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Volumn 166, Issue 1-3, 2011, Pages 36-41

De novo generation of short antimicrobial peptides with simple amino acid composition

Author keywords

Amphipathic helical peptide; De novo design; LKW model peptide; Tryptophan

Indexed keywords

ANTIINFECTIVE AGENT; LEUCINE; LYSINE; OMIGANAN; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPTOPHAN;

EID: 78650179473     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2010.08.010     Document Type: Article
Times cited : (59)

References (52)
  • 1
    • 69249096200 scopus 로고    scopus 로고
    • The roles of antimicrobial peptides in innate host defense
    • Diamond G., Beckloff N., Weinberg A., Kisich K.O. The roles of antimicrobial peptides in innate host defense. Curr Pharm Des 2009, 15:2377-2392.
    • (2009) Curr Pharm Des , vol.15 , pp. 2377-2392
    • Diamond, G.1    Beckloff, N.2    Weinberg, A.3    Kisich, K.O.4
  • 2
    • 33947418509 scopus 로고    scopus 로고
    • Multifunctional antimicrobial peptides: therapeutic targets in several human diseases
    • Zaiou M. Multifunctional antimicrobial peptides: therapeutic targets in several human diseases. J Mol Med 2007, 85:317-329.
    • (2007) J Mol Med , vol.85 , pp. 317-329
    • Zaiou, M.1
  • 3
    • 54449085000 scopus 로고    scopus 로고
    • Are cationic antimicrobial peptides also 'double-edged swords?
    • Ginsburg I., Koren E. Are cationic antimicrobial peptides also 'double-edged swords?. Expert Rev Anti Infect Ther 2008, 6:453-462.
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 453-462
    • Ginsburg, I.1    Koren, E.2
  • 5
    • 0043239019 scopus 로고    scopus 로고
    • Antimicrobial peptides: potential use in skin infections
    • Ulvatne H. Antimicrobial peptides: potential use in skin infections. Am J Clin Dermatol 2003, 4:591-595.
    • (2003) Am J Clin Dermatol , vol.4 , pp. 591-595
    • Ulvatne, H.1
  • 6
    • 33746842648 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment
    • Mader J.S., Hoskin D.W. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin Investig Drugs 2006, 15:933-946.
    • (2006) Expert Opin Investig Drugs , vol.15 , pp. 933-946
    • Mader, J.S.1    Hoskin, D.W.2
  • 7
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo N., Shai Y. Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci 2005, 62:784-790.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 8
    • 67649268280 scopus 로고    scopus 로고
    • Amphibian antimicrobial peptides and Protozoa: lessons from parasites
    • Rivas L., Luque-Ortega J.R., Andreu D. Amphibian antimicrobial peptides and Protozoa: lessons from parasites. Biochim Biophys Acta 2009, 1788:1570-1581.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1570-1581
    • Rivas, L.1    Luque-Ortega, J.R.2    Andreu, D.3
  • 9
    • 34548675371 scopus 로고    scopus 로고
    • Insulin releasing properties of the temporin family of antimicrobial peptides
    • Abdel-Wahab Y.H., Marenah L., Flatt P.R., Conlon J.M. Insulin releasing properties of the temporin family of antimicrobial peptides. Protein Pept Lett 2007, 14:702-707.
    • (2007) Protein Pept Lett , vol.14 , pp. 702-707
    • Abdel-Wahab, Y.H.1    Marenah, L.2    Flatt, P.R.3    Conlon, J.M.4
  • 10
    • 38649103176 scopus 로고    scopus 로고
    • Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue
    • Abdel-Wahab Y.H., Power G.J., Ng M.T., Flatt P.R., Conlon J.M. Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue. Biol Chem 2008, 389:143-148.
    • (2008) Biol Chem , vol.389 , pp. 143-148
    • Abdel-Wahab, Y.H.1    Power, G.J.2    Ng, M.T.3    Flatt, P.R.4    Conlon, J.M.5
  • 11
    • 33644757817 scopus 로고    scopus 로고
    • Natural antibiotics and insulin sensitivity: the role of bactericidal/permeability-increasing protein
    • Gubern C., López-Bermejo A., Biarnés J., Vendrell J., Ricart W., Fernández-Real J.M. Natural antibiotics and insulin sensitivity: the role of bactericidal/permeability-increasing protein. Diabetes 2006, 55:216-224.
    • (2006) Diabetes , vol.55 , pp. 216-224
    • Gubern, C.1    López-Bermejo, A.2    Biarnés, J.3    Vendrell, J.4    Ricart, W.5    Fernández-Real, J.M.6
  • 12
    • 71549152200 scopus 로고    scopus 로고
    • Gaegurin-6 stimulates insulin secretion through calcium influx in pancreatic β Rin5mf cells
    • Kim J.H., Lee J.O., Jung J.H., Lee S.K., You G.Y., Park S.J., et al. Gaegurin-6 stimulates insulin secretion through calcium influx in pancreatic β Rin5mf cells. Regul Pept 2009, 159:123-128.
    • (2009) Regul Pept , vol.159 , pp. 123-128
    • Kim, J.H.1    Lee, J.O.2    Jung, J.H.3    Lee, S.K.4    You, G.Y.5    Park, S.J.6
  • 13
    • 31544471813 scopus 로고    scopus 로고
    • Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity
    • Marenah L., Flatt P.R., Orr D.F., Shaw C., Abdel-Wahab Y.H.A. Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity. J Endocrinol 2006, 188:1-9.
    • (2006) J Endocrinol , vol.188 , pp. 1-9
    • Marenah, L.1    Flatt, P.R.2    Orr, D.F.3    Shaw, C.4    Abdel-Wahab, Y.H.A.5
  • 14
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: an overview of a promising class of therapeutics
    • Giuliani A., Pirri G., Nicoletto S.F. Antimicrobial peptides: an overview of a promising class of therapeutics. Cent Eur J Biol 2007, 2:1-33.
    • (2007) Cent Eur J Biol , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.F.3
  • 15
    • 23444437935 scopus 로고    scopus 로고
    • A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs
    • Gordon Y.J., Romanowski E.G., McDermott A.M. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs. Curr Eye Res 2005, 30:505-515.
    • (2005) Curr Eye Res , vol.30 , pp. 505-515
    • Gordon, Y.J.1    Romanowski, E.G.2    McDermott, A.M.3
  • 16
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 17
    • 69949191216 scopus 로고    scopus 로고
    • Antimicrobial and antifungal activities of novel cationic antimicrobial peptide, omigana, in experimental skin colonization models
    • Rubinchik E., Dugourd D., Algara T., Pasetka C., Friedland H.D. Antimicrobial and antifungal activities of novel cationic antimicrobial peptide, omigana, in experimental skin colonization models. Int J Antimicrob Agents 2009, 34:457-461.
    • (2009) Int J Antimicrob Agents , vol.34 , pp. 457-461
    • Rubinchik, E.1    Dugourd, D.2    Algara, T.3    Pasetka, C.4    Friedland, H.D.5
  • 19
    • 2442475526 scopus 로고    scopus 로고
    • Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5
    • Won H.S., Jung S.J., Kim H.E., Seo M.D., Lee B.J. Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5. J Biol Chem 2004, 279:14784-14791.
    • (2004) J Biol Chem , vol.279 , pp. 14784-14791
    • Won, H.S.1    Jung, S.J.2    Kim, H.E.3    Seo, M.D.4    Lee, B.J.5
  • 20
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi A., Sandri L., Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 2000, 55:4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 21
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationships studies
    • Zelezetsky I., Tossi A. Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationships studies. Biochim Biophys Acta 2006, 1758:1436-1449.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 22
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren Z., Shai Y. Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 1998, 47:451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 23
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1999, 1462:55-70.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 24
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeman M.R., Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 2003, 55:27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeman, M.R.1    Yount, N.Y.2
  • 26
    • 0036467404 scopus 로고    scopus 로고
    • General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides
    • Dathe M., Meyer J., Beyermann M., Maul B., Hoischen C., Bienert M. General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides. Biochim Biophys Acta 2002, 1558:171-186.
    • (2002) Biochim Biophys Acta , vol.1558 , pp. 171-186
    • Dathe, M.1    Meyer, J.2    Beyermann, M.3    Maul, B.4    Hoischen, C.5    Bienert, M.6
  • 27
    • 34250195381 scopus 로고    scopus 로고
    • Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity
    • Fernández-Vidal M., Jayasinghe S., Ladokhin A.S., White S.H. Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity. J Mol Biol 2007, 370:459-470.
    • (2007) J Mol Biol , vol.370 , pp. 459-470
    • Fernández-Vidal, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4
  • 28
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • Chou H.T., Kuo T.Y., Chiang J.C., Pei M.J., Yang W.T., Yu H.C., et al. Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. Int J Antimicrob Agents 2008, 32:130-138.
    • (2008) Int J Antimicrob Agents , vol.32 , pp. 130-138
    • Chou, H.T.1    Kuo, T.Y.2    Chiang, J.C.3    Pei, M.J.4    Yang, W.T.5    Yu, H.C.6
  • 29
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E.W., Vasil M.L., Hodges R.S. Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem 2005, 280:12316-12329.
    • (2005) J Biol Chem , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 30
    • 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 2001, 40:12591-12603.
    • (2001) Biochemistry , vol.40 , pp. 12591-12603
    • Avrahami, D.1    Oren, Z.2    Shai, Y.3
  • 32
    • 0038192455 scopus 로고    scopus 로고
    • The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes
    • Béven L., Castano S., Dufourcq J., Wieslander Å., Wróblewski H. The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur J Biochem 2003, 270:2207-2217.
    • (2003) Eur J Biochem , vol.270 , pp. 2207-2217
    • Béven, L.1    Castano, S.2    Dufourcq, J.3    Wieslander, Å.4    Wróblewski, H.5
  • 33
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle S.E., Houghten R.A. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 1992, 31:12688-12694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 34
    • 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., et al. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett 1997, 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
  • 35
    • 11244267508 scopus 로고    scopus 로고
    • De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity
    • Deslouches B., Phadke S.M., Lazarevic V., Cascio M., Islam K., Montelaro R.C., et al. De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. Antimicrob Agents Chemother 2005, 49:316-322.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 316-322
    • Deslouches, B.1    Phadke, S.M.2    Lazarevic, V.3    Cascio, M.4    Islam, K.5    Montelaro, R.C.6
  • 36
    • 0042572540 scopus 로고    scopus 로고
    • Influence of tryptophan on lipid binding of lenear amphipathic cationic antimicrobial peptides
    • Jin Y., Mozsolits H., Hammer J., Zmuda E., Zhu F., Zhang Y., et al. Influence of tryptophan on lipid binding of lenear amphipathic cationic antimicrobial peptides. Biochemistry 2003, 42:9395-9405.
    • (2003) Biochemistry , vol.42 , pp. 9395-9405
    • Jin, Y.1    Mozsolits, H.2    Hammer, J.3    Zmuda, E.4    Zhu, F.5    Zhang, Y.6
  • 37
    • 28844467956 scopus 로고    scopus 로고
    • Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic -sheet and -helical potentials
    • Jin Y., Hammer J., Pate M., Zhang Y., Zhu F., Zmuda E., et al. Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic -sheet and -helical potentials. Antimicrob Agents Chemother 2005, 49:4957-4964.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4957-4964
    • Jin, Y.1    Hammer, J.2    Pate, M.3    Zhang, Y.4    Zhu, F.5    Zmuda, E.6
  • 38
    • 0036038922 scopus 로고    scopus 로고
    • Structures and mode of membrane interaction of a short α helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy
    • Oren Z., Ramesh J., Avrahami D., Suryaprakash N., Shai Y., Jelinek R. Structures and mode of membrane interaction of a short α helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy. Eur J Biochem 2002, 269:3869-3880.
    • (2002) Eur J Biochem , vol.269 , pp. 3869-3880
    • Oren, Z.1    Ramesh, J.2    Avrahami, D.3    Suryaprakash, N.4    Shai, Y.5    Jelinek, R.6
  • 39
    • 3343021995 scopus 로고    scopus 로고
    • A short α-helical antimicrobial peptide with antibacterial selectivity
    • Shin S.Y., Hahm K.S. A short α-helical antimicrobial peptide with antibacterial selectivity. Biotechnol Lett 2004, 26:735-739.
    • (2004) Biotechnol Lett , vol.26 , pp. 735-739
    • Shin, S.Y.1    Hahm, K.S.2
  • 40
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, α-sheet, and random coil regions calculated from proteins
    • Chou P.Y., Fasman G.D. Conformational parameters for amino acids in helical, α-sheet, and random coil regions calculated from proteins. Biochemistry 1974, 13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 41
    • 0036049082 scopus 로고    scopus 로고
    • Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4
    • Won H.S., Park S.H., Kim H.E., Hyun B., Kim M., Lee B., et al. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. Eur J Biochem 2002, 269:4367-4374.
    • (2002) Eur J Biochem , vol.269 , pp. 4367-4374
    • Won, H.S.1    Park, S.H.2    Kim, H.E.3    Hyun, B.4    Kim, M.5    Lee, B.6
  • 42
    • 33746911159 scopus 로고    scopus 로고
    • Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5
    • Won H.S., Seo M.D., Jung S.J., Lee S.J., Kang S.J., Son W.S., et al. Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5. J Med Chem 2006, 49:4886-4895.
    • (2006) J Med Chem , vol.49 , pp. 4886-4895
    • Won, H.S.1    Seo, M.D.2    Jung, S.J.3    Lee, S.J.4    Kang, S.J.5    Son, W.S.6
  • 43
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel
    • Hu W., Lee K.C., Cross T.A. Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel. Biochemistry 1993, 32:7035-7047.
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.C.2    Cross, T.A.3
  • 44
    • 0034601806 scopus 로고    scopus 로고
    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-Magainin 2(1-12) and its analogues, on their antibiotic activities and structures
    • Oh D., Shin S.Y., Lee S., Kang J.H., Kim S.D., Ryu P.D., et al. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-Magainin 2(1-12) and its analogues, on their antibiotic activities and structures. Biochemistry 2000, 39:11855-11964.
    • (2000) Biochemistry , vol.39 , pp. 11855-11964
    • Oh, D.1    Shin, S.Y.2    Lee, S.3    Kang, J.H.4    Kim, S.D.5    Ryu, P.D.6
  • 45
    • 0036295702 scopus 로고    scopus 로고
    • Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy
    • Park K., Oh D., Shin S.Y., Hahm K.S., Kim Y. Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy. Biochem Biophys Res Commun 2002, 290:204-212.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 204-212
    • Park, K.1    Oh, D.2    Shin, S.Y.3    Hahm, K.S.4    Kim, Y.5
  • 46
    • 0034732952 scopus 로고    scopus 로고
    • Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins
    • Ridder A.N., Morein S., Stam J.G., Kuhn A., de Kruijff B., Killian J.A. Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins. Biochemistry 2000, 39:6521-6528.
    • (2000) Biochemistry , vol.39 , pp. 6521-6528
    • Ridder, A.N.1    Morein, S.2    Stam, J.G.3    Kuhn, A.4    de Kruijff, B.5    Killian, J.A.6
  • 47
    • 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. Biochim Biophys Acta 1999, 1462:11-28.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 48
    • 33645960442 scopus 로고    scopus 로고
    • Antimicrobial peptides with unusual amino acid compositions and unusual structures
    • Sitaram N. Antimicrobial peptides with unusual amino acid compositions and unusual structures. Curr Med Chem 2006, 13:679-696.
    • (2006) Curr Med Chem , vol.13 , pp. 679-696
    • Sitaram, N.1
  • 49
    • 67649277614 scopus 로고    scopus 로고
    • Action mechanism and structural requirements of the antimicrobial peptides, gaegurins
    • Won H.S., Kang S.J., Lee B.J. Action mechanism and structural requirements of the antimicrobial peptides, gaegurins. Biochim Biophys Acta 2009, 1788:1620-1629.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1620-1629
    • Won, H.S.1    Kang, S.J.2    Lee, B.J.3
  • 50
    • 0021911383 scopus 로고
    • Occurrence of a β-lactam-inducible penicillin-binding protein in methicillin-resistant staphylococci
    • Ubukata K., Yamashita N., Konno M. Occurrence of a β-lactam-inducible penicillin-binding protein in methicillin-resistant staphylococci. Antimicrob Agents Chemother 1985, 5:851-857.
    • (1985) Antimicrob Agents Chemother , vol.5 , pp. 851-857
    • Ubukata, K.1    Yamashita, N.2    Konno, M.3
  • 51
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg D. Three-dimensional structure of membrane and surface proteins. Annu Rev Biochem 1984, 53:595-623.
    • (1984) Annu Rev Biochem , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 52
    • 36949003906 scopus 로고    scopus 로고
    • Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence
    • Zhu W.L., Nan Y.H., Hahm K.S., Shin S.Y. Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence. J Biochem Mol Biol 2007, 40:1090-1094.
    • (2007) J Biochem Mol Biol , vol.40 , pp. 1090-1094
    • Zhu, W.L.1    Nan, Y.H.2    Hahm, K.S.3    Shin, S.Y.4


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