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Volumn 125, Issue 4, 1999, Pages 705-712

Structure-function relationship of model Aib-containing peptides as ion transfer intermembrane templates

Author keywords

Aib (2 aminoisobutyric acid) peptide; Antimicrobial activity; Ion channel activity; Peptide chain aggregation; Solid phase peptide synthesis

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; ION CHANNEL; PEPTAIBOL; PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; TETRAMER;

EID: 0032930050     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022340     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0026734109 scopus 로고
    • Tracing the roots of ion channels
    • Jan, L.Y. and Jan, Y.N. (1992) Tracing the roots of ion channels. Cell 69, 715-718
    • (1992) Cell , vol.69 , pp. 715-718
    • Jan, L.Y.1    Jan, Y.N.2
  • 2
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. (1997) Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156, 197-211
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 3
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom, M.S.P. (1993) Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26, 365-421
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.S.P.1
  • 4
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J.D., Wasserman, Z.R., andDeGrado, W.F. (1988) Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177-1181
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 5
    • 0027275498 scopus 로고
    • Orientation and aggregation of hydrophobic helical peptides in phospholipid bilayer membrane
    • Otoda, K., Kimura, S., and Imanishi, Y. (1993) Orientation and aggregation of hydrophobic helical peptides in phospholipid bilayer membrane. Biochim. Biophys. Acta 1150, 1-8
    • (1993) Biochim. Biophys. Acta , vol.1150 , pp. 1-8
    • Otoda, K.1    Kimura, S.2    Imanishi, Y.3
  • 6
    • 37049078481 scopus 로고
    • Effect of cation binding to hydrophobic helical peptides on orientation, aggregation, and ion-channel activity in phospholipid bilayer membranes
    • Otoda, K., Kimura, S., and Imanishi, Y. (1993) Effect of cation binding to hydrophobic helical peptides on orientation, aggregation, and ion-channel activity in phospholipid bilayer membranes. J. Chem. Soc., Perkin Trans. 1, 3011-3016
    • (1993) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 3011-3016
    • Otoda, K.1    Kimura, S.2    Imanishi, Y.3
  • 7
    • 37049082263 scopus 로고
    • Changes in conformation and antimicrobial properties caused by replacement of D-amino acids with α-amino-isobutyric acid in the gramicidin backbone: Synthesis and circular dichroic studies
    • Jelokhani-Niaraki, M., Yoshioka, K., Takahashi, H., Kato, F., and Kondo, M. (1992) Changes in conformation and antimicrobial properties caused by replacement of D-amino acids with α-amino-isobutyric acid in the gramicidin backbone: synthesis and circular dichroic studies. J. Chem. Soc., Perkin Trans. 2, 1187-1193
    • (1992) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1187-1193
    • Jelokhani-Niaraki, M.1    Yoshioka, K.2    Takahashi, H.3    Kato, F.4    Kondo, M.5
  • 8
    • 37049073063 scopus 로고
    • Conformational studies and pore-forming properties of α-aminoisobutyric acid analogue of gramicidin B
    • Jelokhani-Niaraki, M., Kodama, H., Ehara, T., and Kondo, M. (1995) Conformational studies and pore-forming properties of α-aminoisobutyric acid analogue of gramicidin B. J. Chem. Soc., Perkin Trans. 2, 801-808
    • (1995) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 801-808
    • Jelokhani-Niaraki, M.1    Kodama, H.2    Ehara, T.3    Kondo, M.4
  • 9
    • 0031970684 scopus 로고    scopus 로고
    • Interaction and orientation of an α-aminoisobutyric acid- and tryptophan-containing short helical peptide pore-former in phospholipid vesicles, as revealed by fluorescence spectroscopy
    • Jelokhani-Niaraki, M., Nakashima, K., Kodama, H., and Kondo, M. (1998) Interaction and orientation of an α-aminoisobutyric acid-and tryptophan-containing short helical peptide pore-former in phospholipid vesicles, as revealed by fluorescence spectroscopy. J. Biochem. 123, 790-797
    • (1998) J. Biochem. , vol.123 , pp. 790-797
    • Jelokhani-Niaraki, M.1    Nakashima, K.2    Kodama, H.3    Kondo, M.4
  • 12
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N. and Woody, R.W. (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 13
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G.R. (1959) Phosphorus assay in column chromatography. J. Biol. Chem. 234, 466-468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 14
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols model ion channels
    • Sansom, M.S.P. (1993) Alamethicin and related peptaibols model ion channels. Eur. Biophys. J. 22, 105-124
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.P.1
  • 15
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphiphatic helical peptides
    • Epand, R.M., Shai, Y., Sgrest, J.P., and Anantharamainh, G.M. (1995) Mechanisms for the modulation of membrane bilayer properties by amphiphatic helical peptides. Biopolymers 37, 319-338
    • (1995) Biopolymers , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.2    Sgrest, J.P.3    Anantharamainh, G.M.4
  • 16
    • 0015767632 scopus 로고
    • An obligatory α-helical amino acid residue
    • Burgess, A.W. and Leach, S.J. (1973) An obligatory α-helical amino acid residue. Biopolymers 12, 2599-2605
    • (1973) Biopolymers , vol.12 , pp. 2599-2605
    • Burgess, A.W.1    Leach, S.J.2
  • 18
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphiphilic α-helical model peptides of various chain lengths
    • Agawa, Y., Lee, S., Ono, S., Aoyagi, H., Ohno, M., Taniguchi, T., Anzai, K., and Kirino, Y. (1991) Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphiphilic α-helical model peptides of various chain lengths. J. Biol. Chem. 266, 20218-20222
    • (1991) J. Biol. Chem. , vol.266 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Ohno, M.5    Taniguchi, T.6    Anzai, K.7    Kirino, Y.8
  • 19
    • 0030057655 scopus 로고    scopus 로고
    • Flexibility in peptide molecules and restraints imposed by hydrogen bonds, the aib residue, and core inserts
    • Karle, I.L. (1996) Flexibility in peptide molecules and restraints imposed by hydrogen bonds, the aib residue, and core inserts. Biopolymers 40, 157-180
    • (1996) Biopolymers , vol.40 , pp. 157-180
    • Karle, I.L.1
  • 20
    • 0025268582 scopus 로고
    • pH-dependent interaction of amphiphilic polypeptide poly(Lys-Aib-Leu-Aib) with lipid bilayer membrane
    • Kono, K., Kimura, S., and Imanishi, Y. (1990) pH-dependent interaction of amphiphilic polypeptide poly(Lys-Aib-Leu-Aib) with lipid bilayer membrane. Biochemistry 29, 3631-3637
    • (1990) Biochemistry , vol.29 , pp. 3631-3637
    • Kono, K.1    Kimura, S.2    Imanishi, Y.3
  • 21
    • 37049067297 scopus 로고
    • Amphiphilic α-helical structure in water stabilized by dioctadecyl chain
    • Zhao, J., Kimura, S., and Imanishi, Y. (1995) Amphiphilic α-helical structure in water stabilized by dioctadecyl chain. J. Chem. Soc., Perkin Trans. 2, 2243-2248
    • (1995) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 2243-2248
    • Zhao, J.1    Kimura, S.2    Imanishi, Y.3
  • 22
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of α-helices
    • Shoemaker, K.R., Kim, P.S., York, E.J., Stewart, J.M., and Baldwin, R.L. (1987) Tests of the helix dipole model for stabilization of α-helices. Nature 326, 563-567
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 23
    • 0027212028 scopus 로고
    • Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions
    • Dasgupta, S. and Bell, J.A. (1993) Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions. Int. J. Pept. Protein Res. 41, 499-511
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 499-511
    • Dasgupta, S.1    Bell, J.A.2
  • 24
    • 0030698182 scopus 로고    scopus 로고
    • Coupling reagents and activation
    • Alberico, F. and Carpino, L.A. (1997) Coupling reagents and activation. Methods Enzymol. 289, 104-126
    • (1997) Methods Enzymol. , vol.289 , pp. 104-126
    • Alberico, F.1    Carpino, L.A.2
  • 25
    • 0000528761 scopus 로고
    • Fmoc amino acid fluorides: Convenient reagents for the solid-phase assembly of peptides incorporating sterically hindered residues
    • Wenschuh, H., Beyermann, M., Krause, E., Brudel, M., Winter, R., Schumann, M., Carpino, L.A., and Bienert, M. (1994) Fmoc amino acid fluorides: convenient reagents for the solid-phase assembly of peptides incorporating sterically hindered residues. J. Org. Chem. 59, 3275-3280
    • (1994) J. Org. Chem. , vol.59 , pp. 3275-3280
    • Wenschuh, H.1    Beyermann, M.2    Krause, E.3    Brudel, M.4    Winter, R.5    Schumann, M.6    Carpino, L.A.7    Bienert, M.8
  • 26
    • 0028862474 scopus 로고
    • Stepwise automated solid phase synthesis of naturally occurring peptaibols using Fmoc amino acid fluorides
    • Wenschuh, H., Beyermann, M., Haber, H., Seydel, J.K., Krause, E., and Bienert, M. (1995) Stepwise automated solid phase synthesis of naturally occurring peptaibols using Fmoc amino acid fluorides. J. Org. Chem. 60, 405-410
    • (1995) J. Org. Chem. , vol.60 , pp. 405-410
    • Wenschuh, H.1    Beyermann, M.2    Haber, H.3    Seydel, J.K.4    Krause, E.5    Bienert, M.6
  • 29
    • 0023714070 scopus 로고
    • Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 protease
    • Schneider, J. and Kent, S.B. (1988) Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 protease. Cell 54, 363-368
    • (1988) Cell , vol.54 , pp. 363-368
    • Schneider, J.1    Kent, S.B.2
  • 30
    • 0019493825 scopus 로고
    • Synthetic model for two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization of an 86-residue analog of tropomyosin
    • Hodges, R.S., Saund, A.K., Chong, P.C.S., St.-Pierre, S.A., and Reid, R.E. (1981) Synthetic model for two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization of an 86-residue analog of tropomyosin. J. Biol. Chem. 256, 1214-1224
    • (1981) J. Biol. Chem. , vol.256 , pp. 1214-1224
    • Hodges, R.S.1    Saund, A.K.2    Chong, P.C.S.3    St.-Pierre, S.A.4    Reid, R.E.5
  • 31
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure
    • Lau, S.Y.M., Taneja, A.K., and Hodges, R.S. (1984) Synthesis of a model protein of defined secondary and quaternary structure. J. Biol. Chem. 259, 13253-13261
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 33
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal, G. and Nagaraj, R. (1994) Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta 1197, 109-131
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 34
    • 0025761657 scopus 로고
    • Cytolytic pore-forming proteins and peptides: Is there a common structural motif?
    • Ojcius, D.M. and Young, J.D.E. (1991) Cytolytic pore-forming proteins and peptides: is there a common structural motif? Trends Biochem. Sci. 16, 225-229
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.E.2
  • 35
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning helices
    • Shai, Y. (1995) Molecular recognition between membrane-spanning helices. Trends Biochem. Sci. 20, 460-464
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1


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