메뉴 건너뛰기




Volumn 13, Issue 8, 2004, Pages 1988-1996

Orientation and helical conformation of a tissue-specific hunter-killer peptide in micelles

Author keywords

Apoptosis; Circular dichroism; NMR; Peptide

Indexed keywords

ALANINE; AMINO ACID; CALCEIN; DODECYLPHOSPHORYLCHOLINE; HUNTER KILLER PEPTIDE; LEUCINE; PEPTIDE; UNCLASSIFIED DRUG;

EID: 3342948293     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04853204     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 0032535999 scopus 로고    scopus 로고
    • Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model
    • Arap, W., Pasqualini, R., and Ruoslahti, E. 1998. Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model. Science 279: 377-380.
    • (1998) Science , vol.279 , pp. 377-380
    • Arap, W.1    Pasqualini, R.2    Ruoslahti, E.3
  • 3
    • 5144233105 scopus 로고
    • Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. and Davies, D.G. 1985. Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65: 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davies, D.G.2
  • 4
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle, S.E. and Houghten, R.A. 1992. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 31: 12688-12694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 5
    • 0019464732 scopus 로고
    • Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies
    • Brown, L., Bosch, C., and Wüthrich, K. 1981. Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies. Biochim. Biophys. Acta 642: 296-312.
    • (1981) Biochim. Biophys. Acta , vol.642 , pp. 296-312
    • Brown, L.1    Bosch, C.2    Wüthrich, K.3
  • 6
    • 33947091567 scopus 로고
    • The 9-fluorenylmethoxycarbonyl amino-protecting group
    • Carpino, L.A. and Han, G.Y. 1972. The 9-fluorenylmethoxycarbonyl amino-protecting group. J. Org. Chem. 37: 3404-3409.
    • (1972) J. Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 8
    • 4244120872 scopus 로고
    • Micro determination of phosphorus
    • Chen, P.S., Toribara, T.Y., and Warner, H. 1956. Micro determination of phosphorus. Anal. Chem. 28: 1756-1758.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 11
    • 0026571369 scopus 로고
    • Conformation analysis of a 12-residue analogue of mastoparan and of mastoparan-X
    • Faerman, C.H. and Ripoll, D.R. 1992. Conformation analysis of a 12-residue analogue of mastoparan and of mastoparan-X. Proteins 112: 111-116.
    • (1992) Proteins , vol.112 , pp. 111-116
    • Faerman, C.H.1    Ripoll, D.R.2
  • 12
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit, E., Boman, A., Boman, H.G., and Shai, Y. 1995. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34: 11479-11488.
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 14
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 9: 127-135.
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 15
    • 0035115807 scopus 로고    scopus 로고
    • Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue
    • Hara, T., Kodama, H., Kondo, M., Wakamatsu, K., Takeda, A., Tachi, T., and Matsuzaki, K. 2001. Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue. Biopolymers 58: 437-446.
    • (2001) Biopolymers , vol.58 , pp. 437-446
    • Hara, T.1    Kodama, H.2    Kondo, M.3    Wakamatsu, K.4    Takeda, A.5    Tachi, T.6    Matsuzaki, K.7
  • 16
    • 0020484560 scopus 로고
    • Thermodynamics of stacking and of self-association of dinucleoside monphosphate m2(6)A-U from proton NMR chemical shifts: Differential concentration temperature profile method
    • Hartel, A.J., Lankhorst, P.P., and Altona, C. 1982. Thermodynamics of stacking and of self-association of dinucleoside monphosphate m2(6)A-U from proton NMR chemical shifts: Differential concentration temperature profile method. Eur. J. Biochem. 129: 343-357.
    • (1982) Eur. J. Biochem. , vol.129 , pp. 343-357
    • Hartel, A.J.1    Lankhorst, P.P.2    Altona, C.3
  • 17
    • 0028914586 scopus 로고
    • Peptide ligands for integrin α v β 3 selected from random phage display libraries
    • Healy, J.M., Murayama, O., Maeda, T., Yoshino, K., Sekiguchi, K., and Kikuchi, M. 1995. Peptide ligands for integrin α v β 3 selected from random phage display libraries. Biochemistry 34: 3948-3955.
    • (1995) Biochemistry , vol.34 , pp. 3948-3955
    • Healy, J.M.1    Murayama, O.2    Maeda, T.3    Yoshino, K.4    Sekiguchi, K.5    Kikuchi, M.6
  • 18
    • 0031590313 scopus 로고    scopus 로고
    • A cytoplasmic peptide of the neurotrophin receptor p75NTR: Induction of apoptosis and NMR determined helical conformation
    • Hileman, M.R., Chapman, B.S., Rabizadeh, S., Krishnan, V.V., Bredesen, D., Assa-Munt, N. and Plesniak, L.A. 1997. A cytoplasmic peptide of the neurotrophin receptor p75NTR: Induction of apoptosis and NMR determined helical conformation. FEBS Lett. 415: 145-154.
    • (1997) FEBS Lett. , vol.415 , pp. 145-154
    • Hileman, M.R.1    Chapman, B.S.2    Rabizadeh, S.3    Krishnan, V.V.4    Bredesen, D.5    Assa-Munt, N.6    Plesniak, L.A.7
  • 19
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope, M.J., Bally, M.B., Webb, G., and Cullis, P.R. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta 812: 55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 21
    • 0027208289 scopus 로고
    • Phospholipid asymmetry of the outer membrane of rat liver mitochondria. Evidence for the presence of cardiolipin on the outside of the outer membrane
    • Hovius, R., Thijssen, J., van der Linden, P., Nicolay, K., and de Kruijff, B. 1993. Phospholipid asymmetry of the outer membrane of rat liver mitochondria. Evidence for the presence of cardiolipin on the outside of the outer membrane. FEBS Lett. 330: 71-76.
    • (1993) FEBS Lett. , vol.330 , pp. 71-76
    • Hovius, R.1    Thijssen, J.2    Van Der Linden, P.3    Nicolay, K.4    De Kruijff, B.5
  • 23
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachman, P., and Ernst, R.R. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71: 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 24
    • 0042420680 scopus 로고    scopus 로고
    • A left-handed α-helix containing both L- and D-amino acids: The solution structure of the antimicrobial lipodepsipeptide tolaasin
    • Jourdan, F., Lazzaroni, S., Mendez, B.L., Lo Cantore, P., de Julio, M., Amodeo, P., Iacobellis, N.S., Evidente, A., and Motta, A. 2003. A left-handed α-helix containing both L- and D-amino acids: The solution structure of the antimicrobial lipodepsipeptide tolaasin. Proteins 52: 534-543.
    • (2003) Proteins , vol.52 , pp. 534-543
    • Jourdan, F.1    Lazzaroni, S.2    Mendez, B.L.3    Lo Cantore, P.4    De Julio, M.5    Amodeo, P.6    Iacobellis, N.S.7    Evidente, A.8    Motta, A.9
  • 25
    • 0029974513 scopus 로고    scopus 로고
    • Determinants in the presequence of cytochrome B2 for import into mitochondria and for proteolytic processing
    • Klaus, C., Guiard, B., Neupert, W., and Brunner, M. 1996. Determinants in the presequence of cytochrome B2 for import into mitochondria and for proteolytic processing. Eur. J. Biochem. 236: 856-861.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 856-861
    • Klaus, C.1    Guiard, B.2    Neupert, W.3    Brunner, M.4
  • 26
    • 2942703809 scopus 로고    scopus 로고
    • Reversal of obesity by targeted ablation of adipose tissue
    • Epub May 9
    • Kolonin, M., Saha, P.K., Chan, L., Pasqualini, R., and Arap, W. 2004. Reversal of obesity by targeted ablation of adipose tissue. Nat. Med. Epub May 9, 1-8.
    • (2004) Nat. Med. , pp. 1-8
    • Kolonin, M.1    Saha, P.K.2    Chan, L.3    Pasqualini, R.4    Arap, W.5
  • 27
    • 0030810336 scopus 로고    scopus 로고
    • Mastoparan-induced apoptosis of cultured cerebellar granule neurons is initiated by calcium release from intracellular stores
    • Lin, S.Z., Yan, G.M., Koch, K.E., Paul, S.M., and Irwin, R.P. 1997. Mastoparan-induced apoptosis of cultured cerebellar granule neurons is initiated by calcium release from intracellular stores. Brain Res. 771: 184-195.
    • (1997) Brain Res. , vol.771 , pp. 184-195
    • Lin, S.Z.1    Yan, G.M.2    Koch, K.E.3    Paul, S.M.4    Irwin, R.P.5
  • 28
    • 0342976767 scopus 로고
    • Improved solvent suppression in 1-dimensional and 2-dimensional NMR spectra by convolution of time-domain data
    • Marion, D., Ikura, M., and Bax, A. 1989. Improved solvent suppression in 1-dimensional and 2-dimensional NMR spectra by convolution of time-domain data. J. Magn. Reson 84: 425-430.
    • (1989) J. Magn. Reson. , vol.84 , pp. 425-430
    • Marion, D.1    Ikura, M.2    Bax, A.3
  • 30
    • 0027660404 scopus 로고
    • Permeabilization and morphological changes in phosphatidylglycerol bilayers induced by an antimicrobial peptide, tachyplesin I
    • Matsuzaki, K., Fujii, N., Fujii, N., and Miyajima, K. 1993. Permeabilization and morphological changes in phosphatidylglycerol bilayers induced by an antimicrobial peptide, tachyplesin I. Colloid Polym. Sci. 271: 901-908.
    • (1993) Colloid Polym. Sci. , vol.271 , pp. 901-908
    • Matsuzaki, K.1    Fujii, N.2    Fujii, N.3    Miyajima, K.4
  • 31
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., Murase, O., Tokuda, H., Funakoshi, S., Fujii, N., and Miyahima, K. 1994. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 33: 3342-3349.
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyahima, K.6
  • 32
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. 1995a. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry 34: 6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 33
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki, K., Murase, O., and Miyahima, K. 1995b. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 34: 12553-12559.
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyahima, K.3
  • 34
    • 0030037217 scopus 로고    scopus 로고
    • Transbilayer transport of ions and lipids coupled with mastoparan X translocation
    • Matsuzaki, K., Yoneyama, S., Murase, O., and Miyajima, K. 1996. Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry 35: 8450-8456.
    • (1996) Biochemistry , vol.35 , pp. 8450-8456
    • Matsuzaki, K.1    Yoneyama, S.2    Murase, O.3    Miyajima, K.4
  • 35
    • 0036205144 scopus 로고    scopus 로고
    • Transient vesicle leakage initiated by a synthetic apoptotic peptide derived from the death domain of neurotrophin receptor, p75NTR
    • Medina, M.L., Chapman, B.S., Bolender, J.P., and Plesniak, L.A. 2002. Transient vesicle leakage initiated by a synthetic apoptotic peptide derived from the death domain of neurotrophin receptor, p75NTR. J. Peptide Res. 59: 149-158.
    • (2002) J. Peptide Res. , vol.59 , pp. 149-158
    • Medina, M.L.1    Chapman, B.S.2    Bolender, J.P.3    Plesniak, L.A.4
  • 36
    • 0029115958 scopus 로고
    • Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin
    • Meininger, D.P., Hunter, M.J., and Komives, E.A. 1995. Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin. Protein Sci. 4: 1683-1695.
    • (1995) Protein Sci. , vol.4 , pp. 1683-1695
    • Meininger, D.P.1    Hunter, M.J.2    Komives, E.A.3
  • 38
    • 0023873256 scopus 로고
    • An NMR study of polymorphous behaviour of the mismatched DNA octamer d(m5C-6-m5C-G-A-G-m5C-6) in solution. The B-duplex and hairpin forms
    • Orbons, L.P.M., van der Marel, G.A., van Boom, J.H., and Altona, C. 1987. An NMR study of polymorphous behaviour of the mismatched DNA octamer d(m5C-6-m5C-G-A-G-m5C-6) in solution. The B-duplex and hairpin forms. Eur. J. Biochem. 170: 225-239.
    • (1987) Eur. J. Biochem. , vol.170 , pp. 225-239
    • Orbons, L.P.M.1    Van Der Marel, G.A.2    Van Boom, J.H.3    Altona, C.4
  • 39
    • 0028905958 scopus 로고
    • The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition
    • Pfieffer, D.R., Gudz, T.I., Novgorodov, S.A., and Erdahl, W.L. 1995. The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition. J. Biol. Chem. 270: 4923-4932.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4923-4932
    • Pfieffer, D.R.1    Gudz, T.I.2    Novgorodov, S.A.3    Erdahl, W.L.4
  • 40
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 41
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., Rapaport, D., Mor, A., Nicolas, P., and Shai, Y. 1992. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31: 12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 43
    • 0022725788 scopus 로고
    • A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers
    • Roise, D., Horvath, S.J., Tomich, J.M., Richards, J.H., and Schatz, G. 1986. A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J. 5: 1327-1334.
    • (1986) EMBO J. , vol.5 , pp. 1327-1334
    • Roise, D.1    Horvath, S.J.2    Tomich, J.M.3    Richards, J.H.4    Schatz, G.5
  • 44
    • 0029314345 scopus 로고
    • 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: Application to mastoparan X solubilized in n-ocylglucoside
    • 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: Application to mastoparan X solubilized in n-ocylglucoside. J. Biomol. NMR 5: 345-352.
    • (1995) J. Biomol. NMR , vol.5 , pp. 345-352
    • Seigneruret, M.1    Levy, D.2
  • 45
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. 1995. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20: 460-464.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 46
    • 0026734546 scopus 로고
    • Membrane-bound conformation of mastoparan-X, a G-protein-activating peptide
    • Wakamatsu, K., Okada, A., Miyazawa, T., Ohya, M., and Higashijima, T. 1992. Membrane-bound conformation of mastoparan-X, a G-protein-activating peptide. Biochemistry 31: 5654-5660.
    • (1992) Biochemistry , vol.31 , pp. 5654-5660
    • Wakamatsu, K.1    Okada, A.2    Miyazawa, T.3    Ohya, M.4    Higashijima, T.5
  • 47
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D., and Richards, F.M. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222: 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 48
    • 0026597879 scopus 로고
    • The chemical shift index - A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • -. 1992. The chemical shift index-A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.