메뉴 건너뛰기




Volumn 10, Issue 1, 2015, Pages

Enhanced amphiphilic profile of a short β-stranded peptide improves its antimicrobial activity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BETA SB 056; COLISTIN; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; SB 056; UNCLASSIFIED DRUG; HEMOLYTIC AGENT; PEPTIDE; SURFACTANT;

EID: 84921940501     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0116379     Document Type: Article
Times cited : (51)

References (57)
  • 2
    • 75449102744 scopus 로고    scopus 로고
    • De novo design of antimicrobial polymers, foldamers, and small molecules: From discovery to practical applications
    • Tew GN, Scott RW, Klein ML, Degrado WF (2009) De novo design of antimicrobial polymers, foldamers, and small molecules: from discovery to practical applications. Accounts of Chemical Research 43: 30-39.
    • (2009) Accounts of Chemical Research , vol.43 , pp. 30-39
    • Tew, G.N.1    Scott, R.W.2    Klein, M.L.3    Degrado, W.F.4
  • 3
    • 67649295450 scopus 로고    scopus 로고
    • Antimicrobial peptide mimics for improved therapeutic properties
    • PMID: 19028449
    • Rotem S, Mor A (2009) Antimicrobial peptide mimics for improved therapeutic properties. Biochimica et Biophysica Acta 1788: 1582-1592. doi: 10.1016/j.bbamem.2008.10.020 PMID: 19028449
    • (2009) Biochimica Et Biophysica Acta , vol.1788 , pp. 1582-1592
    • Rotem, S.1    Mor, A.2
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • PMID: 11807545
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395. doi: 10.1038/415389a PMID: 11807545
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • PMID: 11814654
    • Hancock REW, Rozek A (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiology Letters 206: 143-149. doi: 10.1111/j.1574-6968.2002.tb11000.x PMID: 11814654
    • (2002) FEMS Microbiology Letters , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 6
    • 50249103779 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural templates for synthetic membrane-active compounds
    • PMID: 18661101
    • Giuliani A, Pirri G, Bozzi A, Di Giulio A, Aschi M, et al. (2008) Antimicrobial peptides: natural templates for synthetic membrane-active compounds. Cellular and Molecular Life Sciences 65: 2450-2460. doi: 10.1007/s00018-008-8188-x PMID: 18661101
    • (2008) Cellular and Molecular Life Sciences , vol.65 , pp. 2450-2460
    • Giuliani, A.1    Pirri, G.2    Bozzi, A.3    Di Giulio, A.4    Aschi, M.5
  • 7
    • 17844376024 scopus 로고    scopus 로고
    • NMR methods for studying membrane-active antimicrobial peptides
    • Strandberg E, Ulrich AS (2004) NMR methods for studying membrane-active antimicrobial peptides. Concepts in Magnetic Resonance A 23: 89-120.
    • (2004) Concepts In Magnetic Resonance A , vol.23 , pp. 89-120
    • Strandberg, E.1    Ulrich, A.S.2
  • 8
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y (2006) Mode of action of membrane active antimicrobial peptides. Biopolymers 66: 236-248.
    • (2006) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 9
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • PMID: 16778838
    • Peschel A, Sahl HG (2006) The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nature Reviews Microbiology 4: 529-536. doi: 10.1038/nrmicro1441 PMID: 16778838
    • (2006) Nature Reviews Microbiology , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 10
    • 69249096200 scopus 로고    scopus 로고
    • The roles of antimicrobial peptides in innate host defense
    • PMID: 19601838
    • Diamond G, Beckloff N, Weinberg A, Kisich KO (2009) The roles of antimicrobial peptides in innate host defense. Current Pharmaceutical Design 15: 2377-2392. doi: 10.2174/138161209788682325 PMID: 19601838
    • (2009) Current Pharmaceutical Design , vol.15 , pp. 2377-2392
    • Diamond, G.1    Beckloff, N.2    Weinberg, A.3    Kisich, K.O.4
  • 11
    • 84874083043 scopus 로고    scopus 로고
    • Antimicrobial peptidomimetics: Reinterpreting nature to deliver innovative therapeutics
    • PMID: 22798960
    • Scorciapino MA, Rinaldi AC (2012) Antimicrobial peptidomimetics: reinterpreting nature to deliver innovative therapeutics. Frontiers in Immunology 3: 1-4. doi: 10.3389/fimmu.2012.00171 PMID: 22798960
    • (2012) Frontiers In Immunology , vol.3 , pp. 1-4
    • Scorciapino, M.A.1    Rinaldi, A.C.2
  • 13
    • 84858013352 scopus 로고    scopus 로고
    • Exploiting dendrimer multivalency to combat emerging and re-emerging infectious diseases
    • PMID: 22126461
    • Mintzer MA, Dane EL, O'Toole GA, Grinstaff MW(2012) Exploiting dendrimer multivalency to combat emerging and re-emerging infectious diseases. Molecular Pharmaceutics 9: 342-354. doi: 10.1021/ mp2005033 PMID: 22126461
    • (2012) Molecular Pharmaceutics , vol.9 , pp. 342-354
    • Mintzer, M.A.1    Dane, E.L.2    O'Toole, G.A.3    Grinstaff, M.W.4
  • 14
    • 0036177932 scopus 로고    scopus 로고
    • Peptide dendrimers: Applications and synthesis
    • PMID: 12071226
    • Sadler K, Tam JP (2002) Peptide dendrimers: applications and synthesis. Reviews in Molecular Biotechnology 90: 195-229. PMID: 12071226
    • (2002) Reviews In Molecular Biotechnology , vol.90 , pp. 195-229
    • Sadler, K.1    Tam, J.P.2
  • 15
    • 21444448725 scopus 로고    scopus 로고
    • Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification
    • Pini A, Giuliani A, Falciani C, Runci Y, Ricci C, et al. (2005) Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification. Antimicrobial Agents and Chemotherapy 7: 2665-2672.
    • (2005) Antimicrobial Agents and Chemotherapy , vol.7 , pp. 2665-2672
    • Pini, A.1    Giuliani, A.2    Falciani, C.3    Runci, Y.4    Ricci, C.5
  • 16
    • 79960950287 scopus 로고    scopus 로고
    • Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches
    • PMID: 21598022
    • Giuliani A, Rinaldi AC (2011) Beyond natural antimicrobial peptides: multimeric peptides and other peptidomimetic approaches. Cellular and Molecular Life Sciences 68: 2255-2266. doi: 10.1007/s00018-011-0717-3 PMID: 21598022
    • (2011) Cellular and Molecular Life Sciences , vol.68 , pp. 2255-2266
    • Giuliani, A.1    Rinaldi, A.C.2
  • 17
    • 78249271990 scopus 로고    scopus 로고
    • Synthesis, characterization, antimicrobial activity and LPS-interaction properties of SB041, a novel dendrimeric peptide with antimicrobial properties
    • PMID: 20438783
    • Bruschi M, Pirri G, Giuliani A, Nicoletto SF, Baster I, et al. (2010) Synthesis, characterization, antimicrobial activity and LPS-interaction properties of SB041, a novel dendrimeric peptide with antimicrobial properties. Peptides 31: 1459-1467. doi: 10.1016/j.peptides.2010.04.022 PMID: 20438783
    • (2010) Peptides , vol.31 , pp. 1459-1467
    • Bruschi, M.1    Pirri, G.2    Giuliani, A.3    Nicoletto, S.F.4    Baster, I.5
  • 18
    • 84858040977 scopus 로고    scopus 로고
    • A novel dendrimeric peptide with antimicrobial properties: Structure-function analysis of SB056
    • PMID: 22404926
    • Scorciapino MA, Pirri G, Vargiu AV, Ruggerone P, Giuliani A, et al. (2012) A novel dendrimeric peptide with antimicrobial properties: structure-function analysis of SB056. Biophysical Journal 102: 1039-1048. doi: 10.1016/j.bpj.2012.01.048 PMID: 22404926
    • (2012) Biophysical Journal , vol.102 , pp. 1039-1048
    • Scorciapino, M.A.1    Pirri, G.2    Vargiu, A.V.3    Ruggerone, P.4    Giuliani, A.5
  • 19
    • 0035958848 scopus 로고    scopus 로고
    • A novel linear amphipathic β-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids
    • Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, et al. (2001) A novel linear amphipathic β-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. The Journal of Biological Chemistry 276: 27899-27906.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 27899-27906
    • Blazyk, J.1    Wiegand, R.2    Klein, J.3    Hammer, J.4    Epand, R.M.5
  • 20
    • 84858068813 scopus 로고    scopus 로고
    • Self-assembly of flexible β-strands into immobile amyloid-like β -sheets in membranes as revealed by solid-state19F NMR
    • PMID: 22452513
    • Wadhwani P, Strandberg E, Heidenreich N, Bürck J, Fanghänel S, et al. (2012) Self-assembly of flexible β-strands into immobile amyloid-like β -sheets in membranes as revealed by solid-state19F NMR. Journal of the American Chemical Society 134: 6512-6515. doi: 10.1021/ja301328f PMID: 22452513
    • (2012) Journal of The American Chemical Society , vol.134 , pp. 6512-6515
    • Wadhwani, P.1    Strandberg, E.2    Heidenreich, N.3    Bürck, J.4    Fanghänel, S.5
  • 21
    • 84878027678 scopus 로고    scopus 로고
    • Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes
    • PMID: 23652359
    • Wadhwani P, Reichert J, Strandberg E, Bürck J, Misiewicz J, et al. (2013) Stereochemical effects on the aggregation and biological properties of the fibril-forming peptide [KIGAKI]3 in membranes. Physical Chemistry Chemical Physics 15: 8962-8971. doi: 10.1039/c3cp50896j PMID: 23652359
    • (2013) Physical Chemistry Chemical Physics , vol.15 , pp. 8962-8971
    • Wadhwani, P.1    Reichert, J.2    Strandberg, E.3    Bürck, J.4    Misiewicz, J.5
  • 22
    • 38349121952 scopus 로고    scopus 로고
    • Length dependence of the coil $ β-sheet transition in a membrane environment
    • PMID: 18163629
    • Meier M, Seelig J (2008) Length dependence of the coil $ β-sheet transition in a membrane environment. Journal of the American Chemical Society 130: 1017-1024. doi: 10.1021/ja077231r PMID: 18163629
    • (2008) Journal of The American Chemical Society , vol.130 , pp. 1017-1024
    • Meier, M.1    Seelig, J.2
  • 23
    • 33748543300 scopus 로고    scopus 로고
    • Conformationally rigid trifluoromethyl-substituted α-amino acid designed for peptide structure analysis by solid state 19F-NMR
    • Mykhailiuk PK, Afonin S, Chernega AN, Rusanov EB, Platonov MO, et al. (2006) Conformationally rigid trifluoromethyl-substituted α-amino acid designed for peptide structure analysis by solid state 19F-NMR, Angewandte Chemie International Edition 45: 5659-5661.
    • (2006) Angewandte Chemie International Edition , vol.45 , pp. 5659-5661
    • Mykhailiuk, P.K.1    Afonin, S.2    Chernega, A.N.3    Rusanov, E.B.4    Platonov, M.O.5
  • 25
    • 0041525971 scopus 로고    scopus 로고
    • 4-Fluorophenylglycine as a label for 19F NMR structure analysis of membrane-associated peptides
    • Afonin S, Glaser RW, Berditchevskaia M, Wadhwani P, Gührs K-H, et al. (2003) 4-Fluorophenylglycine as a label for 19F NMR structure analysis of membrane-associated peptides. ChemBioChem 4: 1151-1163.
    • (2003) ChemBioChem , vol.4 , pp. 1151-1163
    • Afonin, S.1    Glaser, R.W.2    Berditchevskaia, M.3    Wadhwani, P.4    Gührs, K.-H.5
  • 26
    • 34249800918 scopus 로고    scopus 로고
    • Microtitre plate-based antibacterial assay incorporating resazurin as an indicator of cell growth, and its application in the in vitro antibacterial screening of phytochemicals
    • Sarker SD, Nahar L, Kumarasamy Y (2007) Microtitre plate-based antibacterial assay incorporating resazurin as an indicator of cell growth, and its application in the in vitro antibacterial screening of phytochemicals. Methods 42: 321-324.
    • (2007) Methods , vol.42 , pp. 321-324
    • Sarker, S.D.1    Nahar, L.2    Kumarasamy, Y.3
  • 27
    • 3843085404 scopus 로고    scopus 로고
    • CD12: A new high-flux beamline for ultraviolet and vacuum-ultraviolet circular dichroism on the SRS, Daresbury
    • Clarke DT, Jones G (2004) CD12: a new high-flux beamline for ultraviolet and vacuum-ultraviolet circular dichroism on the SRS, Daresbury. Journal of Synchrotron Radiation 11: 142-149.
    • (2004) Journal of Synchrotron Radiation , vol.11 , pp. 142-149
    • Clarke, D.T.1    Jones, G.2
  • 28
    • 25444446609 scopus 로고    scopus 로고
    • Calcium fluoride micro cells for synchrotron radiation circular dichroism spectroscopy
    • Wien F, Wallace BA (2005) Calcium fluoride micro cells for synchrotron radiation circular dichroism spectroscopy. Applied Spectroscopy 59: 1109-1113.
    • (2005) Applied Spectroscopy , vol.59 , pp. 1109-1113
    • Wien, F.1    Wallace, B.A.2
  • 29
    • 57549086833 scopus 로고    scopus 로고
    • Using a sterically restrictive amino acid as a 19F NMR label to monitor and to control peptide aggregation in membranes
    • Wadhwani P, Bürck J, Strandberg E, Mink C, Afonin S, et al. (2008) Using a sterically restrictive amino acid as a 19F NMR label to monitor and to control peptide aggregation in membranes. Journal of the American Chemical Society 130: 16515-16517.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 16515-16517
    • Wadhwani, P.1    Bürck, J.2    Strandberg, E.3    Mink, C.4    Afonin, S.5
  • 31
    • 84857371360 scopus 로고    scopus 로고
    • Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation
    • Wadhwani P, Reichert J, Bürck J, Ulrich AS (2012) Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation. European Biophysics Journal 41: 177-187.
    • (2012) European Biophysics Journal , vol.41 , pp. 177-187
    • Wadhwani, P.1    Reichert, J.2    Bürck, J.3    Ulrich, A.S.4
  • 32
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • Zhao H, Kinnunen PKJ (2002) Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. Journal of Biological Chemistry 277: 25170-25177.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.J.2
  • 34
    • 33645737243 scopus 로고    scopus 로고
    • Membrane lipid composition and the interaction of pardaxin: The role of cholesterol
    • Epand RF, Ramamoorthy A, Epand RM (2006) Membrane lipid composition and the interaction of pardaxin: the role of cholesterol. Protein and Peptide Letters 13: 1-5.
    • (2006) Protein and Peptide Letters , vol.13 , pp. 1-5
    • Epand, R.F.1    Ramamoorthy, A.2    Epand, R.M.3
  • 35
    • 65949090768 scopus 로고    scopus 로고
    • Domains in bacterial membranes and the action of antimicrobial agents
    • Epand RM, Epand RF (2009) Domains in bacterial membranes and the action of antimicrobial agents. Molecular Biosystems 5: 580-587.
    • (2009) Molecular Biosystems , vol.5 , pp. 580-587
    • Epand, R.M.1    Epand, R.F.2
  • 36
    • 0016377375 scopus 로고
    • Lipid composition as a guide to the classification of bacteria
    • Shaw N (1974) Lipid composition as a guide to the classification of bacteria. Advances in Applied Microbiology 17: 63-108.
    • (1974) Advances in Applied Microbiology , vol.17 , pp. 63-108
    • Shaw, N.1
  • 37
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane
    • Breukink E, Van Kraaij C, Demel RA, Siezen RJ, Kuipers OP, et al. (1997) The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane. Biochemistry 36: 6968-6976.
    • (1997) Biochemistry , vol.36 , pp. 6968-6976
    • Breukink, E.1    Van Kraaij, C.2    Demel, R.A.3    Siezen, R.J.4    Kuipers, O.P.5
  • 38
    • 33644873189 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics
    • Miles AJ, Wallace BA (2006) Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chemical Society Reviews 35: 39-51.
    • (2006) Chemical Society Reviews , vol.35 , pp. 39-51
    • Miles, A.J.1    Wallace, B.A.2
  • 39
    • 77952380215 scopus 로고    scopus 로고
    • Protein characterization by synchrotron radiation circular dichroism spectroscopy
    • Wallace BA (2009) Protein characterization by synchrotron radiation circular dichroism spectroscopy. Quarterly Reviews of Biophysics 42: 317-370.
    • (2009) Quarterly Reviews of Biophysics , vol.42 , pp. 317-370
    • Wallace, B.A.1
  • 41
    • 77952363935 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism (SRCD) spectroscopy-An enhanced method for examining protein conformations and protein interactions
    • Wallace BA, Janes RW (2010) Synchrotron radiation circular dichroism (SRCD) spectroscopy-An enhanced method for examining protein conformations and protein interactions. Biochemical Society Transactions 38: 861-873.
    • (2010) Biochemical Society Transactions , vol.38 , pp. 861-873
    • Wallace, B.A.1    Janes, R.W.2
  • 43
    • 0023652252 scopus 로고
    • Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments
    • Wallace BA, Teeters CL (1987) Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments. Biochemistry 26: 65-70.
    • (1987) Biochemistry , vol.26 , pp. 65-70
    • Wallace, B.A.1    Teeters, C.L.2
  • 44
    • 0020770309 scopus 로고
    • Circular differential scattering can be an important part of the circular dichroism of macromolecules
    • Bustamante C, Tinoco IJr, Maestre MF (1983) Circular differential scattering can be an important part of the circular dichroism of macromolecules. Proceedings of the National Academy of Science USA 80: 3568-3572.
    • (1983) Proceedings of the National Academy of Science USA , vol.80 , pp. 3568-3572
    • Bustamante, C.1    Tinoco, I.2    Maestre, M.F.3
  • 45
    • 1842783092 scopus 로고    scopus 로고
    • Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels
    • Glaser RW, Sachse C, Dürr UHN, Wadhwani P, Ulrich AS (2004) Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels. Journal of Magnetic Resonance 168: 153-163.
    • (2004) Journal of Magnetic Resonance , vol.168 , pp. 153-163
    • Glaser, R.W.1    Sachse, C.2    Dürr, U.H.N.3    Wadhwani, P.4    Ulrich, A.S.5
  • 46
    • 57549112908 scopus 로고    scopus 로고
    • Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F-NMR
    • Afonin SE, Grage SL, Ieronimo M, Wadhwani P, Ulrich AS (2008) Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F-NMR, Journal of the American Chemical Society 130: 16512-16514.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 16512-16514
    • Afonin, S.E.1    Grage, S.L.2    Ieronimo, M.3    Wadhwani, P.4    Ulrich, A.S.5
  • 47
    • 70350660660 scopus 로고    scopus 로고
    • Chemical labeling strategy with (R)- and (S)-trifluoromethylalanine for solid state 19F-NMR analysis of peptaibols in membranes
    • Maisch D, Wadhwani P, Afonin S, Böttcher C, Koksch B, et al. (2009) Chemical labeling strategy with (R)- and (S)-trifluoromethylalanine for solid state 19F-NMR analysis of peptaibols in membranes, Journal of the American Chemical Society 131: 15596-15597.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 15596-15597
    • Maisch, D.1    Wadhwani, P.2    Afonin, S.3    Böttcher, C.4    Koksch, B.5
  • 49
    • 85056024814 scopus 로고    scopus 로고
    • Solid-state 19F-nuclear magnetic resonance analysis of membrane-active peptides
    • Ramamoorthy A (ed.) CRC Press, Boca Raton, FL, USA
    • Grage S, Ulrich AS, Strandberg E, Sachse C, Berditchevskaia M, et al. (2005) Solid-state 19F-nuclear magnetic resonance analysis of membrane-active peptides. In: Ramamoorthy A (ed.), NMR Spectroscopy of Biological Solids. CRC Press, Boca Raton, FL, USA. Pp. 215-236.
    • (2005) NMR Spectroscopy of Biological Solids. , pp. 215-236
    • Grage, S.1    Ulrich, A.S.2    Strandberg, E.3    Sachse, C.4    Berditchevskaia, M.5
  • 51
    • 39749155818 scopus 로고    scopus 로고
    • Solid-state NMR analysis comparing the designer-made antibiotic MSI-103 with its parent peptide PGLa in lipid bilayers
    • Strandberg E, Kanithasen N, Tiltak D, Bürck J, Wadhwani P, et al. (2008) Solid-state NMR analysis comparing the designer-made antibiotic MSI-103 with its parent peptide PGLa in lipid bilayers. Biochemistry 47: 2601-2616.
    • (2008) Biochemistry , vol.47 , pp. 2601-2616
    • Strandberg, E.1    Kanithasen, N.2    Tiltak, D.3    Bürck, J.4    Wadhwani, P.5
  • 52
    • 78449307933 scopus 로고    scopus 로고
    • Compatibility of the conformationally rigid CF3-Bpg side chain with the hydrophobic coiled-coil interface
    • Salwiczek M, Mikhailiuk PK, Afonin S, Komarov IV, Ulrich AS, et al. (2010) Compatibility of the conformationally rigid CF3-Bpg side chain with the hydrophobic coiled-coil interface. Amino Acids 39: 1589-1593.
    • (2010) Amino Acids , vol.39 , pp. 1589-1593
    • Salwiczek, M.1    Mikhailiuk, P.K.2    Afonin, S.3    Komarov, I.V.4    Ulrich, A.S.5
  • 55
    • 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 (1999) Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochimica et Biophysica Acta 1462: 71-87.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 56
    • 84874199480 scopus 로고    scopus 로고
    • The mechanism of action of antimicrobial peptides: Lipid vesicles vs. Bacteria
    • Melo MN, Castanho MA (2012) The mechanism of action of antimicrobial peptides: lipid vesicles vs. bacteria. Frontiers in Immunology 3: 236.
    • (2012) Frontiers In Immunology , vol.3 , pp. 236
    • Melo, M.N.1    Castanho, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.