메뉴 건너뛰기




Volumn 46, Issue 12, 2013, Pages 2924-2933

Extramembrane control of ion channel peptide assemblies, using alamethicin as an example

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; ION CHANNEL; PEPTIDE;

EID: 84890641940     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar400051f     Document Type: Article
Times cited : (18)

References (62)
  • 3
    • 0022924412 scopus 로고
    • Molecular basis for the function of ionic channels
    • Numa, S. Molecular basis for the function of ionic channels Biochem. Soc. Symp. 1986, 52, 119-143 (Pubitemid 17235120)
    • (1986) Biochemical Society Symposia , vol.52 , pp. 119-143
    • Numa, S.1
  • 4
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • DOI 10.1038/nature01748
    • Miyazawa, A.; Fujiyoshi, Y.; Unwin, N. Structure and gating mechanism of the acetylcholine receptor pore Nature 2003, 423, 949-955 (Pubitemid 36806903)
    • (2003) Nature , vol.423 , Issue.6943 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 6
    • 13844306732 scopus 로고    scopus 로고
    • Rigid-rod molecules in biomembrane models: From hydrogen-bonded chains to synthetic multifunctional pores
    • DOI 10.1021/ar0400802
    • Sakai, N.; Mareda, J.; Matile, S. Rigid-rod molecules in biomembrane models: from hydrogen-bonded chains to synthetic multifunctional pores Acc. Chem. Res. 2005, 38, 79-87 (Pubitemid 40261718)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.2 , pp. 79-87
    • Sakai, N.1    Mareda, J.2    Matile, S.3
  • 7
    • 0032921876 scopus 로고    scopus 로고
    • Designed membrane channels and pores
    • DOI 10.1016/S0958-1669(99)80017-2
    • Bayley, H. Designed membrane channels and pores Curr. Opin. Biotechnol. 1999, 10, 94-103 (Pubitemid 29054633)
    • (1999) Current Opinion in Biotechnology , vol.10 , Issue.1 , pp. 94-103
    • Bayley, H.1
  • 8
    • 27744592429 scopus 로고    scopus 로고
    • Protein components for nanodevices
    • DOI 10.1016/j.cbpa.2005.10.012, PII S1367593105001468, Biopolymers / Model Systems
    • Astier, Y.; Bayley, H.; Howorka, S. Protein components for nanodevices Curr. Opin. Chem. Biol. 2005, 9, 576-584 (Pubitemid 41612185)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.6 , pp. 576-584
    • Astier, Y.1    Bayley, H.2    Howorka, S.3
  • 9
    • 33846666853 scopus 로고    scopus 로고
    • Synthetic ion channels in bilayer membranes
    • Fyles, T. M. Synthetic ion channels in bilayer membranes Chem. Soc. Rev. 2007, 36, 335-347
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 335-347
    • Fyles, T.M.1
  • 10
    • 0031904167 scopus 로고    scopus 로고
    • Peptide ion channels: Design and creation of function
    • Futaki, S. Peptide ion channels: design and creation of function Biopolymers 1998, 47, 75-81
    • (1998) Biopolymers , vol.47 , pp. 75-81
    • Futaki, S.1
  • 13
    • 0037523526 scopus 로고    scopus 로고
    • Synthetic multifunctional pores: Deletion and inversion of anion/cation selectivity using pM and pH
    • Sakai, N.; Sordé, N.; Das, G.; Perrottet, P.; Gerard, D.; Matile, S. Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH Org. Biomol. Chem. 2003, 1, 1226-1231
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 1226-1231
    • Sakai, N.1    Sordé, N.2    Das, G.3    Perrottet, P.4    Gerard, D.5    Matile, S.6
  • 14
    • 55949102375 scopus 로고    scopus 로고
    • A light-gated synthetic ion channel
    • Jog, P. V.; Gin, M. S. A light-gated synthetic ion channel Org. Lett. 2008, 10, 3693-3696
    • (2008) Org. Lett. , vol.10 , pp. 3693-3696
    • Jog, P.V.1    Gin, M.S.2
  • 19
    • 0023078222 scopus 로고
    • Reconstitution of channel proteins from excitable cells in planar lipid bilayer membranes
    • Montal, M. Reconstitution of channel proteins from excitable cells in planar lipid bilayer membranes J. Membr. Biol. 1987, 98, 101-115
    • (1987) J. Membr. Biol. , vol.98 , pp. 101-115
    • Montal, M.1
  • 20
    • 0017258698 scopus 로고
    • Single-channel currents recorded from membrane of denervated frog muscle fibres
    • Neher, E.; Sakmann, B. Single-channel currents recorded from membrane of denervated frog muscle fibres Nature 1976, 260, 799-802
    • (1976) Nature , vol.260 , pp. 799-802
    • Neher, E.1    Sakmann, B.2
  • 22
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley, G. A.; Wallace, B. A. Model ion channels: gramicidin and alamethicin J. Membr. Biol. 1992, 129, 109-136
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 23
    • 0015513556 scopus 로고
    • The unit conductance channel of alamethicin
    • Gordon, L. G.; Haydon, D. A. The unit conductance channel of alamethicin Biochim. Biophys. Acta 1972, 255, 1014-1018
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 1014-1018
    • Gordon, L.G.1    Haydon, D.A.2
  • 25
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J. D.; Wasserman, Z. R.; DeGrado, W. F. Synthetic amphiphilic peptide models for protein ion channels Science 1988, 240, 1177-1181
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    Degrado, W.F.3
  • 26
    • 0028174318 scopus 로고
    • Artificial transmembrane ion channels from self-assembling peptide nanotubes
    • Ghadiri, M. R.; Granja, J. R.; Buehler, L. K. Artificial transmembrane ion channels from self-assembling peptide nanotubes Nature 1994, 369, 301-304
    • (1994) Nature , vol.369 , pp. 301-304
    • Ghadiri, M.R.1    Granja, J.R.2    Buehler, L.K.3
  • 27
    • 0028020468 scopus 로고
    • Triggers and switches in a self-assembling pore-forming protein
    • DOI 10.1002/jcb.240560210
    • Bayley, H. Triggers and switches in a self-assembling pore-forming protein J. Cell Biochem. 1994, 56, 177-182 (Pubitemid 24318393)
    • (1994) Journal of Cellular Biochemistry , vol.56 , Issue.2 , pp. 177-182
    • Bayley, H.1
  • 28
    • 0028226051 scopus 로고
    • Alamethicin: A peptide model for voltage gating and protein-membrane interactions
    • Cafiso, D. S. Alamethicin: a peptide model for voltage gating and protein-membrane interactions Annu. Rev. Biophys. Biomol. Struct. 1994, 23, 141-165 (Pubitemid 24217365)
    • (1994) Annual Review of Biophysics and Biomolecular Structure , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 29
    • 34447330999 scopus 로고    scopus 로고
    • Ligand-induced extramembrane conformation switch controlling alamethicin assembly and the channel current
    • DOI 10.1002/cbdv.200790112
    • Futaki, S.; Asami, K. Ligand-induced extramembrane conformation switch controlling alamethicin assembly and the channel current Chem. Biodiversity 2007, 4, 1313-1322 (Pubitemid 47072877)
    • (2007) Chemistry and Biodiversity , vol.4 , Issue.6 , pp. 1313-1322
    • Futaki, S.1    Asami, K.2
  • 31
    • 0035852013 scopus 로고    scopus 로고
    • Alamethicin-leucine zipper hybrid peptide: A prototype for the design of artificial receptors and ion channels
    • DOI 10.1021/ja011166i
    • Futaki, S.; Fukuda, M.; Omote, M.; Yamauchi, K.; Yagami, T.; Niwa, M.; Sugiura, Y. Alamethicin-leucine zipper hybrid peptide: a prototype for the design of artificial receptors and ion channels J. Am. Chem. Soc. 2001, 123, 12127-12134 (Pubitemid 33136049)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.49 , pp. 12127-12134
    • Futaki, S.1    Fukuda, M.2    Omote, M.3    Yamauchi, K.4    Yagami, T.5    Niwa, M.6    Sugiura, Y.7
  • 32
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H.; Johnson, P. F.; McKnight, S. L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins Science 1988, 240, 1759-1764
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 33
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E. K.; Rutkowski, R.; Kim, P. S. Evidence that the leucine zipper is a coiled coil Science 1989, 243, 538-542 (Pubitemid 19048755)
    • (1989) Science , vol.243 , Issue.4890 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 34
    • 0034867234 scopus 로고    scopus 로고
    • Peptaibols: Models for ion channels
    • DOI 10.1042/BST0290565
    • Chugh, J. K.; Wallace, B. A. Peptaibols: models for ion channels Biochem. Soc. Trans. 2001, 29, 565-570 (Pubitemid 32783658)
    • (2001) Biochemical Society Transactions , vol.29 , Issue.4 , pp. 565-570
    • Chugh, J.K.1    Wallace, B.A.2
  • 35
    • 34447317806 scopus 로고    scopus 로고
    • Channel-forming activity of alamethicin: Effects of covalent tethering
    • DOI 10.1002/cbdv.200790113
    • Woolley, G. A. Channel-forming activity of alamethicin: effects of covalent tethering Chem. Biodiversity 2007, 4, 1323-1337 (Pubitemid 47072878)
    • (2007) Chemistry and Biodiversity , vol.4 , Issue.6 , pp. 1323-1337
    • Woolley, G.A.1
  • 36
    • 1842555216 scopus 로고    scopus 로고
    • Ion-channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel-stave model
    • Matsubara, A.; Asami, K.; Akagi, A.; Nishino, N. Ion-channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by barrel-stave model J. Chem. Soc., Chem. Commun. 1996, 2069-2070 (Pubitemid 126441183)
    • (1996) Chemical Communications , Issue.17 , pp. 2069-2070
    • Matsubara, A.1    Asami, K.2    Akagi, A.3    Nishino, N.4
  • 37
    • 0032774824 scopus 로고    scopus 로고
    • C-terminally shortened alamethicin on templates: Influence of the linkers on conductances
    • DOI 10.1016/S0005-2736(99)00047-4, PII S0005273699000474
    • Duclohier, H.; Kociolek, K.; Stasiak, M.; Leplawy, M. T.; Marshall, G. R. C-terminally shortened alamethicin on templates: influence of the linkers on conductances Biochim. Biophys. Acta 1999, 1420, 14-22 (Pubitemid 29369014)
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1420 , Issue.1-2 , pp. 14-22
    • Duclohier, H.1    Kociolek, K.2    Stasiak, M.3    Leplawy, M.T.4    Marshall, G.R.5
  • 38
    • 0038702245 scopus 로고    scopus 로고
    • N-terminal insertion of alamethicin in channel formation studied using its covalent dimer N-terminally linked by disulfide bond
    • DOI 10.1016/S0005-2736(03)00110-X
    • Sakoh, M.; Okazaki, T.; Nagaoka, Y.; Asami, K. N-terminal insertion of alamethicin in channel formation studied using its covalent dimer N-terminally linked by disulfide bond Biochim. Biophys. Acta 2003, 1612, 117-121 (Pubitemid 36555694)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1612 , Issue.1 , pp. 117-121
    • Sakoh, M.1    Okazaki, T.2    Nagaoka, Y.3    Asami, K.4
  • 39
    • 0037974360 scopus 로고    scopus 로고
    • Ion channels of alamethicin dimer N-terminally linked by disulfide bond
    • Okazaki, T.; Sakoh, M.; Nagaoka, Y.; Asami, K. Ion channels of alamethicin dimer N-terminally linked by disulfide bond Biophys. J. 2003, 85, 267-273 (Pubitemid 36753632)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 267-273
    • Okazaki, T.1    Sakoh, M.2    Nagaoka, Y.3    Asami, K.4
  • 40
    • 0030867021 scopus 로고    scopus 로고
    • Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeat I-IV) ofthe sodium channel
    • DOI 10.1016/S0040-4039(97)01651-1, PII S0040403997016511
    • Futaki, S.; Aoki, M.; Fukuda, M.; Kondo, F.; Niwa, M.; Kitagawa, K.; Nakaya, Y. Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeat I-IV) of the sodium channel Tetrahedron Lett. 1997, 38, 7071-7074 (Pubitemid 27402192)
    • (1997) Tetrahedron Letters , vol.38 , Issue.40 , pp. 7071-7074
    • Futaki, S.1    Aoki, M.2    Fukuda, M.3    Kondo, F.4    Niwa, M.5    Kitagawa, K.6    Nakaya, Y.7
  • 43
    • 33646495755 scopus 로고    scopus 로고
    • Transmission of extramembrane conformational change into current: Construction of metal-gated ion channel
    • Kiwada, T.; Sonomura, K.; Sugiura, Y.; Asami, K.; Futaki, S. Transmission of extramembrane conformational change into current: construction of metal-gated ion channel J. Am. Chem. Soc. 2006, 128, 6010-6011
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6010-6011
    • Kiwada, T.1    Sonomura, K.2    Sugiura, Y.3    Asami, K.4    Futaki, S.5
  • 44
    • 10044252376 scopus 로고    scopus 로고
    • Control of peptide structure and recognition by Fe(III)-induced helix destabilization
    • Futaki, S.; Kiwada, T.; Sugiura, Y. Control of peptide structure and recognition by Fe(III)-induced helix destabilization J. Am. Chem. Soc. 2004, 126, 15762-15769 (Pubitemid 39602435)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.48 , pp. 15762-15769
    • Futaki, S.1    Kiwada, T.2    Sugiura, Y.3
  • 46
    • 0021881565 scopus 로고
    • Three-dimensional structure of calmodulin
    • DOI 10.1038/315037a0
    • Babu, Y. S.; Sack, J. S.; Greenhough, T. J.; Bugg, C. E.; Means, A. R.; Cook, W. J. Three-dimensional structure of calmodulin Nature 1985, 315, 37-40 (Pubitemid 15064895)
    • (1985) Nature , vol.315 , Issue.6014 , pp. 37-40
    • Babu, Y.S.1    Sack, J.S.2    Greenhough, T.J.3
  • 48
    • 0031893953 scopus 로고    scopus 로고
    • Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence
    • DOI 10.1074/jbc.273.4.2174
    • Barth, A.; Martin, S. R.; Bayley, P. M. Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence J. Biol. Chem. 1998, 273, 2174-2183 (Pubitemid 28069268)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2174-2183
    • Barth, A.1    Martin, S.R.2    Bayley, P.M.3
  • 49
    • 0022558415 scopus 로고
    • 2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study
    • 2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study Biochem. J. 1986, 238, 485-490 (Pubitemid 16008520)
    • (1986) Biochemical Journal , vol.238 , Issue.2 , pp. 485-490
    • Martin, S.R.1    Bayley, P.M.2
  • 50
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse, S.; Helmersson, A.; Forsén, S. Calcium binding to calmodulin and its globular domains J. Biol. Chem. 1991, 266, 8050-8059
    • (1991) J. Biol. Chem. , vol.266 , pp. 8050-8059
    • Linse, S.1    Helmersson, A.2    Forsén, S.3
  • 51
    • 0034854231 scopus 로고    scopus 로고
    • Intein-mediated ligation and cyclization of expressed proteins
    • Xu, M. Q.; Evans, T. C., Jr. Intein-mediated ligation and cyclization of expressed proteins Methods 2001, 24, 257-77
    • (2001) Methods , vol.24 , pp. 257-277
    • Xu, M.Q.1    Evans Jr., T.C.2
  • 52
    • 0030802865 scopus 로고    scopus 로고
    • Preparation of peptide thioesters using Fmoc-solid-phase peptide synthesis and its application to the construction of a template-assembled synthetic protein (TASP)
    • DOI 10.1016/S0040-4039(97)01434-2, PII S0040403997014342
    • Futaki, S.; Sogawa, K.; Maruyama, J.; Asahara, T.; Niwa, M.; Hojo, H. Preparation of peptide thioesters using Fmoc-solid-phase peptide synthesis and its application to the construction of a template-assembled synthetic protein (TASP) Tetrahedron Lett. 1997, 38, 6237-6240 (Pubitemid 27362166)
    • (1997) Tetrahedron Letters , vol.38 , Issue.35 , pp. 6237-6240
    • Futaki, S.1    Sogawa, K.2    Maruyama, J.3    Asahara, T.4    Niwa, M.5    Hojo, H.6
  • 53
    • 77952286058 scopus 로고    scopus 로고
    • Metal-assisted channel stabilization: Disposition of a single histidine on the N-terminus of alamethicin yields channels with extraordinarily long lifetimes
    • Noshiro, D.; Asami, K.; Futaki, S. Metal-assisted channel stabilization: disposition of a single histidine on the N-terminus of alamethicin yields channels with extraordinarily long lifetimes Biophys. J. 2010, 98, 1801-1808
    • (2010) Biophys. J. , vol.98 , pp. 1801-1808
    • Noshiro, D.1    Asami, K.2    Futaki, S.3
  • 56
    • 75649100915 scopus 로고    scopus 로고
    • Biological nanopores for single-molecule biophysics
    • Ma, L.; Cockroft, S. L. Biological nanopores for single-molecule biophysics ChemBioChem 2010, 11, 25-34
    • (2010) ChemBioChem , vol.11 , pp. 25-34
    • Ma, L.1    Cockroft, S.L.2
  • 57
  • 58
    • 79951535324 scopus 로고    scopus 로고
    • Tuning the cavity of cyclodextrins: Altered sugar adaptors in protein pores
    • Li, W. W.; Claridge, T. D.; Li, Q.; Wormald, M. R.; Davis, B. G.; Bayley, H. Tuning the cavity of cyclodextrins: altered sugar adaptors in protein pores J. Am. Chem. Soc. 2011, 133, 1987-2001
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1987-2001
    • Li, W.W.1    Claridge, T.D.2    Li, Q.3    Wormald, M.R.4    Davis, B.G.5    Bayley, H.6
  • 59
  • 61
    • 33845542689 scopus 로고    scopus 로고
    • Lipid bilayer formation by contacting monolayers in a microfluidic device for membrane protein analysis
    • DOI 10.1021/ac0613479
    • Funakoshi, K.; Suzuki, H.; Takeuchi, S. Lipid bilayer formation by contacting monolayers in a microfluidic device for membrane protein analysis Anal. Chem. 2006, 78, 8169-8174 (Pubitemid 44927591)
    • (2006) Analytical Chemistry , vol.78 , Issue.24 , pp. 8169-8174
    • Funakoshi, K.1    Suzuki, H.2    Takeuchi, S.3
  • 62
    • 84864255691 scopus 로고    scopus 로고
    • Signal transduction using an artificial receptor system that undergoes dimerization upon addition of a bivalent leucine-zipper ligand
    • Nakase, I.; Okumura, S.; Tanaka, G.; Osaki, K.; Imanishi, M.; Futaki, S. Signal transduction using an artificial receptor system that undergoes dimerization upon addition of a bivalent leucine-zipper ligand Angew. Chem., Int. Ed. 2012, 51, 7464-7467
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 7464-7467
    • Nakase, I.1    Okumura, S.2    Tanaka, G.3    Osaki, K.4    Imanishi, M.5    Futaki, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.