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Volumn 1615, Issue 1-2, 2003, Pages 84-92

The role of the abundant phenylalanines in the mode of action of the antimicrobial peptide clavanin

Author keywords

Antibiotic; Biomembrane; Mechanism; Model membrane; Peptide; Phenylalanine

Indexed keywords

AMINO ACID; ANTIINFECTIVE AGENT; CLAVANIN A; ISOLEUCINE; LEUCINE; MEMBRANE LIPID; PHENYLALANINE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 0042510131     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(03)00233-5     Document Type: Article
Times cited : (50)

References (43)
  • 1
    • 0037129944 scopus 로고    scopus 로고
    • Clavanin permeabilizes target membranes via two distinctly different pH dependent mechanisms
    • Van Kan E.J.M., Demel R.A., Breukink E., Van der Bent A., De Kruijff B. Clavanin permeabilizes target membranes via two distinctly different pH dependent mechanisms. Biochemistry. 41:2002;7529-7539.
    • (2002) Biochemistry , vol.41 , pp. 7529-7539
    • Van Kan, E.J.M.1    Demel, R.A.2    Breukink, E.3    Van Der Bent, A.4    De Kruijff, B.5
  • 2
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: An update review
    • Boman H.G. Gene-encoded peptide antibiotics and the concept of innate immunity: an update review. Scandinavian Journal of Immunology. 48:1998;15-25.
    • (1998) Scandinavian Journal of Immunology , vol.48 , pp. 15-25
    • Boman, H.G.1
  • 3
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: Their function, structure, biogenesis, and mechanism of action
    • Nissen-Meyer J., Nes I.F. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Archives of Microbiology. 167:1997;67-77.
    • (1997) Archives of Microbiology , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, I.F.2
  • 4
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrates antibiotics - Defensins, protegrins, and other cysteine-rich antimicrobial peptides
    • Lehrer R.I., Ganz T. Endogenous vertebrates antibiotics - defensins, protegrins, and other cysteine-rich antimicrobial peptides. Annals of the New York Academy of Sciences. 797:1996;228-239.
    • (1996) Annals of the New York Academy of Sciences , vol.797 , pp. 228-239
    • Lehrer, R.I.1    Ganz, T.2
  • 5
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • Gudmundsson G.H., Agerberth B. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. Journal of Immunological Methods. 232:1999;45-54.
    • (1999) Journal of Immunological Methods , vol.232 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 6
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman H.G. Antibacterial peptides: key components needed in immunity. Cell. 65:1991;205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 7
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochimica et Biophysica Acta. 1462:1999;11-28.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 8
    • 0032738473 scopus 로고    scopus 로고
    • Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: Determination and biological specificity
    • Blondelle S.E., Lohner K., Aguilar M.-I. Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity. Biochimica et Biophysica Acta. 1462:1999;89-108.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 89-108
    • Blondelle, S.E.1    Lohner, K.2    Aguilar, M.-I.3
  • 9
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe M., Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochimica et Biophysica Acta. 1462:1999;71-87.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 10
    • 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
    • Dathe M., Schümann M., Wieprecht T., Winkler A., Beyermann M., Krause E., Matsuzaki K., Murase O., Bienert M. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry. 35:1996;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
  • 11
    • 0033592990 scopus 로고    scopus 로고
    • Structure and organization of hemolytic and nonhemolytic diastereomers of antimicrobial peptides in membranes
    • Hong J., Oren Z., Shai Y. Structure and organization of hemolytic and nonhemolytic diastereomers of antimicrobial peptides in membranes. Biochemistry. 38:1999;16963-16973.
    • (1999) Biochemistry , vol.38 , pp. 16963-16973
    • Hong, J.1    Oren, Z.2    Shai, Y.3
  • 13
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi A., Sandri L., Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers. 55:2000;4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 15
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochimica et Biophysica Acta. 1462:1999;1-10.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 16
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two state model
    • Huang H.W. Action of antimicrobial peptides: two state model. Biochemistry. 39:2000;8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 17
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P., Mor A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annual Review of Microbiology. 49:1995;277-304.
    • (1995) Annual Review of Microbiology , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 18
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic a-helical antimicrobial peptides
    • Oren Z., Shai Y. Mode of action of linear amphipathic a-helical antimicrobial peptides. Biopolymers. 47:1999;451-463.
    • (1999) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 19
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T., Dathe M., Epand R.M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., Bienert M. Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry. 36:1997;12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 20
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • Sitaram N., Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochimica et Biophysica Acta. 1462:1999;29-54.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 23
    • 0030739528 scopus 로고    scopus 로고
    • CDNA cloning of clavanins: Antimicrobial peptides of tunicate hemocytes
    • Zhao C., Liaw L., Lee I.H., Lehrer R.I. cDNA cloning of clavanins: antimicrobial peptides of tunicate hemocytes. FEBS Letters. 410:1997;490-492.
    • (1997) FEBS Letters , vol.410 , pp. 490-492
    • Zhao, C.1    Liaw, L.2    Lee, I.H.3    Lehrer, R.I.4
  • 24
    • 0035967521 scopus 로고    scopus 로고
    • Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues
    • Van Kan E.J.M., Van der Bent A., Demel R.A., De Kruijff B. Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues. Biochemistry. 40:2001;6398-6405.
    • (2001) Biochemistry , vol.40 , pp. 6398-6405
    • Van Kan, E.J.M.1    Van Der Bent, A.2    Demel, R.A.3    De Kruijff, B.4
  • 25
    • 1842373858 scopus 로고    scopus 로고
    • Effects of pH and salinity on the antimicrobial properties of clavanins
    • Lee I.H., Cho Y., Lehrer R.I. Effects of pH and salinity on the antimicrobial properties of clavanins. Infection and Immunity. 65:1997;2898-2903.
    • (1997) Infection and Immunity , vol.65 , pp. 2898-2903
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 26
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Structural Biology. 3:1996;842-848.
    • (1996) Nature Structural Biology , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 27
    • 84970071098 scopus 로고
    • Self-quenching of carboxyfluorescein: Fluorescence: Uses in studying liposome stability and liposome-cell interaction
    • G. Gregoriadis. Boca Raton, FL: CRC Press
    • Weinstein J.N., Ralston E., Leserman L.D., Klausner R.D., Dragsten P., Henkart P., Blumenthal R. Self-quenching of carboxyfluorescein: fluorescence: uses in studying liposome stability and liposome-cell interaction. Gregoriadis G. Liposome Technology. 1984;183-204 CRC Press, Boca Raton, FL.
    • (1984) Liposome Technology , pp. 183-204
    • Weinstein, J.N.1    Ralston, E.2    Leserman, L.D.3    Klausner, R.D.4    Dragsten, P.5    Henkart, P.6    Blumenthal, R.7
  • 28
    • 0016188814 scopus 로고
    • Mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles
    • Sims P.J., Waggoner A.S., Wang C.H., Hoffmann J.R. Mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Biochemistry. 13:1974;3315-3330.
    • (1974) Biochemistry , vol.13 , pp. 3315-3330
    • Sims, P.J.1    Waggoner, A.S.2    Wang, C.H.3    Hoffmann, J.R.4
  • 29
    • 0028694425 scopus 로고
    • Monomolecular layers in the study of biomembranes
    • H.J. Hilderson, & G.B. Ralston. New York: Plenum press
    • Demel R.A. Monomolecular layers in the study of biomembranes. Hilderson H.J., Ralston G.B. Subcellular Biochemistry. 1994;83-120 Plenum press, New York.
    • (1994) Subcellular Biochemistry , pp. 83-120
    • Demel, R.A.1
  • 30
    • 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., Cullis P.R. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochimica et Biophysica Acta. 812:1985;55-62.
    • (1985) Biochimica et Biophysica Acta , vol.812 , pp. 55-62
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 31
    • 0014779155 scopus 로고
    • Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser G., Fleischer S., Yamamoto A. Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids. 5:1970;494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 32
    • 0015522150 scopus 로고
    • Determination of the secondary structure from circular dichroism
    • Chen Y.H., Yang J.T., Martinez H.M. Determination of the secondary structure from circular dichroism. Biochemistry. 11:1972;4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 33
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Curtis Johnson W. Protein secondary structure and circular dichroism: a practical guide. Proteins: Structure, Function, and Genetics. 7:1990;205-214.
    • (1990) Proteins: Structure, Function, and Genetics , vol.7 , pp. 205-214
    • Curtis Johnson, W.1
  • 34
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton J.T., McLean L.R. Spectroscopic methods for analysis of protein secondary structure. Analytical Biochemistry. 277:2000;167-176.
    • (2000) Analytical Biochemistry , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 35
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T., Dathe M., Beyermann M., Krause E., Lee Maloy W., MacDonald D.L., Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry. 36:1997;6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Lee Maloy, W.5    MacDonald, D.L.6    Bienert, M.7
  • 36
    • 0029665072 scopus 로고    scopus 로고
    • Diastereomers of cytolysins, a novel class of potent antibacterial peptides
    • Shai Y., Oren Z. Diastereomers of cytolysins, a novel class of potent antibacterial peptides. The Journal of Biological Chemistry. 271:1996;7305-7308.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 7305-7308
    • Shai, Y.1    Oren, Z.2
  • 37
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • Dathe M., Nikolenko H., Meyer J., Beyermann M., Bienert M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Letters. 501:2001;146-150.
    • (2001) FEBS Letters , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 38
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • Dathe M., Wieprecht T., Nikolenko H., Handel L., Maloy W.L., MacDonald D.L., Beyermann M., Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Letters. 403:1997;208-212.
    • (1997) FEBS Letters , 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
  • 40
    • 0035940519 scopus 로고    scopus 로고
    • Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides
    • Avrahami D., Oren Z., Shai Y. Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry. 40:2001;12591-12603.
    • (2001) Biochemistry , vol.40 , pp. 12591-12603
    • Avrahami, D.1    Oren, Z.2    Shai, Y.3
  • 41
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown R.E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. Journal of Cell Science. 111:1998;1-9.
    • (1998) Journal of Cell Science , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 42
    • 0028033733 scopus 로고
    • Transport studies of doxorubicin in model membranes indicate a difference in passive diffusion across and binding at the outer and inner leaflets of the plasma membrane
    • Speelmans G., Staffhorst R.W.H.M., De Kruijff B., De Wolf F.A. Transport studies of doxorubicin in model membranes indicate a difference in passive diffusion across and binding at the outer and inner leaflets of the plasma membrane. Biochemistry. 33:1994;13761-13768.
    • (1994) Biochemistry , vol.33 , pp. 13761-13768
    • Speelmans, G.1    Staffhorst, R.W.H.M.2    De Kruijff, B.3    De Wolf, F.A.4
  • 43
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg D., Weiss R.M., Terwilliger T.C. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Nat. Acad. Sci. USA. 81:1984;140-144.
    • (1984) Proc. Nat. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3


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