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Volumn 10, Issue 1, 2014, Pages 244-257

Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity

Author keywords

Amphipathicity; Antimicrobial peptides; Bactericidal mechanism; Hemolysis; Helix

Indexed keywords

AMINO ACIDS; ANTIMICROBIAL AGENTS; BACTERIA; BLOOD; CELLS; CYTOLOGY; FLUORESCENCE SPECTROSCOPY; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; HYDROGEN BONDS; PEPTIDES; SCANNING ELECTRON MICROSCOPY;

EID: 84888645761     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2013.08.043     Document Type: Article
Times cited : (170)

References (49)
  • 1
    • 79960936612 scopus 로고    scopus 로고
    • Multifunctional cationic host defence peptides and their clinical applications
    • A.T. Yeung, S.L. Gellatly, and R.E. Hancock Multifunctional cationic host defence peptides and their clinical applications Cell Mol Life Sci 68 2011 2161 2176
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2161-2176
    • Yeung, A.T.1    Gellatly, S.L.2    Hancock, R.E.3
  • 2
    • 84865431287 scopus 로고    scopus 로고
    • Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application
    • Y. Li, Q. Xiang, Q. Zhang, Y. Huang, and Z. Su Overview on the recent study of antimicrobial peptides: origins, functions, relative mechanisms and application Peptides 37 2012 207 215
    • (2012) Peptides , vol.37 , pp. 207-215
    • Li, Y.1    Xiang, Q.2    Zhang, Q.3    Huang, Y.4    Su, Z.5
  • 3
    • 77955846576 scopus 로고    scopus 로고
    • Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity
    • D. Takahashi, S.K. Shukla, O. Prakash, and G. Zhang Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity Biochimie 92 2010 1236 1241
    • (2010) Biochimie , vol.92 , pp. 1236-1241
    • Takahashi, D.1    Shukla, S.K.2    Prakash, O.3    Zhang, G.4
  • 4
    • 84856774559 scopus 로고    scopus 로고
    • Role of lipids in the interaction of antimicrobial peptides with membranes
    • V. Teixeira, M.J. Feio, and M. Bastos Role of lipids in the interaction of antimicrobial peptides with membranes Prog Lipid Res 51 2012 149 177
    • (2012) Prog Lipid Res , vol.51 , pp. 149-177
    • Teixeira, V.1    Feio, M.J.2    Bastos, M.3
  • 5
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides
    • H. Sato, and J.B. Feix Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides Biochim Biophys Acta 1758 2006 1245 1256
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 6
    • 80051546187 scopus 로고    scopus 로고
    • Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
    • N.K. Brogden, and K.A. Brogden Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals? Int J Antimicrob Agents 38 2011 217 225
    • (2011) Int J Antimicrob Agents , vol.38 , pp. 217-225
    • Brogden, N.K.1    Brogden, K.A.2
  • 8
    • 79952187401 scopus 로고    scopus 로고
    • Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces
    • F. Costa, I.F. Carvalho, R.C. Montelaro, P. Gomes, and M.C. Martins Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces Acta Biomater 7 2011 1431 1440
    • (2011) Acta Biomater , vol.7 , pp. 1431-1440
    • Costa, F.1    Carvalho, I.F.2    Montelaro, R.C.3    Gomes, P.4    Martins, M.C.5
  • 10
    • 84868131857 scopus 로고    scopus 로고
    • Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity
    • Y. Liu, X. Xia, L. Xu, and Y. Wang Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity Biomaterials 34 2013 237 250
    • (2013) Biomaterials , vol.34 , pp. 237-250
    • Liu, Y.1    Xia, X.2    Xu, L.3    Wang, Y.4
  • 11
    • 78651445030 scopus 로고    scopus 로고
    • Synthetic cationic amphiphilic alpha-helical peptides as antimicrobial agents
    • N. Wiradharma, U. Khoe, C.A. Hauser, S.V. Seow, S. Zhang, and Y.Y. Yang Synthetic cationic amphiphilic alpha-helical peptides as antimicrobial agents Biomaterials 32 2011 2204 2212
    • (2011) Biomaterials , vol.32 , pp. 2204-2212
    • Wiradharma, N.1    Khoe, U.2    Hauser, C.A.3    Seow, S.V.4    Zhang, S.5    Yang, Y.Y.6
  • 12
    • 84873099755 scopus 로고    scopus 로고
    • Dual modes of antitumor action of an amphiphilic peptide A9K
    • H. Xu, C.X. Chen, J. Hu, P. Zhou, P. Zeng, and C.H. Cao Dual modes of antitumor action of an amphiphilic peptide A9K Biomaterials 34 2013 2731 2737
    • (2013) Biomaterials , vol.34 , pp. 2731-2737
    • Xu, H.1    Chen, C.X.2    Hu, J.3    Zhou, P.4    Zeng, P.5    Cao, C.H.6
  • 14
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides - Using a sequence template to guide structure-activity relationship studies
    • I. Zelezetsky, and A. Tossi Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationship studies Biochim Biophys Acta 1758 2006 1436 1449
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 15
    • 84857989917 scopus 로고    scopus 로고
    • Charge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides
    • M. Mihajlovic, and T. Lazaridis Charge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides Biochim Biophys Acta 1818 2012 1274 1283
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1274-1283
    • Mihajlovic, M.1    Lazaridis, T.2
  • 16
    • 49649113211 scopus 로고    scopus 로고
    • Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides
    • A. Hawrani, R.A. Howe, T.R. Walsh, and C.E. Dempsey Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides J Biol Chem 283 2008 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
  • 17
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Y. Chen, C.T. Mant, S.W. Farmer, R.E. Hancock, M.L. Vasil, and R.S. Hodges Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index J Biol Chem 280 2005 12316 12329
    • (2005) J Biol Chem , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 18
    • 79952614254 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides to target Gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: Utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio
    • Z. Jiang, A.I. Vasil, L. Gera, M.L. Vasil, and R.S. Hodges Rational design of alpha-helical antimicrobial peptides to target Gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio Chem Biol Drug Des 77 2011 225 240
    • (2011) Chem Biol Drug des , vol.77 , pp. 225-240
    • Jiang, Z.1    Vasil, A.I.2    Gera, L.3    Vasil, M.L.4    Hodges, R.S.5
  • 19
    • 76549252207 scopus 로고
    • The structure of proteins; Two hydrogen-bonded helical configurations of the polypeptide chain
    • L. Pauling, R.B. Corey, and H.R. Branson The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain Proc Natl Acad Sci U S A 37 1951 205 211
    • (1951) Proc Natl Acad Sci U S A , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 20
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: Structure of proteins of the alpha-keratin type
    • L. Pauling, and R.B. Corey Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type Nature 171 1953 59 61
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, R.B.2
  • 21
    • 78751577565 scopus 로고    scopus 로고
    • Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities
    • B.M. de Souza, M.P. Dos Santos Cabrera, J.R. Neto, and M.S. Palma Investigating the effect of different positioning of lysine residues along the peptide chain of mastoparans for their secondary structures and biological activities Amino Acids 40 2011 77 90
    • (2011) Amino Acids , vol.40 , pp. 77-90
    • De Souza, B.M.1    Dos Santos Cabrera, M.P.2    Neto, J.R.3    Palma, M.S.4
  • 22
    • 33947091990 scopus 로고
    • A method for predicting nucleation sites for protein folding based on hydrophobic contacts
    • R.R. Matheson, and H.A. Scheraga A method for predicting nucleation sites for protein folding based on hydrophobic contacts Macromolecules 11 1978 819 829
    • (1978) Macromolecules , vol.11 , pp. 819-829
    • Matheson, R.R.1    Scheraga, H.A.2
  • 23
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • D.I. Chan, E.J. Prenner, and H.J. Vogel Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim Biophys Acta 1758 2006 1184 1202
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 24
    • 84872714452 scopus 로고    scopus 로고
    • Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units
    • Q.Q. Ma, N. Dong, A.S. Shan, Y.F. Lv, Y.Z. Li, and Z.H. Chen Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units Amino Acids 43 2012 2527 2536
    • (2012) Amino Acids , vol.43 , pp. 2527-2536
    • Ma, Q.Q.1    Dong, N.2    Shan, A.S.3    Lv, Y.F.4    Li, Y.Z.5    Chen, Z.H.6
  • 25
    • 84861123585 scopus 로고    scopus 로고
    • Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine- and valine-rich beta-hairpin-like antimicrobial peptides
    • N. Dong, Q. Ma, A. Shan, Y. Lv, W. Hu, and Y. Gu Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine- and valine-rich beta-hairpin-like antimicrobial peptides Antimicrob Agents Chemother 56 2012 2994 3003
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2994-3003
    • Dong, N.1    Ma, Q.2    Shan, A.3    Lv, Y.4    Hu, W.5    Gu, Y.6
  • 26
    • 37249076371 scopus 로고    scopus 로고
    • Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3
    • G. Maisetta, M. Di Luca, S. Esin, W. Florio, F.L. Brancatisano, and D. Bottai Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3 Peptides 29 2008 1 6
    • (2008) Peptides , vol.29 , pp. 1-6
    • Maisetta, G.1    Di Luca, M.2    Esin, S.3    Florio, W.4    Brancatisano, F.L.5    Bottai, D.6
  • 27
    • 84855690465 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • C. Louis-Jeune, M.A. Andrade-Navarro, and C. Perez-Iratxeta Prediction of protein secondary structure from circular dichroism using theoretically derived spectra Proteins 80 2011 374 381
    • (2011) Proteins , vol.80 , pp. 374-381
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3
  • 28
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • H.W. Huang Molecular mechanism of antimicrobial peptides: the origin of cooperativity Biochim Biophys Acta 1758 2006 1292 1302
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 29
    • 79955164524 scopus 로고    scopus 로고
    • Natural roles of antimicrobial peptides in microbes, plants and animals
    • G. Maroti, A. Kereszt, E. Kondorosi, and P. Mergaert Natural roles of antimicrobial peptides in microbes, plants and animals Res Microbiol 162 2011 363 374
    • (2011) Res Microbiol , vol.162 , pp. 363-374
    • Maroti, G.1    Kereszt, A.2    Kondorosi, E.3    Mergaert, P.4
  • 30
    • 42749096667 scopus 로고    scopus 로고
    • On the mechanisms of biocompatibility
    • D.F. Williams On the mechanisms of biocompatibility Biomaterials 29 2008 2941 2953
    • (2008) Biomaterials , vol.29 , pp. 2941-2953
    • Williams, D.F.1
  • 31
    • 77953959738 scopus 로고    scopus 로고
    • Antibiotic-loaded biomaterials and the risks for the spread of antibiotic resistance following their prophylactic and therapeutic clinical use
    • D. Campoccia, L. Montanaro, P. Speziale, and C.R. Arciola Antibiotic-loaded biomaterials and the risks for the spread of antibiotic resistance following their prophylactic and therapeutic clinical use Biomaterials 31 2010 6363 6377
    • (2010) Biomaterials , vol.31 , pp. 6363-6377
    • Campoccia, D.1    Montanaro, L.2    Speziale, P.3    Arciola, C.R.4
  • 32
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • K. Matsuzaki Control of cell selectivity of antimicrobial peptides Biochim Biophys Acta 1788 2009 1687 1692
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1
  • 33
    • 77955279662 scopus 로고    scopus 로고
    • Novel short antibacterial and antifungal peptides with low cytotoxicity: Efficacy and action mechanisms
    • X. Qi, C. Zhou, P. Li, W. Xu, Y. Cao, and H. Ling Novel short antibacterial and antifungal peptides with low cytotoxicity: efficacy and action mechanisms Biochem Biophys Res Commun 398 2010 594 600
    • (2010) Biochem Biophys Res Commun , vol.398 , pp. 594-600
    • Qi, X.1    Zhou, C.2    Li, P.3    Xu, W.4    Cao, Y.5    Ling, H.6
  • 35
    • 84871909572 scopus 로고    scopus 로고
    • Rationally designed alpha-helical broad-spectrum antimicrobial peptides with idealized facial amphiphilicity
    • N. Wiradharma, M.Y. Sng, M. Khan, Z.Y. Ong, and Y.Y. Yang Rationally designed alpha-helical broad-spectrum antimicrobial peptides with idealized facial amphiphilicity Macromol Rapid Commun 34 2013 74 80
    • (2013) Macromol Rapid Commun , vol.34 , pp. 74-80
    • Wiradharma, N.1    Sng, M.Y.2    Khan, M.3    Ong, Z.Y.4    Yang, Y.Y.5
  • 36
    • 0028009472 scopus 로고
    • Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA
    • P. Storici, M. Scocchi, A. Tossi, R. Gennaro, and M. Zanetti Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA FEBS Lett 337 1994 303 307
    • (1994) FEBS Lett , vol.337 , pp. 303-307
    • Storici, P.1    Scocchi, M.2    Tossi, A.3    Gennaro, R.4    Zanetti, M.5
  • 37
    • 24644436041 scopus 로고    scopus 로고
    • Structural aspects and biological properties of the cathelicidin PMAP-36
    • M. Scocchi, I. Zelezetsky, M. Benincasa, R. Gennaro, A. Mazzoli, and A. Tossi Structural aspects and biological properties of the cathelicidin PMAP-36 FEBS J 272 2005 4398 4406
    • (2005) FEBS J , vol.272 , pp. 4398-4406
    • Scocchi, M.1    Zelezetsky, I.2    Benincasa, M.3    Gennaro, R.4    Mazzoli, A.5    Tossi, A.6
  • 38
    • 84870234194 scopus 로고    scopus 로고
    • Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action
    • J.K. Lee, S.C. Park, K.S. Hahm, and Y. Park Antimicrobial HPA3NT3 peptide analogs: placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action Biochim Biophys Acta 1828 2013 443 454
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 443-454
    • Lee, J.K.1    Park, S.C.2    Hahm, K.S.3    Park, Y.4
  • 39
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • M. Dathe, H. Nikolenko, J. Meyer, M. Beyermann, and M. Bienert Optimization of the antimicrobial activity of magainin peptides by modification of charge FEBS Lett 501 2001 146 150
    • (2001) FEBS Lett , vol.501 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 41
    • 0029745052 scopus 로고    scopus 로고
    • Cation-pi interactions in aromatics of biological and medicinal interest: Electrostatic potential surfaces as a useful qualitative guide
    • S. Mecozzi, A.P. West, and D.A. Dougherty Cation-pi interactions in aromatics of biological and medicinal interest: electrostatic potential surfaces as a useful qualitative guide Proc Natl Acad Sci U S A 93 1996 10566 10571
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10566-10571
    • Mecozzi, S.1    West, A.P.2    Dougherty, D.A.3
  • 42
    • 84871970730 scopus 로고    scopus 로고
    • Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
    • I.M. Torcato, Y.H. Huang, H.G. Franquelim, D. Gaspar, D.J. Craik, and M.A. Castanho Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria Biochim Biophys Acta 1828 2013 944 955
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 944-955
    • Torcato, I.M.1    Huang, Y.H.2    Franquelim, H.G.3    Gaspar, D.4    Craik, D.J.5    Castanho, M.A.6
  • 43
    • 77951212665 scopus 로고    scopus 로고
    • Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis
    • M.U. Hammer, A. Brauser, C. Olak, G. Brezesinski, T. Goldmann, and T. Gutsmann Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis Biochem J 427 2010 477 488
    • (2010) Biochem J , vol.427 , pp. 477-488
    • Hammer, M.U.1    Brauser, A.2    Olak, C.3    Brezesinski, G.4    Goldmann, T.5    Gutsmann, T.6
  • 44
    • 84866951984 scopus 로고    scopus 로고
    • D-Alanylation of lipoteichoic acids confers resistance to cationic peptides in group B streptococcus by increasing the cell wall density
    • R. Saar-Dover, A. Bitler, R. Nezer, L. Shmuel-Galia, A. Firon, and E. Shimoni d-Alanylation of lipoteichoic acids confers resistance to cationic peptides in group B streptococcus by increasing the cell wall density PLoS Pathog 8 2012 e1002891
    • (2012) PLoS Pathog , vol.8 , pp. 1002891
    • Saar-Dover, R.1    Bitler, A.2    Nezer, R.3    Shmuel-Galia, L.4    Firon, A.5    Shimoni, E.6
  • 45
    • 79960292952 scopus 로고    scopus 로고
    • Inhibitory effects and mechanisms of physiological conditions on the activity of enantiomeric forms of an alpha-helical antibacterial peptide against bacteria
    • J. Huang, D. Hao, Y. Chen, Y. Xu, J. Tan, and Y. Huang Inhibitory effects and mechanisms of physiological conditions on the activity of enantiomeric forms of an alpha-helical antibacterial peptide against bacteria Peptides 32 2011 1488 1495
    • (2011) Peptides , vol.32 , pp. 1488-1495
    • Huang, J.1    Hao, D.2    Chen, Y.3    Xu, Y.4    Tan, J.5    Huang, Y.6
  • 47
    • 3142779216 scopus 로고    scopus 로고
    • Solution structure of spheniscin, a beta-defensin from the penguin stomach
    • C. Landon, C. Thouzeau, H. Labbe, P. Bulet, and F. Vovelle Solution structure of spheniscin, a beta-defensin from the penguin stomach J Biol Chem 279 2004 30433 30439
    • (2004) J Biol Chem , vol.279 , pp. 30433-30439
    • Landon, C.1    Thouzeau, C.2    Labbe, H.3    Bulet, P.4    Vovelle, F.5
  • 48
    • 84875278407 scopus 로고    scopus 로고
    • Divalent cations modulate membrane binding and pore formation of a potent antibiotic peptide analog of alamethicin
    • M. Aquila, M. Benedusi, K.W. Koch, D. Dell'Orco, and G. Rispoli Divalent cations modulate membrane binding and pore formation of a potent antibiotic peptide analog of alamethicin Cell Calcium 53 2013 180 186
    • (2013) Cell Calcium , vol.53 , pp. 180-186
    • Aquila, M.1    Benedusi, M.2    Koch, K.W.3    Dell'Orco, D.4    Rispoli, G.5
  • 49
    • 34250654522 scopus 로고    scopus 로고
    • Effects of cations on antimicrobial activity of ostricacins-1 and 2 on E coli O157:H7 and S aureus 1056MRSA
    • H. Sugiarto, and P.L. Yu Effects of cations on antimicrobial activity of ostricacins-1 and 2 on E. coli O157:H7 and S. aureus 1056MRSA Curr Microbiol 55 2007 36 41
    • (2007) Curr Microbiol , vol.55 , pp. 36-41
    • Sugiarto, H.1    Yu, P.L.2


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