-3127
    • Wheeler, S.E.1    Houk, K.N.2
  • 21
    • 73349109506 scopus 로고    scopus 로고
    • Through-space effects of substituents dominate molecular electrostatic potentials of substituted arenes
    • Wheeler, S. E.; Houk, K. N. Through-space effects of substituents dominate molecular electrostatic potentials of substituted arenes J. Chem. Theory Comput. 2009, 5, 2301-2312
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 2301-2312
    • Wheeler, S.E.1    Houk, K.N.2
  • 23
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction - A mechanism of protein-structure stabilization
    • Burley, S. K.; Petsko, G. A. Aromatic-aromatic interaction-A mechanism of protein-structure stabilization Science 1985, 229, 23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 24
    • 79955766939 scopus 로고    scopus 로고
    • Aromatic rings in chemical and biological recognition: Energetics and structures
    • Salonen, L. M.; Ellermann, M.; Diederich, F. Aromatic rings in chemical and biological recognition: Energetics and structures Angew. Chem., Int. Ed. 2011, 50, 4808-4842
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 4808-4842
    • Salonen, L.M.1    Ellermann, M.2    Diederich, F.3
  • 25
    • 43449120151 scopus 로고    scopus 로고
    • Physical organic chemistry on the brain
    • For a recent review: Dougherty, D. A. Physical organic chemistry on the brain J. Org. Chem. 2008, 73, 3667-3673
    • (2008) J. Org. Chem. , vol.73 , pp. 3667-3673
    • Dougherty, D.A.1
  • 26
    • 0032546782 scopus 로고    scopus 로고
    • π-stacking interactions - Alive and well in proteins
    • McGaughey, G. B.; Gagne, M.; Rappe, A. K. π-stacking interactions-Alive and well in proteins J. Biol. Chem. 1998, 273, 15458-15463
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 27
    • 0037151644 scopus 로고    scopus 로고
    • Contribution of aromatic interactions to alpha-helix stability
    • Butterfield, S. M.; Patel, P. R.; Waters, M. L. Contribution of aromatic interactions to alpha-helix stability J. Am. Chem. Soc. 2002, 124, 9751-9755
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9751-9755
    • Butterfield, S.M.1    Patel, P.R.2    Waters, M.L.3
  • 29
    • 33846674483 scopus 로고    scopus 로고
    • Chemical double-mutant cycles: Dissecting non-covalent interactions
    • Cockroft, S. L.; Hunter, C. A. Chemical double-mutant cycles: dissecting non-covalent interactions Chem. Soc. Rev. 2007, 36, 172-188
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 172-188
    • Cockroft, S.L.1    Hunter, C.A.2
  • 30
    • 0037077578 scopus 로고    scopus 로고
    • Selective aromatic interactions in beta-hairpin peptides
    • Tatko, C. D.; Waters, M. L. Selective aromatic interactions in beta-hairpin peptides J. Am. Chem. Soc. 2002, 124, 9372-9373
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9372-9373
    • Tatko, C.D.1    Waters, M.L.2
  • 31
    • 33845575442 scopus 로고    scopus 로고
    • Stabilizing and destabilizing effects of phenylalanine → F-5-phenylalanine mutations on the folding of a small protein
    • Woll, M. G.; Hadley, E. B.; Mecozzi, S.; Gellman, S. H. Stabilizing and destabilizing effects of phenylalanine → F-5-phenylalanine mutations on the folding of a small protein J. Am. Chem. Soc. 2006, 128, 15932-15933
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15932-15933
    • Woll, M.G.1    Hadley, E.B.2    Mecozzi, S.3    Gellman, S.H.4
  • 32
    • 62649156942 scopus 로고    scopus 로고
    • Expanding the fluorous arsenal: Tetrafluorinated phenylalanines for protein design
    • Zheng, H.; Comeforo, K.; Gao, J. Expanding the fluorous arsenal: tetrafluorinated phenylalanines for protein design J. Am. Chem. Soc. 2009, 131, 18-19
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18-19
    • Zheng, H.1    Comeforo, K.2    Gao, J.3
  • 33
  • 34
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • McKnight, C. J.; Matsudaira, P. T.; Kim, P. S. NMR structure of the 35-residue villin headpiece subdomain Nat. Struct. Biol. 1997, 4, 180-184
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 37
    • 0001217733 scopus 로고
    • The electric quadrupole moments of benzene and hexafluorobenzene
    • Battaglia, M. R.; Buckingham, A. D.; Williams, J. H. The electric quadrupole moments of benzene and hexafluorobenzene Chem. Phys. Lett. 1981, 78, 421-423
    • (1981) Chem. Phys. Lett. , vol.78 , pp. 421-423
    • Battaglia, M.R.1    Buckingham, A.D.2    Williams, J.H.3
  • 38
    • 0000491257 scopus 로고
    • The molecular electric quadrupole-moment and solid-state architecture
    • Williams, J. H. The molecular electric quadrupole-moment and solid-state architecture Acc. Chem. Res. 1993, 26, 593-598
    • (1993) Acc. Chem. Res. , vol.26 , pp. 593-598
    • Williams, J.H.1
  • 39
    • 0034600911 scopus 로고    scopus 로고
    • Phenyl/pentafluorophenyl interactions and the generation of ordered mixed crystals: Sym-triphenethynylbenzene and sym-tris(perfluorophenethynyl)benzene
    • Ponzini, F.; Zagha, R.; Hardcastle, K.; Siegel, J. S. Phenyl/pentafluorophenyl interactions and the generation of ordered mixed crystals: sym-triphenethynylbenzene and sym-tris(perfluorophenethynyl)benzene Angew. Chem., Int. Ed. 2000, 39, 2323-2325
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 2323-2325
    • Ponzini, F.1    Zagha, R.2    Hardcastle, K.3    Siegel, J.S.4
  • 40
    • 0031001589 scopus 로고    scopus 로고
    • Phenyl-perfluorophenyl stacking interactions: A new strategy for supermolecule construction
    • Coates, G. W.; Dunn, A. R.; Henling, L. M.; Dougherty, D. A.; Grubbs, R. H. Phenyl-perfluorophenyl stacking interactions: A new strategy for supermolecule construction Angew. Chem., Int. Ed. 1997, 36, 248-251
    • (1997) Angew. Chem., Int. Ed. , vol.36 , pp. 248-251
    • Coates, G.W.1    Dunn, A.R.2    Henling, L.M.3    Dougherty, D.A.4    Grubbs, R.H.5
  • 41
    • 0032557231 scopus 로고    scopus 로고
    • Phenyl-perfluorophenyl stacking interactions: Topochemical 2 + 2 photodimerization and photopolymerization of olefinic compounds
    • Coates, G. W.; Dunn, A. R.; Henling, L. M.; Ziller, J. W.; Lobkovsky, E. B.; Grubbs, R. H. Phenyl-perfluorophenyl stacking interactions: Topochemical 2 + 2 photodimerization and photopolymerization of olefinic compounds J. Am. Chem. Soc. 1998, 120, 3641-3649
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3641-3649
    • Coates, G.W.1    Dunn, A.R.2    Henling, L.M.3    Ziller, J.W.4    Lobkovsky, E.B.5    Grubbs, R.H.6
  • 42
    • 17344363384 scopus 로고    scopus 로고
    • Solutions structure of alpha D-2, a nativelike de novo designed protein
    • Hill, R. B.; DeGrado, W. F. Solutions structure of alpha D-2, a nativelike de novo designed protein J. Am. Chem. Soc. 1998, 120, 1138-1145
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1138-1145
    • Hill, R.B.1    Degrado, W.F.2
  • 43
    • 84855260718 scopus 로고    scopus 로고
    • Stacked fluoroaromatics as supramolecular synthons for programming protein dimerization specificity
    • Pace, C. J.; Zheng, H.; Mylvaganam, R.; Kim, D.; Gao, J. Stacked fluoroaromatics as supramolecular synthons for programming protein dimerization specificity Angew. Chem. Int. Ed 2012, 51, 103-107
    • (2012) Angew. Chem. Int. Ed , vol.51 , pp. 103-107
    • Pace, C.J.1    Zheng, H.2    Mylvaganam, R.3    Kim, D.4    Gao, J.5
  • 44
    • 78149459473 scopus 로고    scopus 로고
    • Highly specific heterodimerization mediated by quadrupole interactions
    • Zheng, H.; Gao, J. Highly specific heterodimerization mediated by quadrupole interactions Angew. Chem., Int. Ed. 2010, 49, 8635-8639
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 8635-8639
    • Zheng, H.1    Gao, J.2
  • 46
    • 33847654171 scopus 로고    scopus 로고
    • Collagen-related peptides: Self-assembly of short, single strands into a functional biomaterial of micrometer scale
    • Cejas, M. A.; Kinney, W. A.; Chen, C.; Leo, G. C.; Tounge, B. A.; Vinter, J. G.; Joshi, P. P.; Maryanoff, B. E. Collagen-related peptides: self-assembly of short, single strands into a functional biomaterial of micrometer scale J. Am. Chem. Soc. 2007, 129, 2202-2203
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2202-2203
    • Cejas, M.A.1    Kinney, W.A.2    Chen, C.3    Leo, G.C.4    Tounge, B.A.5    Vinter, J.G.6    Joshi, P.P.7    Maryanoff, B.E.8
  • 48
    • 80052232617 scopus 로고    scopus 로고
    • Complementary π-π Interactions induce multicomponent coassembly into functional fibrils
    • Ryan, D. M.; Doran, T. M.; Nilsson, B. L. Complementary π-π interactions induce multicomponent coassembly into functional fibrils Langmuir 2011, 27, 11145-11156
    • (2011) Langmuir , vol.27 , pp. 11145-11156
    • Ryan, D.M.1    Doran, T.M.2    Nilsson, B.L.3
  • 49
    • 0000252375 scopus 로고
    • Kinetics of nucleophilic-substitution reactions of polyfluoroaromatic compounds
    • Rodionov, P. P.; Furin, G. G. Kinetics of nucleophilic-substitution reactions of polyfluoroaromatic compounds J. Fluorine Chem. 1990, 47, 361-434
    • (1990) J. Fluorine Chem. , vol.47 , pp. 361-434
    • Rodionov, P.P.1    Furin, G.G.2
  • 50
    • 0037069713 scopus 로고    scopus 로고
    • Synthesis of photoactive p-azidotetrafluorophenylalanine containing peptide by solid-phase Fmoc methodology
    • Redman, J. E.; Ghadiri, M. R. Synthesis of photoactive p-azidotetrafluorophenylalanine containing peptide by solid-phase Fmoc methodology Org. Lett. 2002, 4, 4467-4469
    • (2002) Org. Lett. , vol.4 , pp. 4467-4469
    • Redman, J.E.1    Ghadiri, M.R.2
  • 51
    • 78651486698 scopus 로고    scopus 로고
    • Facile synthesis of tetrafluorotyrosine and its application in pH triggered membrane lysis
    • Wang, F.; Qin, L.; Wong, P.; Gao, J. Facile synthesis of tetrafluorotyrosine and its application in pH triggered membrane lysis Org. Lett. 2011, 13, 236-239
    • (2011) Org. Lett. , vol.13 , pp. 236-239
    • Wang, F.1    Qin, L.2    Wong, P.3    Gao, J.4
  • 54
    • 67849128457 scopus 로고    scopus 로고
    • Halogen bonds as orthogonal molecular interactions to hydrogen bonds
    • Voth, A. R.; Khuu, P.; Oishi, K.; Ho, P. S. Halogen bonds as orthogonal molecular interactions to hydrogen bonds Nat. Chem. 2009, 1, 74-79
    • (2009) Nat. Chem. , vol.1 , pp. 74-79
    • Voth, A.R.1    Khuu, P.2    Oishi, K.3    Ho, P.S.4
  • 55
    • 54049097179 scopus 로고    scopus 로고
    • A rigid molecular balance for measuring face-to-face arene-arene interactions
    • Carroll, W. R.; Pellechia, P.; Shimizu, K. D. A rigid molecular balance for measuring face-to-face arene-arene interactions Org. Lett. 2008, 10, 3547-3550
    • (2008) Org. Lett. , vol.10 , pp. 3547-3550
    • Carroll, W.R.1    Pellechia, P.2    Shimizu, K.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.