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Volumn 1808, Issue 6, 2011, Pages 1592-1600

Investigating the effects of L- to D-amino acid substitution and deamidation on the activity and membrane interactions of antimicrobial peptide anoplin

Author keywords

Antimicrobial peptide; Atomic force microscopy; Model cell membrane; Monolayer; Phospholipid; X ray photoemission electron microscopy

Indexed keywords

ANOPLIN; ANOPLIN HYDROXIDE; ANOPLINAMIDE; ASPARTIC ACID ANOPLINAMIDE; DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 79954767139     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.11.010     Document Type: Article
Times cited : (32)

References (46)
  • 1
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • R.E.W. Hancock, and H.-G. Sahl Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotech. 24 2006 1551 1557 (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 77950499848 scopus 로고    scopus 로고
    • Potential therapeutic application of host defense peptides
    • L. Zhang, and T.J. Falla Potential therapeutic application of host defense peptides Meth. Mol. Biol. 618 2010 303 327
    • (2010) Meth. Mol. Biol. , vol.618 , pp. 303-327
    • Zhang, L.1    Falla, T.J.2
  • 6
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and disease
    • E. Guani-Guerra, T. Santos-Mendoza, S.O. Lugo-Reyes, and L.M. Teran Antimicrobial peptides: general overview and clinical implications in human health and disease Clin. Immunol. 135 2010 1 11
    • (2010) Clin. Immunol. , vol.135 , pp. 1-11
    • Guani-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Teran, L.M.4
  • 7
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • K.J. Hallock, D.K. Lee, and A. Ramamoorthy MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain Biophys. J. 84 2003 3052 3060 (Pubitemid 36531755)
    • (2003) Biophysical Journal , vol.84 , Issue.5 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 8
    • 33646474970 scopus 로고    scopus 로고
    • Structure of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • F. Porcelli, B.A. Buck-Koehntop, S. Thennarasu, A. Ramamoorthy, and G. Veglia Structure 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 2006 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
  • 9
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan - A highly potent antimicrobial peptide designed from magainin
    • L.M. Gottler, and A. Ramamoorthy Structure, membrane orientation, mechanism, and function of pexiganan - a highly potent antimicrobial peptide designed from magainin Biochim. Biophys. Acta 1788 2009 1680 1686
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 10
    • 67649295450 scopus 로고    scopus 로고
    • Antimicrobial peptide mimics for improved therapeutic properties
    • S. Rotem, and A. Mor Antimicrobial peptide mimics for improved therapeutic properties Biochim. Biophys. Acta 1788 2009 1582 1592
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1582-1592
    • Rotem, S.1    Mor, A.2
  • 11
    • 0344418718 scopus 로고    scopus 로고
    • Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide
    • DOI 10.1016/S0006-2952(99)00259-2, PII S0006295299002592
    • S.Y. Hong, J.E. Oh, and K.-H. Lee Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide - a comparison of peptide reactivity in different biological media Biochem. Pharm. 58 1999 1775 1780 (Pubitemid 29505418)
    • (1999) Biochemical Pharmacology , vol.58 , Issue.11 , pp. 1775-1780
    • Hong, S.Y.1    Oh, J.E.2    Lee, K.-H.3
  • 12
    • 75749122220 scopus 로고    scopus 로고
    • Effect of the hydrophobicity to net positive charge ratio on antibacterial and anti-endotoxin activities of structurally similar antimicrobial peptides
    • Y. Rosenfeld, N. Lev, and Y. Shai Effect of the hydrophobicity to net positive charge ratio on antibacterial and anti-endotoxin activities of structurally similar antimicrobial peptides Biochemistry 49 2010 853 861
    • (2010) Biochemistry , vol.49 , pp. 853-861
    • Rosenfeld, Y.1    Lev, N.2    Shai, Y.3
  • 13
    • 0036257510 scopus 로고    scopus 로고
    • From innate immunity to de-Novo designed antimicrobial peptides
    • DOI 10.2174/1381612023395367
    • Y. Shai From innate immunity to de-novo designed antimicrobial peptides Curr. Pharm. Des. 8 2002 715 725 (Pubitemid 34498561)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.9 , pp. 715-725
    • Shai, Y.1
  • 14
    • 2542523985 scopus 로고    scopus 로고
    • Effect of drastic sequence alteration and D-amino acid incorporation on the membrane binding behavior of lytic peptides
    • DOI 10.1021/bi049944h
    • N. Papo, and Y. Shai Effect of drastic sequence alteration and D-amino acid incorporation on the membrane binding behavior of lytic peptides Biochemistry 43 2004 6393 6403 (Pubitemid 38697539)
    • (2004) Biochemistry , vol.43 , Issue.21 , pp. 6393-6403
    • Papo, N.1    Shai, Y.2
  • 15
  • 16
    • 77049098530 scopus 로고    scopus 로고
    • Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37
    • S. Thennarasu, A. Tan, R. Penumatchu, C.E. Shelburne, D.L. Heyl, and A. Ramamoorthy Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37 Biophys. J. 98 2010 248 257
    • (2010) Biophys. J. , vol.98 , pp. 248-257
    • Thennarasu, S.1    Tan, A.2    Penumatchu, R.3    Shelburne, C.E.4    Heyl, D.L.5    Ramamoorthy, A.6
  • 17
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • J.H. Kang, M.K. Lee, K.L. Kim, and K.-S. Hahm Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin Int. J. Pept. Protein Res. 48 1996 357 363 (Pubitemid 26366822)
    • (1996) International Journal of Peptide and Protein Research , vol.48 , Issue.4 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 19
    • 14044266301 scopus 로고    scopus 로고
    • Structure-activity relationship study of anoplin
    • DOI 10.1002/psc.598
    • D. Ifrah, X. Doisy, T.S. Ryge, and P.R. Hansen Structure-activity relationship study of anoplin J. Pept. Sci. 11 2005 113 121 (Pubitemid 40277957)
    • (2005) Journal of Peptide Science , vol.11 , Issue.2 , pp. 113-121
    • Ifrah, D.1    Doisy, X.2    Ryge, T.S.3    Hansen, P.R.4
  • 20
    • 47249140913 scopus 로고    scopus 로고
    • Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus
    • DOI 10.1002/psc.960
    • M.P.D.S. Cabrera, M. Arcisio-Miranda, S.T.B. Costa, K. Konno, J.R. Ruggiero, J. Procopio, and J.R. Neto Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus J. Pept. Sci. 14 2008 661 669 (Pubitemid 351982710)
    • (2008) Journal of Peptide Science , vol.14 , Issue.6 , pp. 661-669
    • Cabrera, M.P.D.S.1    Arcisio-Miranda, M.2    Costa, S.T.B.3    Konno, K.4    Ruggiero, J.R.5    Procopio, J.6    Neto, J.R.7
  • 22
    • 34948877554 scopus 로고    scopus 로고
    • Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins)
    • DOI 10.1016/j.bbamem.2007.05.023, PII S0005273607002003
    • R.F. Epand, P.B. Savage, and R.M. Epand Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins) Biochim. Biophys. Acta 1768 2007 2500 2509 (Pubitemid 47532031)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.10 , pp. 2500-2509
    • Epand, R.F.1    Savage, P.B.2    Epand, R.M.3
  • 23
    • 34447301765 scopus 로고    scopus 로고
    • 1-functionalized liposomes in a microtiter plate assay for cholera toxin in Vibrio cholerae culture samples
    • DOI 10.1016/j.ab.2007.04.019, PII S0003269707002527
    • K.A. Edwards, and J.C. March GM1-functionalized liposomes in a microtiter plate assay for cholera toxin in Vibrio cholerae culture samples Anal. Biochem. 368 2007 39 48 (Pubitemid 47058426)
    • (2007) Analytical Biochemistry , vol.368 , Issue.1 , pp. 39-48
    • Edwards, K.A.1    March, J.C.2
  • 24
  • 25
    • 0037198841 scopus 로고    scopus 로고
    • Quantitative mapping of structured polymeric systems using singular value decomposition analysis of soft X-ray images
    • DOI 10.1021/jp013281l
    • I.N. Koprinarov, A.P. Hitchcock, C.T. McCrory, and R.F. Childs Quantitative mapping of structured polymeric systems using singular value decomposition analysis of soft X-ray images J. Phys. Chem. B 106 2002 5358 5364 (Pubitemid 35281896)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.21 , pp. 5358-5364
    • Koprinarov, I.N.1    Hitchcock, A.P.2    McCrory, C.T.3    Childs, R.F.4
  • 26
    • 79954827687 scopus 로고    scopus 로고
    • aXis2000 is free for non-commercial use. It is written in Interactive Data Language (IDL) and is available from
    • aXis2000 is free for non-commercial use. It is written in Interactive Data Language (IDL) and is available from http://unicorn.mcmaster.ca/aXis200.
  • 28
    • 0000678030 scopus 로고
    • Domain structures of phospholipid monolayer Langmuir-Blodgett films determined by atomic force microscopy
    • X.-M. Yang, D. Xiao, Z.-H. Lu, and Yu. Wei Domain structures of phospholipid monolayer Langmuir-Blodgett films determined by atomic force microscopy Appl. Surf. Sci. 90 1995 175 183
    • (1995) Appl. Surf. Sci. , vol.90 , pp. 175-183
    • Yang, X.-M.1    Xiao, D.2    Lu, Z.-H.3    Wei, Yu.4
  • 29
    • 70349495710 scopus 로고    scopus 로고
    • Interactions of antimicrobial peptide from C-terminus of myotoxin II with phospholipid mono- and bilayers
    • A. Won, and A. Ianoul Interactions of antimicrobial peptide from C-terminus of myotoxin II with phospholipid mono- and bilayers Biochim. Biophys. Acta 1788 2009 2277 2283
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2277-2283
    • Won, A.1    Ianoul, A.2
  • 31
    • 79952087255 scopus 로고    scopus 로고
    • The effects of L- to D-isomerization and C-terminus deamidation on the secondary structure of antimicrobial peptide Anoplin in aqueous and membrane mimicking environment
    • S. Pripotnev, A. Won, and A. Ianoul The effects of L- to D-isomerization and C-terminus deamidation on the secondary structure of antimicrobial peptide Anoplin in aqueous and membrane mimicking environment Raman Spectrosc 41 2010 1645 1649
    • (2010) Raman Spectrosc , vol.41 , pp. 1645-1649
    • Pripotnev, S.1    Won, A.2    Ianoul, A.3
  • 34
    • 40149084042 scopus 로고    scopus 로고
    • Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles
    • DOI 10.1021/bi702205r
    • L.E. Yandek, A. Pokorny, and P.F.F. Almeida Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles Biochemistry 47 2008 3051 3060 (Pubitemid 351328858)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 3051-3060
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.F.3
  • 36
    • 34248147074 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide dicynthaurin with membrane phospholipids at the air-liquid interface
    • DOI 10.1021/jp0672398
    • M. Majerowicz, A.J. Waring, S. Wen, and F. Bringezu Interaction of the antimicrobial peptide dicynthaurin with membrane phospholipids at the air-liquid interface J. Phys. Chem. B 111 2007 3813 3821 (Pubitemid 46724011)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.14 , pp. 3813-3821
    • Majerowicz, M.1    Waring, A.J.2    Wen, S.3    Bringezu, F.4
  • 37
    • 33746695401 scopus 로고    scopus 로고
    • Investigations into the ability of an oblique α-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide
    • DOI 10.1111/j.1742-4658.2006.05387.x
    • S.R. Dennison, L.H.G. Morton, K. Brandenburg, F. Harris, and D.A. Phoenix Investigations into the ability of an oblique alpha-helical template to provide the basis for design of an antimicrobial amphiphilic peptide FEBS J. 273 2006 3792 3803 (Pubitemid 44166658)
    • (2006) FEBS Journal , vol.273 , Issue.16 , pp. 3792-3803
    • Dennison, S.R.1    Morton, L.H.G.2    Brandenburg, K.3    Harris, F.4    Phoenix, D.A.5
  • 38
    • 0141508844 scopus 로고    scopus 로고
    • Nanoscale stripe patterns in phospholipid bilayers formed by the Langmuir-Blodgett technique
    • P. Moraille, and A. Badia Nanoscale stripe patterns in phospholipid bilayers formed by the Langmuir-Blodgett technique Langmuir 19 2003 8041 8049
    • (2003) Langmuir , vol.19 , pp. 8041-8049
    • Moraille, P.1    Badia, A.2
  • 39
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • N. Manuel, M.N. Melo, R. Ferre, and M.A.R.B. Castanho Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations Nat. Rev. Microbiol. 7 2009 245 250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Manuel, N.1    Melo, M.N.2    Ferre, R.3    Castanho, M.A.R.B.4
  • 42
    • 27444443817 scopus 로고    scopus 로고
    • Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins
    • DOI 10.1016/j.bbamem.2005.09.009, PII S0005273605002841
    • M. Magzoub, K. Oglecka, A. Pramanik, L.E.G. Eriksson, and A. Graslund Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins Biochim. Biophys. Acta 1716 2005 126 136 (Pubitemid 41532290)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1716 , Issue.2 , pp. 126-136
    • Magzoub, M.1    Oglecka, K.2    Pramanik, A.3    Eriksson, L.E.G.4    Graslund, A.5
  • 43
    • 70349523247 scopus 로고    scopus 로고
    • Cardiolipin membrane domains in prokaryotes and eukaryotes
    • E. Mileykovskaya, and W. Dowhan Cardiolipin membrane domains in prokaryotes and eukaryotes Biochim. Biophys. Acta 1788 2009 2084 2091
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2084-2091
    • Mileykovskaya, E.1    Dowhan, W.2
  • 44
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • DOI 10.1074/jbc.272.39.24224
    • K. Hristova, M. Selsted, and S.H. White Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins J. Biol. Chem. 272 1997 24224 24233 (Pubitemid 27418623)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.39 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 45
    • 68949173708 scopus 로고    scopus 로고
    • Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: Effect on membrane permeability and nanoscale lipid membrane organization
    • O. Domenech, G. Francius, P.M. Tulkens, F. van Bambeke, Y. Dufrene, and M.P. Mingeot-Leclercq Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: effect on membrane permeability and nanoscale lipid membrane organization Biochim. Biophys. Acta 1788 2009 1832 1840
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1832-1840
    • Domenech, O.1    Francius, G.2    Tulkens, P.M.3    Van Bambeke, F.4    Dufrene, Y.5    Mingeot-Leclercq, M.P.6
  • 46
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as predictors of antimicrobial potency
    • R.M. Epand, S. Rotem, A. Mor, B. Berno, and R.F. Epand Bacterial membranes as predictors of antimicrobial potency J. Am. Chem. Soc. 130 2008 14346 14352
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14346-14352
    • Epand, R.M.1    Rotem, S.2    Mor, A.3    Berno, B.4    Epand, R.F.5


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