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Volumn 48, Issue 46, 2009, Pages 10905-10917

Design of nontoxic analogues of cathelicidin-derived bovine antimicrobial peptide BMAP-27: The role of leucine as well as phenylalanine zipper sequences in determining its toxicity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANTI-BACTERIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; CATHELICIDIN; CYTOTOXIC ACTIVITIES; GRAM-NEGATIVE BACTERIA; LEUCINE ZIPPERS; MAMMALIAN CELLS; NATURALLY OCCURRING; PHENYLALANINE RESIDUES; WILD TYPES;

EID: 72749118747     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9009874     Document Type: Article
Times cited : (43)

References (53)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: Microbicidal activity, mechanisms of action, and roles in innate immunity
    • DOI 10.1016/S1286-4579(02)01549-6, PII S1286457902015496
    • Ramanathan, B., Davis, E. G., Ross, C. R., and Blecha, F. (2002) Cathelicidins: Microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect. 4, 361-372. (Pubitemid 34293642)
    • (2002) Microbes and Infection , vol.4 , Issue.3 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3    Blecha, F.4
  • 3
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer, R. I., Lichtenstein, A. K., and Ganz, T. (1993) Defensins: Antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105-128.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 4
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock, R. E. (2001) Cationic peptides: Effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1, 156-164.
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 5
    • 0033664277 scopus 로고    scopus 로고
    • Leukocyte antimicrobial peptides: Multifunctional effector molecules of innate immunity
    • Risso, A. (2000) Leukocyte antimicrobial peptides: Multifunctional effector molecules of innate immunity. J. Leukocyte Biol. 68, 785-792.
    • (2000) J. Leukocyte Biol. , vol.68 , pp. 785-792
    • Risso, A.1
  • 6
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • DOI 10.1002/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9
    • Gennaro, R., and Zanetti, M. (2000) Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55, 31-49. (Pubitemid 30680237)
    • (2000) Biopolymers - Peptide Science Section , vol.55 , Issue.1 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 7
    • 0024460671 scopus 로고
    • Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils
    • Gennaro, R., Skerlavaj, B., and Romeo, D. (1989) Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect. Immun. 57, 3142-3146.
    • (1989) Infect. Immun. , vol.57 , pp. 3142-3146
    • Gennaro, R.1    Skerlavaj, B.2    Romeo, D.3
  • 8
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins: A family of multifunctional antimicrobial peptides
    • Bals, R., and Wilson, J. M. (2003) Cathelicidins: A family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 60, 711-720.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 9
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti, M., Gennaro, R., and Romeo, D. (1995) Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374, 1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 11
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer, R. I., and Ganz, T. (2002) Cathelicidins: A family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 9, 18-22.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 12
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Durr, U. H., Sudheendra, U. S., and Ramamoorthy, A. (2006) LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta 1758, 1408-1425.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1408-1425
    • Durr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 13
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 18
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson, G. H., Agerberth, B., Odeberg, J., Bergman, T., Olsson, B., and Salcedo, R. (1996) The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238, 325-332.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 19
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm, M., Agerberth, B., Ahangari, G., Stahle-Backdahl, M., Liden, S., Wigzell, H., and Gudmundsson, G. H. (1997) The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272, 15258-15263.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 20
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., and Agerberth, B. (1998) Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273, 3718-3724.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 21
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E., and Lehrer, R. (1998) Cationic peptides: A new source of antibiotics. Trends Biotechnol. 16, 82-88.
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 22
    • 33746014692 scopus 로고    scopus 로고
    • Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity
    • Zelezetsky, I., Pontillo, A., Puzzi, L., Antcheva, N., Segat, L., Pacor, S., Crovella, S., and Tossi, A. (2006) Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. J. Biol. Chem. 281, 19861-19871.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19861-19871
    • Zelezetsky, I.1    Pontillo, A.2    Puzzi, L.3    Antcheva, N.4    Segat, L.5    Pacor, S.6    Crovella, S.7    Tossi, A.8
  • 23
    • 59849118467 scopus 로고    scopus 로고
    • Primate cathelicidin orthologues display different structures and membrane interactions
    • Morgera, F., Vaccari, L., Antcheva, N., Scaini, D., Pacor, S., and Tossi, A. (2009) Primate cathelicidin orthologues display different structures and membrane interactions. Biochem. J. 417, 727-735.
    • (2009) Biochem. J. , vol.417 , pp. 727-735
    • Morgera, F.1    Vaccari, L.2    Antcheva, N.3    Scaini, D.4    Pacor, S.5    Tossi, A.6
  • 24
    • 0031574103 scopus 로고    scopus 로고
    • The cathelicidin family of antimicrobial peptide precursors: A component of the oxygen-independent defense mechanisms of neutrophils
    • Zanetti, M., Gennaro, R., and Romeo, D. (1997) The cathelicidin family of antimicrobial peptide precursors: A component of the oxygen-independent defense mechanisms of neutrophils. Ann. N.Y. Acad. Sci. 832, 147-162.
    • (1997) Ann. N.Y. Acad. Sci. , vol.832 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 25
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj, B., Gennaro, R., Bagella, L., Merluzzi, L., Risso, A., and Zanetti, M. (1996) Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271, 28375-28381.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 26
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin: A leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • Asthana, N., Yadav, S. P., and Ghosh, J. K. (2004) Dissection of antibacterial and toxic activity of melittin: A leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J. Biol. Chem. 279, 55042-55050.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 27
    • 33746807690 scopus 로고    scopus 로고
    • Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells
    • Ahmad, A., Yadav, S. P., Asthana, N., Mitra, K., Srivastava, S. P., and Ghosh, J. K. (2006) Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells. J. Biol. Chem. 281, 22029-22038.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22029-22038
    • Ahmad, A.1    Yadav, S.P.2    Asthana, N.3    Mitra, K.4    Srivastava, S.P.5    Ghosh, J.K.6
  • 28
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B., and Noble, R. L. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35, 161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 29
    • 0347065360 scopus 로고    scopus 로고
    • Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization
    • Yadav, S. P., Kundu, B., and Ghosh, J. K. (2003) Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization. J. Biol. Chem. 278, 51023-51034.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51023-51034
    • Yadav, S.P.1    Kundu, B.2    Ghosh, J.K.3
  • 30
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • DOI 10.1021/bi962507l
    • Oren, Z., and Shai, Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study. Biochemistry 36, 1826-1835. (Pubitemid 27086279)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 31
    • 0036786839 scopus 로고    scopus 로고
    • Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells
    • Sal-Man, N., Oren, Z., and Shai, Y. (2002) Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells. Biochemistry 41, 11921-11930.
    • (2002) Biochemistry , vol.41 , pp. 11921-11930
    • Sal-Man, N.1    Oren, Z.2    Shai, Y.3
  • 33
    • 27144555794 scopus 로고    scopus 로고
    • Domain 5 of high molecular weight kininogen is antibacterial
    • Nordahl, E. A., Rydengard, V., Morgelin, M., and Schmidtchen, A. (2005) Domain 5 of high molecular weight kininogen is antibacterial. J. Biol. Chem. 280, 34832-34839.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34832-34839
    • Nordahl, E.A.1    Rydengard, V.2    Morgelin, M.3    Schmidtchen, A.4
  • 34
    • 4143110396 scopus 로고    scopus 로고
    • Suppression of human prostate tumor growth in mice by a cytolytic D-, L-amino acid peptide: Membrane lysis, increased necrosis, and inhibition of prostate-specific antigen secretion
    • DOI 10.1158/0008-5472.CAN-04-1438
    • Papo, N., Braunstein, A., Eshhar, Z., and Shai, Y. (2004) Suppression of human prostate tumor growth in mice by a cytolytic D-,L-amino Acid Peptide: Membrane lysis, increased necrosis, and inhibition of prostate-specific antigen secretion. Cancer Res. 64, 5779-5786. (Pubitemid 39095578)
    • (2004) Cancer Research , vol.64 , Issue.16 , pp. 5779-5786
    • Papo, N.1    Braunstein, A.2    Eshhar, Z.3    Shai, Y.4
  • 35
    • 39649103630 scopus 로고    scopus 로고
    • Inhibition of lytic activity of Escherichia coli toxin hemolysin e against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism
    • DOI 10.1021/bi701187e
    • Yadav, S. P., Ahmad, A., Pandey, B. K., Verma, R., and Ghosh, J. K. (2008) Inhibition of lytic activity of Escherichia coli toxin hemolysin E against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism. Biochemistry 47, 2134-2142. (Pubitemid 351287139)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 2134-2142
    • Yadav, S.P.1    Ahmad, A.2    Pandey, B.K.3    Verma, R.4    Ghosh, J.K.5
  • 36
    • 0016188814 scopus 로고
    • Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles
    • Sims, P. J., Waggoner, A. S., Wang, C. H., and Hoffman, J. F. (1974) Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Biochemistry 13, 3315-3330.
    • (1974) Biochemistry , vol.13 , pp. 3315-3330
    • Sims, P.J.1    Waggoner, A.S.2    Wang, C.H.3    Hoffman, J.F.4
  • 37
    • 0021103430 scopus 로고
    • Diffusion potential cascade. Convenient detection of transferable membrane pores
    • Loew, L. M., Rosenberg, I., Bridge, M., and Gitler, C. (1983) Diffusion potential cascade. Convenient detection of transferable membrane pores. Biochemistry 22, 837-844.
    • (1983) Biochemistry , vol.22 , pp. 837-844
    • Loew, L.M.1    Rosenberg, I.2    Bridge, M.3    Gitler, C.4
  • 38
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang, L., Rozek, A., and Hancock, R. E. (2001) Interaction of cationic antimicrobial peptides with model membranes. J. Biol. Chem. 276, 35714-35722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3
  • 39
    • 34147135478 scopus 로고    scopus 로고
    • Characterization of the structure and membrane interaction of the antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs
    • DOI 10.1529/biophysj.106.097238
    • Pan, Y. L., Cheng, J. T., Hale, J., Pan, J., Hancock, R. E., and Straus, S. K. (2007) Characterization of the structure and membrane interaction of the antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys. J. 92, 2854-2864. (Pubitemid 46557859)
    • (2007) Biophysical Journal , vol.92 , Issue.8 , pp. 2854-2864
    • Pan, Y.-L.1    Cheng, J.T.-J.2    Hale, J.3    Pan, J.4    Hancock, R.E.W.5    Straus, S.K.6
  • 40
    • 49649113211 scopus 로고    scopus 로고
    • Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides
    • Hawrani, A., Howe, R. A., Walsh, T. R., and Dempsey, C. E. (2008) Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides. J. Biol. Chem. 283, 18636-18645.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18636-18645
    • Hawrani, A.1    Howe, R.A.2    Walsh, T.R.3    Dempsey, C.E.4
  • 41
    • 0018899158 scopus 로고
    • Serum-induced leakage of liposome contents. Biochim
    • Allen, T. M., and Cleland, L. G. (1980) Serum-induced leakage of liposome contents. Biochim. Biophys. Acta 597, 418-426.
    • (1980) Biophys. Acta , vol.597 , pp. 418-426
    • Allen, T.M.1    Cleland, L.G.2
  • 42
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 43
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • Wu, C. S., Ikeda, K., and Yang, J. T. (1981) Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20, 566-570.
    • (1981) Biochemistry , vol.20 , pp. 566-570
    • Wu, C.S.1    Ikeda, K.2    Yang, J.T.3
  • 44
    • 0030745356 scopus 로고    scopus 로고
    • Self-assembly of designed antimicrobial peptides in solution and micelles
    • Javadpour, M. M., and Barkley, M. D. (1997) Self-assembly of designed antimicrobial peptides in solution and micelles. Biochemistry 36, 9540-9549.
    • (1997) Biochemistry , vol.36 , pp. 9540-9549
    • Javadpour, M.M.1    Barkley, M.D.2
  • 45
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
    • Giddings, K. S., Johnson, A. E., and Tweten, R. K. (2003) Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins. Proc. Natl. Acad. Sci. U.S.A. 100, 11315-11320.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 46
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • DOI 10.1083/jcb.200210140
    • Sekar, R. B., and Periasamy, A. (2003) Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 160, 629-633. (Pubitemid 36298259)
    • (2003) Journal of Cell Biology , vol.160 , Issue.5 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 47
    • 0344981532 scopus 로고    scopus 로고
    • FRET detection of cellular R4-integrin conformational activation
    • Chigaev, A., Buranda, T., Dwyer, D. C., Prossnitz, E. R., and Sklar, L. A. (2003) FRET detection of cellular R4-integrin conformational activation. Biophys. J. 85, 3951-3962.
    • (2003) Biophys. J. , vol.85 , pp. 3951-3962
    • Chigaev, A.1    Buranda, T.2    Dwyer, D.C.3    Prossnitz, E.R.4    Sklar, L.A.5
  • 49
    • 20444383852 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching
    • Van Munster, E. B., Kremers, G. J., Adjobo-Hermans, M. J., and Gadella, T. W., Jr. (2005) Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching. J. Microsc. 218, 253-262.
    • (2005) J. Microsc. , vol.218 , pp. 253-262
    • Van Munster, E.B.1    Kremers, G.J.2    Adjobo-Hermans, M.J.3    Gadella Jr., T.W.4
  • 51
    • 21444456146 scopus 로고    scopus 로고
    • Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37
    • Ciornei, C. D., Sigurdardottir, T., Schmidtchen, A., and Bodelsson, M. (2005) Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob. Agents Chemother. 49, 2845-2850.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2845-2850
    • Ciornei, C.D.1    Sigurdardottir, T.2    Schmidtchen, A.3    Bodelsson, M.4
  • 52
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • DOI 10.1042/0264-6021:3410501
    • Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B., and Shai, Y. (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341 (Part 3), 501-513. (Pubitemid 29389178)
    • (1999) Biochemical Journal , vol.341 , Issue.3 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 53
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli, F., Buck-Koehntop, B. A., Thennarasu, S., Ramamoorthy, A., and Veglia, G. (2006) Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry 45, 5793-5799.
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5


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