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Volumn 107, Issue 18, 2010, Pages 8165-8170

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Author keywords

Alpha hemolysin; Single molecule; Stochastic sensing; Structure; Unnatural amino acid

Indexed keywords

AMINO ACID; CYCLODEXTRIN; MONOMER; POLYPEPTIDE; SCATTER FACTOR RECEPTOR;

EID: 77952412597     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0914229107     Document Type: Article
Times cited : (98)

References (61)
  • 2
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M, Skerra A (2009) Engineered protein scaffolds as next-generation antibody therapeutics. Curr Opin Chem Biol 13:245-255.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 3
    • 62849116221 scopus 로고    scopus 로고
    • Engineered affinity proteins - Generation and applications
    • Gronwall C, Stahl S (2009) Engineered affinity proteins - Generation and applications. J Biotechnol 140:254-269.
    • (2009) J Biotechnol , vol.140 , pp. 254-269
    • Gronwall, C.1    Stahl, S.2
  • 4
    • 69849107116 scopus 로고    scopus 로고
    • Incorporation of non-natural modules into proteins: Structural features beyond the genetic code
    • Arnold U (2009) Incorporation of non-natural modules into proteins: Structural features beyond the genetic code. Biotechnol Lett 31:1129-1139.
    • (2009) Biotechnol Lett , vol.31 , pp. 1129-1139
    • Arnold, U.1
  • 5
    • 65249177164 scopus 로고    scopus 로고
    • Directed enzyme evolution: Climbing fitness peaks one amino acid at a time
    • Tracewell CA, Arnold FH (2009) Directed enzyme evolution: Climbing fitness peaks one amino acid at a time. Curr Opin Chem Biol 13:3-9.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 3-9
    • Tracewell, C.A.1    Arnold, F.H.2
  • 6
    • 60749134505 scopus 로고    scopus 로고
    • Apoenzyme reconstitution as a chemical tool for structural enzymology and biotechnology
    • Fruk L, Kuo CH, Torres E, Niemeyer CM (2009) Apoenzyme reconstitution as a chemical tool for structural enzymology and biotechnology. Angew Chem Int Ed Engl 48:1550-1574.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 1550-1574
    • Fruk, L.1    Kuo, C.H.2    Torres, E.3    Niemeyer, C.M.4
  • 7
    • 4444247468 scopus 로고    scopus 로고
    • Functional engineered channels and pores
    • Bayley H, Jayasinghe L (2004) Functional engineered channels and pores. Mol Membr Biol 21:209-220.
    • (2004) Mol Membr Biol , vol.21 , pp. 209-220
    • Bayley, H.1    Jayasinghe, L.2
  • 8
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley H, Cremer PS (2001) Stochastic sensors inspired by biology. Nature 413:226-230.
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 9
    • 53649108801 scopus 로고    scopus 로고
    • The potential and challenges of nanopore sequencing
    • Branton D, et al. (2008) The potential and challenges of nanopore sequencing. Nature Biotechnol 26:1146-1153.
    • (2008) Nature Biotechnol , vol.26 , pp. 1146-1153
    • Branton, D.1
  • 11
    • 67651236466 scopus 로고    scopus 로고
    • Droplet networks with incorporated protein diodes show collective properties
    • Maglia G, et al. (2009) Droplet networks with incorporated protein diodes show collective properties. Nat Nanotechnol 4:437-440.
    • (2009) Nat Nanotechnol , vol.4 , pp. 437-440
    • Maglia, G.1
  • 12
    • 32244449078 scopus 로고    scopus 로고
    • Toward single molecule DNA sequencing: Direct identification of ribonucleoside and deoxyribonucleoside 5′-monophosphates by using an engineered protein nanopore equipped with a molecular adapter
    • DOI 10.1021/ja057123+
    • Astier Y, Braha O, Bayley H (2006) Toward single molecule DNA sequencing: Direct identification of ribonucleoside and deoxyribonucleoside 5′-monophosphates by using an engineered protein nanopore equipped with a molecular adapter. J Am Chem Soc 128:1705-1710. (Pubitemid 43214885)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.5 , pp. 1705-1710
    • Astier, Y.1    Braha, O.2    Bayley, H.3
  • 13
    • 64449088698 scopus 로고    scopus 로고
    • Continuous base identification for single-molecule nanopore DNA sequencing
    • Clarke J, et al. (2009) Continuous base identification for single-molecule nanopore DNA sequencing. Nature Nanotechnol 4:265-270.
    • (2009) Nature Nanotechnol , vol.4 , pp. 265-270
    • Clarke, J.1
  • 14
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • DOI 10.1038/19491
    • Gu L-Q, Braha O, Conlan S, Cheley S, Bayley H (1999) Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature 398:686-690. (Pubitemid 29197642)
    • (1999) Nature , vol.398 , Issue.6729 , pp. 686-690
    • Gu, L.-Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 15
    • 0035169385 scopus 로고    scopus 로고
    • Prolonged residence time of a noncovalent molecular adapter, β-Cyclodextrin, within the lumen of mutant α-Hemolysin pores
    • DOI 10.1085/jgp.118.5.481
    • Gu L-Q, Cheley S, Bayley H (2001) Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores. J Gen Physiol 118:481-494. (Pubitemid 33064287)
    • (2001) Journal of General Physiology , vol.118 , Issue.5 , pp. 481-493
    • Gu, L.-Q.1    Cheley, S.2    Bayley, H.3
  • 16
    • 41449084966 scopus 로고    scopus 로고
    • Simultaneous alternating and direct current readout of protein ion channel blocking events using glass nanopore membranes
    • DOI 10.1021/ac7021103
    • Ervin EN, Kawano R, White RJ, White HS (2008) Simultaneous alternating and direct current readout of protein ion channel blocking events using glass nanopore membranes. Anal Chem 80:2069-2076. (Pubitemid 351458054)
    • (2008) Analytical Chemistry , vol.80 , Issue.6 , pp. 2069-2076
    • Ervin, E.N.1    Kawano, R.2    White, R.J.3    White, H.S.4
  • 17
    • 67650069570 scopus 로고    scopus 로고
    • The dynamic side of the Hofmeister effect: A single-molecule nanopore study of specific complex formation
    • Gurnev PA, Harries D, Parsegian VA, Bezrukov SM (2009) The dynamic side of the Hofmeister effect: A single-molecule nanopore study of specific complex formation. ChemPhysChem 10:1445-1449.
    • (2009) ChemPhysChem , vol.10 , pp. 1445-1449
    • Gurnev, P.A.1    Harries, D.2    Parsegian, V.A.3    Bezrukov, S.M.4
  • 18
    • 33846079272 scopus 로고    scopus 로고
    • Structure and energetics of channel-forming protein-polysaccharide complexes inferred via computational statistical thermodynamics
    • DOI 10.1021/jp065009n
    • Mamonova T, Kurnikova M (2006) Structure and energetics of channel-forming protein-polysaccharide complexes inferred via computational statistical thermodynamics. J Phys Chem B 110:25091-25100. (Pubitemid 46065714)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.49 , pp. 25091-25100
    • Mamonova, T.1    Kurnikova, M.2
  • 19
    • 77749336161 scopus 로고    scopus 로고
    • Ion selectivity of alpha-hemolysin with beta-cyclodextrin adapter. II. Multi-ion effects studied with grand canonical monte carlo/brownian dynamics simulations
    • Egwolf B, Luo Y, Walters DE, Roux B (2010) Ion selectivity of alpha-hemolysin with beta-cyclodextrin adapter. II. Multi-ion effects studied with grand canonical monte carlo/brownian dynamics simulations. J Phys Chem B 114:2901-2909.
    • (2010) J Phys Chem B , vol.114 , pp. 2901-2909
    • Egwolf, B.1    Luo, Y.2    Walters, D.E.3    Roux, B.4
  • 22
    • 2542491118 scopus 로고    scopus 로고
    • Reversible pore block of connexin channels by cyclodextrins
    • DOI 10.1074/jbc.M401980200
    • Locke D, Koreen IV, Liu JY, Harris AL (2004) Reversible pore block of connexin channels by cyclodextrins. J Biol Chem 279:22883-22892. (Pubitemid 38685589)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22883-22892
    • Locke, D.1    Koreen, I.V.2    Liu, J.Y.3    Harris, A.L.4
  • 25
    • 58149470836 scopus 로고    scopus 로고
    • Method of creating a nanopore-terminated probe for single-molecule enantiomer discrimination
    • Gao C, Ding S, Tan Q, Gu LQ (2009) Method of creating a nanopore-terminated probe for single-molecule enantiomer discrimination. Anal Chem 81:80-86.
    • (2009) Anal Chem , vol.81 , pp. 80-86
    • Gao, C.1    Ding, S.2    Tan, Q.3    Gu, L.Q.4
  • 26
    • 33748216393 scopus 로고
    • Towards artificial ion channels: Transport of alkali metal ions across liposomal membranes by "bouquet" molecules
    • Pregel MJ, Jullien L, Lehn J-M (1992) Towards artificial ion channels: Transport of alkali metal ions across liposomal membranes by "bouquet" molecules. Angew Chem Int Edit 31:1637-1639.
    • (1992) Angew Chem Int Edit , vol.31 , pp. 1637-1639
    • Pregel, M.J.1    Jullien, L.2    Lehn, J.-M.3
  • 27
    • 21644446153 scopus 로고    scopus 로고
    • Ionic channel behavior of modified cyclodextrins inserted in lipid membranes
    • DOI 10.1021/la047211s
    • Bacri L, Benkhaled A, Guegan P, Auvray L (2005) Ionic channel behavior of modified cyclodextrins inserted in lipid membranes. Langmuir 21:5842-5846. (Pubitemid 40925830)
    • (2005) Langmuir , vol.21 , Issue.13 , pp. 5842-5846
    • Bacri, L.1    Benkhaled, A.2    Guegan, P.3    Auvray, L.4
  • 28
    • 55949102375 scopus 로고    scopus 로고
    • A light-gated synthetic ion channel
    • Jog PV, Gin MS (2008) A light-gated synthetic ion channel. Org Lett 10:3693-3696.
    • (2008) Org Lett , vol.10 , pp. 3693-3696
    • Jog, P.V.1    Gin, M.S.2
  • 29
    • 0034930381 scopus 로고    scopus 로고
    • Sequence-specific detection of individual DNA strands using engineered nanopores
    • DOI 10.1038/90236
    • Howorka S, Cheley S, Bayley H (2001) Sequence-specific detection of individual DNA strands using engineered nanopores. Nat Biotechnol 19:636-639. (Pubitemid 32625433)
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 636-639
    • Howorka, S.1    Cheley, S.2    Bayley, H.3
  • 31
    • 0037016451 scopus 로고    scopus 로고
    • The hydrogen bond in the solid state
    • Steiner T (2002) The hydrogen bond in the solid state. Angew Chem Int Ed 41:49-76.
    • (2002) Angew Chem Int Ed , vol.41 , pp. 49-76
    • Steiner, T.1
  • 32
    • 0037187814 scopus 로고    scopus 로고
    • Hydrogen bonds from water molecules to aromatic acceptors in very high-resolution protein crystal structures
    • Steiner T (2002) Hydrogen bonds from water molecules to aromatic acceptors in very high-resolution protein crystal structures. Biophys Chem 95:195-201.
    • (2002) Biophys Chem , vol.95 , pp. 195-201
    • Steiner, T.1
  • 33
    • 0035910278 scopus 로고    scopus 로고
    • Hydrogen bonds with pi-acceptors in proteins: Frequencies and role in stabilizing local 3D structures
    • DOI 10.1006/jmbi.2000.4301
    • Steiner T, Koellner G (2001) Hydrogen bonds with pi-acceptors in proteins: Frequencies and role in stabilizing local 3D structures. J Mol Biol 305:535-557. (Pubitemid 33032860)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 535-557
    • Steiner, T.1    Koellner, G.2
  • 37
    • 0035951448 scopus 로고    scopus 로고
    • Capture of a single molecule in a nanocavity
    • Gu L-Q, Cheley S, Bayley H (2001) Capture of a single molecule in a nanocavity. Science 291:636-640.
    • (2001) Science , vol.291 , pp. 636-640
    • Gu, L.-Q.1    Cheley, S.2    Bayley, H.3
  • 39
    • 0345099650 scopus 로고    scopus 로고
    • Cooperativity, partially bound states, and enthalpy-entropy compensation
    • Hunter CA, Tomas S (2003) Cooperativity, partially bound states, and enthalpy-entropy compensation. Chem Biol 10:1023-1032.
    • (2003) Chem Biol , vol.10 , pp. 1023-1032
    • Hunter, C.A.1    Tomas, S.2
  • 40
    • 0002640140 scopus 로고    scopus 로고
    • Cooperativity in the assembly of zipper complexes
    • Bisson AP, Hunter CA (1996) Cooperativity in the assembly of zipper complexes. Chem Commun 1723-1724.
    • (1996) Chem Commun , pp. 1723-1724
    • Bisson, A.P.1    Hunter, C.A.2
  • 41
    • 19744371399 scopus 로고    scopus 로고
    • Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate-aromatic interactions
    • DOI 10.1021/ja051020+
    • del Carmen Fernandez-Alonso M, Canada FJ, Jimenez-Barbero J, Cuevas G (2005) Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate-aromatic interactions. J Am Chem Soc 127:7379-7386. (Pubitemid 40746022)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.20 , pp. 7379-7386
    • Fernandez-Alonso, M.D.C.1    Canada, F.J.2    Jimenez-Barbero, J.3    Cuevas, G.4
  • 43
    • 34547919222 scopus 로고    scopus 로고
    • Carbohydrate molecular recognition: A spectroscopic investigation of carbohydrate-aromatic interactions
    • Stanca-Kaposta EC, et al. (2007) Carbohydrate molecular recognition: A spectroscopic investigation of carbohydrate-aromatic interactions. Phys Chem Chem Phys 9:4444-4451.
    • (2007) Phys Chem Chem Phys , vol.9 , pp. 4444-4451
    • Stanca-Kaposta, E.C.1
  • 45
    • 33845575442 scopus 로고    scopus 로고
    • 5-phenylalanine mutations on the folding of a small protein
    • DOI 10.1021/ja0634573
    • Woll MG, Hadley EB, Mecozzi S, Gellman SH (2006) Stabilizing and destabilizing effects of phenylalanine ->F5-phenylalanine mutations on the folding of a small protein. J Am Chem Soc 128:15932-15933. (Pubitemid 44936535)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.50 , pp. 15932-15933
    • Woll, M.G.1    Hadley, E.B.2    Mecozzi, S.3    Gellman, S.H.4
  • 47
    • 44849128243 scopus 로고    scopus 로고
    • Cys-loop neuroreceptors: Structure to the rescue?
    • Dougherty DA (2008) Cys-loop neuroreceptors: Structure to the rescue?. Chem Rev 108:1642-1653.
    • (2008) Chem Rev , vol.108 , pp. 1642-1653
    • Dougherty, D.A.1
  • 48
    • 41949139216 scopus 로고    scopus 로고
    • Substrate recognition mechanism of alpha-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans
    • Hondoh H, et al. (2008) Substrate recognition mechanism of alpha-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans. J Mol Biol 378:913-922.
    • (2008) J Mol Biol , vol.378 , pp. 913-922
    • Hondoh, H.1
  • 50
    • 59649114364 scopus 로고    scopus 로고
    • Orientation of the monomeric porin OmpG in planar lipid bilayers
    • Chen M, Li QH, Bayley H (2008) Orientation of the monomeric porin OmpG in planar lipid bilayers. ChemBioChem 9:3029-3036.
    • (2008) ChemBioChem , vol.9 , pp. 3029-3036
    • Chen, M.1    Li, Q.H.2    Bayley, H.3
  • 51
    • 37549026870 scopus 로고    scopus 로고
    • Protein nanopores with covalently attached molecular adapters
    • Wu H-C, Astier Y, Maglia G, Mikhailova E, Bayley H (2007) Protein nanopores with covalently attached molecular adapters. J Am Chem Soc 129:16142-16148.
    • (2007) J Am Chem Soc , vol.129 , pp. 16142-16148
    • Wu, H.-C.1    Astier, Y.2    Maglia, G.3    Mikhailova, E.4    Bayley, H.5
  • 52
    • 33751414735 scopus 로고    scopus 로고
    • Sequencing single molecules of DNA
    • Bayley H (2006) Sequencing single molecules of DNA. Curr Opin Chem Biol 10:628-637.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 628-637
    • Bayley, H.1
  • 54
    • 0024822218 scopus 로고
    • The use of 5′-phospho-2 deoxyribocytidylylriboadenosine as a facile route to chemical aminoacylation of tRNA
    • Robertson SA, Noren CJ, Anthony-Cahill SJ, Griffith MC, Schultz PG (1989) The use of 5′-phospho-2 deoxyribocytidylylriboadenosine as a facile route to chemical aminoacylation of tRNA. Nucleic Acids Res 17:9649-9660.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9649-9660
    • Robertson, S.A.1    Noren, C.J.2    Anthony-Cahill, S.J.3    Griffith, M.C.4    Schultz, P.G.5
  • 55
    • 0026342056 scopus 로고
    • Biosynthetic method for introducing unnatural amino acids site-specifically into proteins
    • Ellman J, Mendel D, Anthony-Cahill S, Noren CJ, Schultz PG (1991) Biosynthetic method for introducing unnatural amino acids site-specifically into proteins. Method Enzymol 202:301-336.
    • (1991) Method Enzymol , vol.202 , pp. 301-336
    • Ellman, J.1    Mendel, D.2    Anthony-Cahill, S.3    Noren, C.J.4    Schultz, P.G.5
  • 56
    • 0029811223 scopus 로고    scopus 로고
    • Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists
    • Kearney PC, et al. (1996) Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists. Mol Pharmacol 50:1401-1412.
    • (1996) Mol Pharmacol , vol.50 , pp. 1401-1412
    • Kearney, P.C.1
  • 57
    • 0018877893 scopus 로고
    • Specific labeling of 3′ termini of RNA with T4 RNA ligase
    • England TE, Bruce AG, Uhlenbeck OC (1980) Specific labeling of 3′ termini of RNA with T4 RNA ligase. Method Enzymol 65:65-74.
    • (1980) Method Enzymol , vol.65 , pp. 65-74
    • England, T.E.1    Bruce, A.G.2    Uhlenbeck, O.C.3
  • 58
    • 0032311418 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids into ion channels in xenopus oocyte expression system
    • Nowak MW, et al. (1998) In vivo incorporation of unnatural amino acids into ion channels in xenopus oocyte expression system. Method Enzymol 293:504-529.
    • (1998) Method Enzymol , vol.293 , pp. 504-529
    • Nowak, M.W.1
  • 59
    • 0032993061 scopus 로고    scopus 로고
    • A functional protein pore with a "retro" transmembrane domain
    • Cheley S, Braha O, Lu X, Conlan S, Bayley H (1999) A functional protein pore with a "retro" transmembrane domain. Protein Sci 8:1257-1267.
    • (1999) Protein Sci , vol.8 , pp. 1257-1267
    • Cheley, S.1    Braha, O.2    Lu, X.3    Conlan, S.4    Bayley, H.5
  • 60
    • 0034635954 scopus 로고    scopus 로고
    • Reversal of charge selectivity in transmembrane protein pores by using non-covalent molecular adapters
    • Gu L-Q, et al. (2000) Reversal of charge selectivity in transmembrane protein pores by using non-covalent molecular adapters. Proc Natl Acad Sci USA 97:3959-3964.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3959-3964
    • Gu, L.-Q.1
  • 61
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • DOI 10.1126/science.274.5294.1859
    • Song L, et al. (1996) Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274:1859-1865. (Pubitemid 26424757)
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6


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