메뉴 건너뛰기




Volumn 5, Issue 4, 1999, Pages 185-194

Structural requirements for cellular uptake of α-helical amphipathic peptides

Author keywords

Amphipathic peptides; Cellular uptake

Indexed keywords

AMINO ACID; SYNTHETIC PEPTIDE;

EID: 0032949646     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199904)5:4<185::AID-PSC184>3.0.CO;2-9     Document Type: Article
Times cited : (152)

References (30)
  • 1
    • 0028244315 scopus 로고
    • Transport of oligonucleotides across natural and model membranes
    • V.V. Vlassov, L.A. Balakireva and L.A. Yakubov (1994). Transport of oligonucleotides across natural and model membranes. Biochim. Biophys. Acta 1197, 95-108.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 95-108
    • Vlassov, V.V.1    Balakireva, L.A.2    Yakubov, L.A.3
  • 2
    • 0025949812 scopus 로고
    • Adenovirus enhancement of transferrin-polylysine-mediated gene delivery
    • D.T. Curiel, S. Agarwal, E. Wagner and M. Cotten (1991). Adenovirus enhancement of transferrin-polylysine-mediated gene delivery. Proc. Natl. Acad. Sci. USA 88, 8850-8854.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8850-8854
    • Curiel, D.T.1    Agarwal, S.2    Wagner, E.3    Cotten, M.4
  • 3
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia home-odomain translocates through biological membranes
    • D. Derossi, A.H. Joliot, G. Chassaing and A. Prochiantz (1994). The third helix of the Antennapedia home-odomain translocates through biological membranes. J. Biol. Chem. 269, 10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 4
    • 0030273590 scopus 로고    scopus 로고
    • Getting hydrophilic compounds into cells: Lessons from homeopeptides
    • A. Prochiantz (1996). Getting hydrophilic compounds into cells: lessons from homeopeptides. Curr. Opin. Neurobiol. 6, 629-634.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 629-634
    • Prochiantz, A.1
  • 5
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-kB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Y.-Z. Lin, S. Yao, R.A. Veach, T.R. Torgerson and J. Hawiger (1995). Inhibition of nuclear translocation of transcription factor NF-kB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 270, 14255-14258.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14255-14258
    • Lin, Y.-Z.1    Yao, S.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 7
    • 0030955260 scopus 로고    scopus 로고
    • Conformations of primary amphipathic carrier peptides in membrane mimicking environments
    • L. Chaloin, P. Vidal, A. Heitz, N. Van Mau, J. Mesery, G. Divita and F. Heitz (1997). Conformations of primary amphipathic carrier peptides in membrane mimicking environments. Biochemistry 36, 11179-11187.
    • (1997) Biochemistry , vol.36 , pp. 11179-11187
    • Chaloin, L.1    Vidal, P.2    Heitz, A.3    Van Mau, N.4    Mesery, J.5    Divita, G.6    Heitz, F.7
  • 8
    • 0030904245 scopus 로고    scopus 로고
    • Truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • E. Vives, P. Brodin and B.A. Lebleu (1997). Truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.A.3
  • 9
    • 0000021028 scopus 로고    scopus 로고
    • Nonendocytic, amphipathicity dependent cellular uptake of helical model peptides
    • J. Oehlke, E. Krause, B. Wiesner, M. Beyermann and M. Bienert (1996). Nonendocytic, amphipathicity dependent cellular uptake of helical model peptides. Protein Peptide Lett. 3, 393-398.
    • (1996) Protein Peptide Lett. , vol.3 , pp. 393-398
    • Oehlke, J.1    Krause, E.2    Wiesner, B.3    Beyermann, M.4    Bienert, M.5
  • 10
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • in press
    • J. Oehlke, A. Scheller, B. Wiesner, E. Krause, M. Beyermann, E. Klauschenz, M. Melzig and M. Bienert (1998). Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta, in press.
    • (1998) Biochim. Biophys. Acta
    • Oehlke, J.1    Scheller, A.2    Wiesner, B.3    Krause, E.4    Beyermann, M.5    Klauschenz, E.6    Melzig, M.7    Bienert, M.8
  • 11
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • D. Eisenberg (1984). Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 53, 595-623.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 12
    • 0002870324 scopus 로고
    • New uronium salts as coupling reagents in peptide chemistry
    • E. Giralt and D. Andreu, Eds, ESCOM, Leiden
    • P. Henklein, M. Beyermann, M. Bienert and R. Knorr. New uronium salts as coupling reagents in peptide chemistry, in: Peptides 1990, E. Giralt and D. Andreu, Eds, p. 67-68, ESCOM, Leiden, 1990.
    • (1990) Peptides 1990 , pp. 67-68
    • Henklein, P.1    Beyermann, M.2    Bienert, M.3    Knorr, R.4
  • 13
    • 0019255307 scopus 로고
    • Über die In-vitro-Kultivierung und das Verhalten von Aorten-Endothelzellen in einem serum-armen Nährmedium
    • W. Halle, A. Mann, W.-E. Siems and K.D. Jentzsch (1980). Über die In-vitro-Kultivierung und das Verhalten von Aorten-Endothelzellen in einem serum-armen Nährmedium. Acta Biol. Med. Germ. 39, 1165-1175.
    • (1980) Acta Biol. Med. Germ. , vol.39 , pp. 1165-1175
    • Halle, W.1    Mann, A.2    Siems, W.-E.3    Jentzsch, K.D.4
  • 14
    • 0028584448 scopus 로고
    • Utilization of endothelial cell monolayers of low tightness for estimation of transcellular transport characteristics of hydrophilic compounds
    • J. Oehlke, B. Savoly and I.E. Blasig (1994). Utilization of endothelial cell monolayers of low tightness for estimation of transcellular transport characteristics of hydrophilic compounds. Eur. J. Pharm. Sci. 2, 365-372.
    • (1994) Eur. J. Pharm. Sci. , vol.2 , pp. 365-372
    • Oehlke, J.1    Savoly, B.2    Blasig, I.E.3
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0025854825 scopus 로고
    • High-performance liquid chromatography packing materials for the analysis of small molecules in biological matrices by direct injection
    • T.C. Pinkerton (1991). High-performance liquid chromatography packing materials for the analysis of small molecules in biological matrices by direct injection. J. Chromatogr. 544, 13-23.
    • (1991) J. Chromatogr. , vol.544 , pp. 13-23
    • Pinkerton, T.C.1
  • 17
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • M. Dathe, T. Wieprecht, H. Nikolenko, L. Handel, W.L. Maloy, D.L., MacDonald, M. Beyermann and M. Bienert (1997). Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 403, 208-212.
    • (1997) FEBS Lett. , vol.403 , pp. 208-212
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    MacDonald, D.L.6    Beyermann, M.7    Bienert, M.8
  • 19
    • 0027411585 scopus 로고
    • SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
    • S. Felder, M. Zhou, P. Hu, J. Urena, A. Ullrich, M. Chaudhuri, M. White, S.E. Shoelson and J. Schlessinger (1993). SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13, 1449-1455.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1449-1455
    • Felder, S.1    Zhou, M.2    Hu, P.3    Urena, J.4    Ullrich, A.5    Chaudhuri, M.6    White, M.7    Shoelson, S.E.8    Schlessinger, J.9
  • 21
    • 0029066326 scopus 로고
    • Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins
    • B.S. Knudsen, J. Zheng, S.M. Feller, J.P. Mayer, S.K. Burrell, D. Cowburn and H. Hanatusa (1995). Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins. EMBO J. 14, 2191-2198.
    • (1995) EMBO J. , vol.14 , pp. 2191-2198
    • Knudsen, B.S.1    Zheng, J.2    Feller, S.M.3    Mayer, J.P.4    Burrell, S.K.5    Cowburn, D.6    Hanatusa, H.7
  • 22
    • 0030043913 scopus 로고    scopus 로고
    • Potent peptide analogues of a G-protein-receptor-binding region obtained with a combinatorial library
    • E.L. Martin, S. Rens-Domiano, P.J. Schatz and H.E. Hamm (1996). Potent peptide analogues of a G-protein-receptor-binding region obtained with a combinatorial library. J. Biol. Chem. 271, 361-366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 361-366
    • Martin, E.L.1    Rens-Domiano, S.2    Schatz, P.J.3    Hamm, H.E.4
  • 24
    • 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
    • G. Saberwal and R. Nagaraj (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. Blophys. Acta 1197, 109-131.
    • (1994) Biochim. Blophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 26
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • M. Dathe, M. Schümann, T. Wieprecht, A. Winkler, M. Beyermann, E. Krause, K. Matsuzaki, O. Murase and M. Bienert (1996). Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35, 12612-12622.
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schümann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 27
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • T. Wieprecht, M. Dathe, R.M. Epand, M. Beyemmann, E. Krause, W.L. Maloy, D.L. MacDonald and M. Bienert (1997). Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 36, 12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyemmann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 28
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • T.A. Rapoport, B. Jungnickel and U. Kutay (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 29
    • 0024350149 scopus 로고
    • Transport of proteins into mitochondria
    • N. Pfanner and W. Neupert (1989). Transport of proteins into mitochondria. Curr. Opin. Cell Biol. 1, 624-629.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 624-629
    • Pfanner, N.1    Neupert, W.2
  • 30
    • 0026909329 scopus 로고
    • Molecular trafficking across the nuclear pore complex
    • L. Gerace (1992). Molecular trafficking across the nuclear pore complex. Curr. Opin. Cell Biol. 4, 637-645.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 637-645
    • Gerace, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.