메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

High Yield Production and Refolding of the Double-Knot Toxin, an Activator of TRPV1 Channels

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE KNOT TOXIN; SPIDER VENOM; UNCLASSIFIED DRUG; VANILLOID RECEPTOR 1;

EID: 84871166454     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051516     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 83255191679 scopus 로고    scopus 로고
    • Spider bite
    • Isbister GK, Fan HW, (2011) Spider bite. Lancet 378: 2039-2047.
    • (2011) Lancet , vol.378 , pp. 2039-2047
    • Isbister, G.K.1    Fan, H.W.2
  • 3
    • 0024562287 scopus 로고
    • Two classes of channel-specific toxins from funnel web spider venom
    • Adams ME, Herold EE, Venema VJ, (1989) Two classes of channel-specific toxins from funnel web spider venom. J Comp Physiol A 164: 333-342.
    • (1989) J Comp Physiol A , vol.164 , pp. 333-342
    • Adams, M.E.1    Herold, E.E.2    Venema, V.J.3
  • 4
    • 79251641918 scopus 로고    scopus 로고
    • Nigriventrine: a low molecular mass neuroactive compound from the venom of the spider Phoneutria nigriventer
    • Gomes PC, de Souza BM, Dias NB, Cesar-Tognoli LM, Silva-Filho LC, et al. (2011) Nigriventrine: a low molecular mass neuroactive compound from the venom of the spider Phoneutria nigriventer. Toxicon 57: 266-274.
    • (2011) Toxicon , vol.57 , pp. 266-274
    • Gomes, P.C.1    de Souza, B.M.2    Dias, N.B.3    Cesar-Tognoli, L.M.4    Silva-Filho, L.C.5
  • 5
    • 28244475780 scopus 로고    scopus 로고
    • An inhibitor of TRPV1 channels isolated from funnel Web spider venom
    • Kitaguchi T, Swartz KJ, (2005) An inhibitor of TRPV1 channels isolated from funnel Web spider venom. Biochemistry 44: 15544-15549.
    • (2005) Biochemistry , vol.44 , pp. 15544-15549
    • Kitaguchi, T.1    Swartz, K.J.2
  • 6
    • 0942279703 scopus 로고    scopus 로고
    • Solution structure and functional characterization of SGTx1, a modifier of Kv2.1 channel gating
    • Lee CW, Kim S, Roh SH, Endoh H, Kodera Y, et al. (2004) Solution structure and functional characterization of SGTx1, a modifier of Kv2.1 channel gating. Biochemistry 43: 890-897.
    • (2004) Biochemistry , vol.43 , pp. 890-897
    • Lee, C.W.1    Kim, S.2    Roh, S.H.3    Endoh, H.4    Kodera, Y.5
  • 7
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas P, Diochot S, Corzo G, (2000) Structure and pharmacology of spider venom neurotoxins. Biochimie 82: 893-907.
    • (2000) Biochimie , vol.82 , pp. 893-907
    • Escoubas, P.1    Diochot, S.2    Corzo, G.3
  • 8
    • 0037189567 scopus 로고    scopus 로고
    • Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins
    • Corzo G, Villegas E, Gomez-Lagunas F, Possani LD, Belokoneva OS, et al. (2002) Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. J Biol Chem 277: 23627-23637.
    • (2002) J Biol Chem , vol.277 , pp. 23627-23637
    • Corzo, G.1    Villegas, E.2    Gomez-Lagunas, F.3    Possani, L.D.4    Belokoneva, O.S.5
  • 9
    • 1942438979 scopus 로고    scopus 로고
    • Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta
    • Adams ME, (2004) Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta. Toxicon 43: 509-525.
    • (2004) Toxicon , vol.43 , pp. 509-525
    • Adams, M.E.1
  • 10
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz KJ, MacKinnon R, (1995) An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron 15: 941-949.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 11
    • 0028111357 scopus 로고
    • Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta
    • Nicholson GM, Willow M, Howden ME, Narahashi T, (1994) Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta. Pflugers Arch 428: 400-409.
    • (1994) Pflugers Arch , vol.428 , pp. 400-409
    • Nicholson, G.M.1    Willow, M.2    Howden, M.E.3    Narahashi, T.4
  • 12
    • 0028872342 scopus 로고
    • Inhibition of acetylcholine release from mouse motor nerve by a P-type calcium channel blocker, omega-agatoxin IVA
    • Hong SJ, Chang CC, (1995) Inhibition of acetylcholine release from mouse motor nerve by a P-type calcium channel blocker, omega-agatoxin IVA. J Physiol 482 (Pt 2): 283-290.
    • (1995) J Physiol , vol.482 , Issue.Pt 2 , pp. 283-290
    • Hong, S.J.1    Chang, C.C.2
  • 13
    • 0029084407 scopus 로고
    • Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers
    • Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, et al. (1995) Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers. J Mol Biol 250: 659-671.
    • (1995) J Mol Biol , vol.250 , pp. 659-671
    • Kim, J.I.1    Konishi, S.2    Iwai, H.3    Kohno, T.4    Gouda, H.5
  • 14
    • 17644381598 scopus 로고    scopus 로고
    • Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel
    • Jung HJ, Lee JY, Kim SH, Eu YJ, Shin SY, et al. (2005) Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel. Biochemistry 44: 6015-6023.
    • (2005) Biochemistry , vol.44 , pp. 6015-6023
    • Jung, H.J.1    Lee, J.Y.2    Kim, S.H.3    Eu, Y.J.4    Shin, S.Y.5
  • 15
    • 0037435021 scopus 로고    scopus 로고
    • Functional analysis of an archaebacterial voltage-dependent K+ channel
    • Ruta V, Jiang Y, Lee A, Chen J, MacKinnon R, (2003) Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature 422: 180-185.
    • (2003) Nature , vol.422 , pp. 180-185
    • Ruta, V.1    Jiang, Y.2    Lee, A.3    Chen, J.4    MacKinnon, R.5
  • 16
    • 0030981657 scopus 로고    scopus 로고
    • The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider
    • Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, et al. (1997) The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol 4: 559-566.
    • (1997) Nat Struct Biol , vol.4 , pp. 559-566
    • Fletcher, J.I.1    Smith, R.2    O'Donoghue, S.I.3    Nilges, M.4    Connor, M.5
  • 17
    • 77953271751 scopus 로고    scopus 로고
    • A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
    • Bohlen CJ, Priel A, Zhou S, King D, Siemens J, et al. (2011) A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell 141: 834-845.
    • (2011) Cell , vol.141 , pp. 834-845
    • Bohlen, C.J.1    Priel, A.2    Zhou, S.3    King, D.4    Siemens, J.5
  • 18
    • 33750873334 scopus 로고    scopus 로고
    • Spider toxins activate the capsaicin receptor to produce inflammatory pain
    • Siemens J, Zhou S, Piskorowski R, Nikai T, Lumpkin EA, et al. (2006) Spider toxins activate the capsaicin receptor to produce inflammatory pain. Nature 444: 208-212.
    • (2006) Nature , vol.444 , pp. 208-212
    • Siemens, J.1    Zhou, S.2    Piskorowski, R.3    Nikai, T.4    Lumpkin, E.A.5
  • 19
    • 53049093899 scopus 로고    scopus 로고
    • Analgesic compound from sea anemone Heteractis crispa is the first polypeptide inhibitor of vanilloid receptor 1 (TRPV1)
    • Andreev YA, Kozlov SA, Koshelev SG, Ivanova EA, Monastyrnaya MM, et al. (2008) Analgesic compound from sea anemone Heteractis crispa is the first polypeptide inhibitor of vanilloid receptor 1 (TRPV1). J Biol Chem 283: 23914-23921.
    • (2008) J Biol Chem , vol.283 , pp. 23914-23921
    • Andreev, Y.A.1    Kozlov, S.A.2    Koshelev, S.G.3    Ivanova, E.A.4    Monastyrnaya, M.M.5
  • 20
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer WP, Crameri A, Ha KD, Brennan TM, Heyneker HL, (1995) Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164: 49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 21
    • 0017637022 scopus 로고
    • Cleavage at Asn-Gly bonds with hydroxylamine
    • Bornstein P, Balian G, (1977) Cleavage at Asn-Gly bonds with hydroxylamine. Methods Enzymol 47: 132-145.
    • (1977) Methods Enzymol , vol.47 , pp. 132-145
    • Bornstein, P.1    Balian, G.2
  • 22
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method
    • Raussens V, Ruysschaert JM, Goormaghtigh E, (2003) Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method. Anal Biochem 319: 114-121.
    • (2003) Anal Biochem , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 23
    • 18144366586 scopus 로고    scopus 로고
    • Expression and preparation of recombinant hepcidin in Escherichia coli
    • Zhang H, Yuan Q, Zhu Y, Ma R, (2005) Expression and preparation of recombinant hepcidin in Escherichia coli. Protein Expr Purif 41: 409-416.
    • (2005) Protein Expr Purif , vol.41 , pp. 409-416
    • Zhang, H.1    Yuan, Q.2    Zhu, Y.3    Ma, R.4
  • 24
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H, (1996) In vitro folding of inclusion body proteins. FASEB J 10: 49-56.
    • (1996) FASEB J , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 25
    • 33845761868 scopus 로고    scopus 로고
    • Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus
    • Pi C, Liu J, Wang L, Jiang X, Liu Y, et al. (2007) Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus. J Biotechnol 128: 184-193.
    • (2007) J Biotechnol , vol.128 , pp. 184-193
    • Pi, C.1    Liu, J.2    Wang, L.3    Jiang, X.4    Liu, Y.5
  • 26
    • 0242299749 scopus 로고    scopus 로고
    • A fusion protein of conotoxin MVIIA and thioredoxin expressed in Escherichia coli has significant analgesic activity
    • Zhan J, Chen X, Wang C, Qiu J, Ma F, et al. (2003) A fusion protein of conotoxin MVIIA and thioredoxin expressed in Escherichia coli has significant analgesic activity. Biochem Biophys Res Commun 311: 495-500.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 495-500
    • Zhan, J.1    Chen, X.2    Wang, C.3    Qiu, J.4    Ma, F.5
  • 27
    • 0028985407 scopus 로고
    • Tyr13 is essential for the activity of omega-conotoxin MVIIA and GVIA, specific N-type calcium channel blockers
    • Kim JI, Takahashi M, Ohtake A, Wakamiya A, Sato K, (1995) Tyr13 is essential for the activity of omega-conotoxin MVIIA and GVIA, specific N-type calcium channel blockers. Biochem Biophys Res Commun 206: 449-454.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 449-454
    • Kim, J.I.1    Takahashi, M.2    Ohtake, A.3    Wakamiya, A.4    Sato, K.5
  • 28
    • 0028782785 scopus 로고
    • Hydroxyl group of Tyr13 is essential for the activity of omega-conotoxin GVIA, a peptide toxin for N-type calcium channel
    • Kim JI, Takahashi M, Ogura A, Kohno T, Kudo Y, et al. (1994) Hydroxyl group of Tyr13 is essential for the activity of omega-conotoxin GVIA, a peptide toxin for N-type calcium channel. J Biol Chem 269: 23876-23878.
    • (1994) J Biol Chem , vol.269 , pp. 23876-23878
    • Kim, J.I.1    Takahashi, M.2    Ogura, A.3    Kohno, T.4    Kudo, Y.5
  • 29
    • 78650235303 scopus 로고    scopus 로고
    • Optimization of oxidative folding methods for cysteine-rich peptides: a study of conotoxins containing three disulfide bridges
    • Steiner AM, Bulaj G, (2011) Optimization of oxidative folding methods for cysteine-rich peptides: a study of conotoxins containing three disulfide bridges. J Pept Sci 17: 1-7.
    • (2011) J Pept Sci , vol.17 , pp. 1-7
    • Steiner, A.M.1    Bulaj, G.2
  • 30
    • 36148996891 scopus 로고    scopus 로고
    • Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of Conus peptides
    • Bulaj G, Olivera BM, (2008) Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of Conus peptides. Antioxid Redox Signal 10: 141-155.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 141-155
    • Bulaj, G.1    Olivera, B.M.2
  • 31
    • 0037382348 scopus 로고    scopus 로고
    • Detergent-assisted oxidative folding of delta-conotoxins
    • DeLa Cruz R, Whitby FG, Buczek O, Bulaj G, (2003) Detergent-assisted oxidative folding of delta-conotoxins. J Pept Res 61: 202-212.
    • (2003) J Pept Res , vol.61 , pp. 202-212
    • DeLa Cruz, R.1    Whitby, F.G.2    Buczek, O.3    Bulaj, G.4
  • 32
    • 0033613178 scopus 로고    scopus 로고
    • Synthesis, bioactivity, and cloning of the L-type calcium channel blocker omega-conotoxin TxVII
    • Sasaki T, Feng ZP, Scott R, Grigoriev N, Syed NI, et al. (1999) Synthesis, bioactivity, and cloning of the L-type calcium channel blocker omega-conotoxin TxVII. Biochemistry 38: 12876-12884.
    • (1999) Biochemistry , vol.38 , pp. 12876-12884
    • Sasaki, T.1    Feng, Z.P.2    Scott, R.3    Grigoriev, N.4    Syed, N.I.5
  • 33
    • 0034610399 scopus 로고    scopus 로고
    • Three-dimensional solution structure of omega-conotoxin TxVII, an L-type calcium channel blocker
    • Kobayashi K, Sasaki T, Sato K, Kohno T, (2000) Three-dimensional solution structure of omega-conotoxin TxVII, an L-type calcium channel blocker. Biochemistry 39: 14761-14767.
    • (2000) Biochemistry , vol.39 , pp. 14761-14767
    • Kobayashi, K.1    Sasaki, T.2    Sato, K.3    Kohno, T.4
  • 34
    • 1842786935 scopus 로고    scopus 로고
    • Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels
    • Wang JM, Roh SH, Kim S, Lee CW, Kim JI, et al. (2004) Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels. J Gen Physiol 123: 455-467.
    • (2004) J Gen Physiol , vol.123 , pp. 455-467
    • Wang, J.M.1    Roh, S.H.2    Kim, S.3    Lee, C.W.4    Kim, J.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.