메뉴 건너뛰기




Volumn 29, Issue 12, 2013, Pages 4048-4056

Peptide-bacteria interactions using engineered surface-immobilized peptides from class IIa bacteriocins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL PEPTIDE; BIOSENSING PLATFORMS; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIUM; GRAZING ANGLE INFRARED SPECTROSCOPY; LISTERIA MONOCYTOGENES; MEMBRANE-BOUND RECEPTORS; MOLECULAR RECOGNITION ELEMENT;

EID: 84875593249     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la3041743     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D.; Hill, C.; Ross, R. P. Bacteriocins: Developing innate immunity for food Nat. Rev. Microbiol. 2005, 3, 777-88
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 2
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 2005, 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. W. Peptide antibiotics Lancet. 1997, 349, 418-422
    • (1997) Lancet. , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 5
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, 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
    • Yeaman, M.R.1    Yount, N.Y.2
  • 6
    • 77950860384 scopus 로고    scopus 로고
    • Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy
    • Fantner, G. E.; Barbero, R. J.; Gray, D. S.; Belcher, A. M. Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy Nat. Nanotechnol. 2010, 5, 280-5
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 280-285
    • Fantner, G.E.1    Barbero, R.J.2    Gray, D.S.3    Belcher, A.M.4
  • 7
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E. W.; Scott, M. G. The role of antimicrobial peptides in animal defenses Proc. Natl. Acad. Sci. U.S.A 2000, 97, 8856-8861
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 8
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley, W. C. Describing the mechanism of antimicrobial peptide action with the interfacial activity model ACS Chem. Biol. 2010, 5, 905-917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 9
    • 33749464383 scopus 로고    scopus 로고
    • Advances in antimicrobial peptide immunobiology
    • Yount, N. Y.; Bayer, A. S.; Xiong, Y. Q.; Yeaman, M. R. Advances in antimicrobial peptide immunobiology Biopolymers 2006, 84, 435-58
    • (2006) Biopolymers , vol.84 , pp. 435-458
    • Yount, N.Y.1    Bayer, A.S.2    Xiong, Y.Q.3    Yeaman, M.R.4
  • 10
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin, D. W.; Ramamoorthy, A. Studies on anticancer activities of antimicrobial peptides Biochim. Biophys. Acta 2008, 1778, 357-75
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 11
    • 0030220363 scopus 로고    scopus 로고
    • Fluorogenic and chromogenic enzyme substrates in culture media and identification tests
    • Manafi, M. Fluorogenic and chromogenic enzyme substrates in culture media and identification tests Int. J. Food Microbiol. 1996, 31, 45-58
    • (1996) Int. J. Food Microbiol. , vol.31 , pp. 45-58
    • Manafi, M.1
  • 12
    • 37349033608 scopus 로고    scopus 로고
    • Detection, quantification and vitality of Listeria monocytogenes in food as determined by quantitative PCR
    • Rantsiou, K.; Alessandria, V.; Urso, R.; Dolci, P.; Cocolin, L. Detection, quantification and vitality of Listeria monocytogenes in food as determined by quantitative PCR Int. J. Food Microbiol. 2008, 121, 99-105
    • (2008) Int. J. Food Microbiol. , vol.121 , pp. 99-105
    • Rantsiou, K.1    Alessandria, V.2    Urso, R.3    Dolci, P.4    Cocolin, L.5
  • 13
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas, P.; Mor, A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates Annu. Rev. Microbiol. 1995, 49, 277-304
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 14
    • 78650593740 scopus 로고    scopus 로고
    • Electrical detection of pathogenic bacteria via immobilized antimicrobial peptides
    • Mannoor, M. S.; Zhang, S.; Link, A. J.; McAlpine, M. C. Electrical detection of pathogenic bacteria via immobilized antimicrobial peptides Proc. Natl. Acad. Sci. U.S.A 2010, 107, 19207-12
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 19207-19212
    • Mannoor, M.S.1    Zhang, S.2    Link, A.J.3    McAlpine, M.C.4
  • 15
    • 36849045621 scopus 로고    scopus 로고
    • Antimicrobial peptides: New recognition molecules for detecting botulinum toxins
    • Kulagina, N.; Anderson, G.; Ligler, F.; Shaffer, K.; Taitt, C. Antimicrobial peptides: New recognition molecules for detecting botulinum toxins Sensors 2007, 7, 2808-2824
    • (2007) Sensors , vol.7 , pp. 2808-2824
    • Kulagina, N.1    Anderson, G.2    Ligler, F.3    Shaffer, K.4    Taitt, C.5
  • 17
    • 26444573133 scopus 로고    scopus 로고
    • Antimicrobial peptides for detection of bacteria in biosensor assays
    • Kulagina, N. V.; Lassman, M. E.; Ligler, F. S.; Taitt, C. R. Antimicrobial peptides for detection of bacteria in biosensor assays Anal. Chem. 2005, 77, 6504-8
    • (2005) Anal. Chem. , vol.77 , pp. 6504-6508
    • Kulagina, N.V.1    Lassman, M.E.2    Ligler, F.S.3    Taitt, C.R.4
  • 18
    • 78649821260 scopus 로고    scopus 로고
    • Tethering antimicrobial peptides: Current status and potential challenges
    • Onaizi, S. A.; Leong, S. S. Tethering antimicrobial peptides: Current status and potential challenges Biotechnol. Adv. 2011, 29, 67-74
    • (2011) Biotechnol. Adv. , vol.29 , pp. 67-74
    • Onaizi, S.A.1    Leong, S.S.2
  • 19
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher, N. L.; Sailer, M.; Niemczura, W. P.; Nakashima, T. T.; Stiles, M. E.; Vederas, J. C. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria Biochemistry 1997, 36, 15062-72
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau Gallagher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 21
    • 28044472548 scopus 로고    scopus 로고
    • Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure, and mode of action
    • Fimland, G.; Johnsen, L.; Dalhus, B.; Nissen-Meyer, J. Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure, and mode of action J. Pept. Sci. 2005, 11, 688-96
    • (2005) J. Pept. Sci. , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 22
    • 65149100197 scopus 로고    scopus 로고
    • Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria
    • Nissen-Meyer, J.; Rogne, P.; Oppegard, C.; Haugen, H. S.; Kristiansen, P. E. Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria Curr. Pharm. Biotechnol. 2009, 10, 19-37
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegard, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 23
    • 15744401646 scopus 로고    scopus 로고
    • The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • Johnsen, L.; Fimland, G.; Nissen-Meyer, J. The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum J. Biol. Chem. 2005, 280, 9243-50
    • (2005) J. Biol. Chem. , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 24
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland, G.; Blingsmo, O. R.; Sletten, K.; Jung, G.; Nes, I. F.; Nissen-Meyer, J. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity Appl. Environ. Microbiol. 1996, 62, 3313-8
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 25
    • 0034736095 scopus 로고    scopus 로고
    • Analogues of bacteriocins: Antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives
    • Yan, L. Z.; Gibbs, A. C.; Stiles, M. E.; Wishart, D. S.; Vederas, J. C. Analogues of bacteriocins: Antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives J. Med. Chem. 2000, 43, 4579-81
    • (2000) J. Med. Chem. , vol.43 , pp. 4579-4581
    • Yan, L.Z.1    Gibbs, A.C.2    Stiles, M.E.3    Wishart, D.S.4    Vederas, J.C.5
  • 26
    • 3142737226 scopus 로고    scopus 로고
    • Dynamic relationships among type IIa bacteriocins: Temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic alpha helix as a receptor-binding region
    • Kaur, K.; Andrew, L. C.; Wishart, D. S.; Vederas, J. C. Dynamic relationships among type IIa bacteriocins: Temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic alpha helix as a receptor-binding region Biochemistry 2004, 43, 9009-20
    • (2004) Biochemistry , vol.43 , pp. 9009-9020
    • Kaur, K.1    Andrew, L.C.2    Wishart, D.S.3    Vederas, J.C.4
  • 27
    • 79953227398 scopus 로고    scopus 로고
    • Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1
    • Haugen, H. S.; Fimland, G.; Nissen-Meyer, J. Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1 Appl. Environ. Microbiol. 2011, 77, 1966-72
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1966-1972
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3
  • 28
    • 4444341230 scopus 로고    scopus 로고
    • Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis
    • Ramnath, M.; Arous, S.; Gravesen, A.; Hastings, J. W.; Hechard, Y. Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis Microbiology 2004, 150, 2663-8
    • (2004) Microbiology , vol.150 , pp. 2663-2668
    • Ramnath, M.1    Arous, S.2    Gravesen, A.3    Hastings, J.W.4    Hechard, Y.5
  • 29
    • 0033930978 scopus 로고    scopus 로고
    • Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Ramnath, M.; Beukes, M.; Tamura, K.; Hastings, J. W. Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis Appl. Environ. Microbiol. 2000, 66, 3098-101
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3098-3101
    • Ramnath, M.1    Beukes, M.2    Tamura, K.3    Hastings, J.W.4
  • 30
    • 33847796246 scopus 로고    scopus 로고
    • Common mechanisms of target cell recognition and immunity for class II bacteriocins
    • Diep, D. B.; Skaugen, M.; Salehian, Z.; Holo, H.; Nes, I. F. Common mechanisms of target cell recognition and immunity for class II bacteriocins Proc. Natl. Acad. Sci. U.S.A 2007, 104, 2384-9
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5
  • 31
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E.; Colescott, R. L.; Bossinger, C. D.; Cook, P. I. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides Anal. Biochem. 1970, 34, 595-8
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 32
    • 54349099254 scopus 로고    scopus 로고
    • Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1
    • Derksen, D. J.; Boudreau, M. A.; Vederas, J. C. Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1 ChemBiochem 2008, 9, 1898-901
    • (2008) ChemBiochem , vol.9 , pp. 1898-1901
    • Derksen, D.J.1    Boudreau, M.A.2    Vederas, J.C.3
  • 33
    • 0032204284 scopus 로고    scopus 로고
    • Formation of oriented helical peptide layers on a gold surface due to the self-assembling properties of peptides
    • Miura, Y.; Kimura, S.; Imanishi, Y.; Umemura, J. Formation of oriented helical peptide layers on a gold surface due to the self-assembling properties of peptides Langmuir 1998, 14, 6935-6940
    • (1998) Langmuir , vol.14 , pp. 6935-6940
    • Miura, Y.1    Kimura, S.2    Imanishi, Y.3    Umemura, J.4
  • 34
    • 0030739097 scopus 로고    scopus 로고
    • Formation of stable polypeptide monolayers at interfaces: Controlling molecular conformation and orientation
    • Boncheva, M.; Vogel, H. Formation of stable polypeptide monolayers at interfaces: Controlling molecular conformation and orientation Biophys. J. 1997, 73, 1056-1072
    • (1997) Biophys. J. , vol.73 , pp. 1056-1072
    • Boncheva, M.1    Vogel, H.2
  • 35
    • 0001242101 scopus 로고
    • Infrared dichroism and molecular conformation of alpha-form poly-gamma-benzyl- l -glutamate
    • Tsuboi, M. Infrared dichroism and molecular conformation of alpha-form poly-gamma-benzyl- l -glutamate J. Polym. Sci. 1962, 59, 139-153
    • (1962) J. Polym. Sci. , vol.59 , pp. 139-153
    • Tsuboi, M.1
  • 36
    • 0000982685 scopus 로고    scopus 로고
    • Using surface plasmon resonance spectroscopy to measure the association of detergents with self-assembled monolayers of hexadecanethiolate on gold
    • Sigal, G. B.; Mrksich, M.; Whitesides, G. M. Using surface plasmon resonance spectroscopy to measure the association of detergents with self-assembled monolayers of hexadecanethiolate on gold Langmuir 1997, 13, 2749-2755
    • (1997) Langmuir , vol.13 , pp. 2749-2755
    • Sigal, G.B.1    Mrksich, M.2    Whitesides, G.M.3
  • 37
    • 34447567289 scopus 로고    scopus 로고
    • Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity
    • Salvucci, E.; Saavedra, L.; Sesma, F. Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity J. Antimicrob. Chemother. 2007, 59, 1102-8
    • (2007) J. Antimicrob. Chemother. , vol.59 , pp. 1102-1108
    • Salvucci, E.1    Saavedra, L.2    Sesma, F.3
  • 39
    • 0025880710 scopus 로고
    • Studies of forming 3(10)-helices and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by fourier-transform infrared-spectroscopy
    • Kennedy, D. F.; Crisma, M.; Toniolo, C.; Chapman, D. Studies of forming 3(10)-helices and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by fourier-transform infrared-spectroscopy Biochemistry 1991, 30, 6541-6548
    • (1991) Biochemistry , vol.30 , pp. 6541-6548
    • Kennedy, D.F.1    Crisma, M.2    Toniolo, C.3    Chapman, D.4
  • 40
    • 15844417244 scopus 로고    scopus 로고
    • Alpha-helix-inducing dimerization of synthetic polypeptide scaffolds on gold
    • Enander, K.; Aili, D.; Baltzer, L.; Lundstrom, I.; Liedberg, B. Alpha-helix-inducing dimerization of synthetic polypeptide scaffolds on gold Langmuir 2005, 21, 2480-7
    • (2005) Langmuir , vol.21 , pp. 2480-2487
    • Enander, K.1    Aili, D.2    Baltzer, L.3    Lundstrom, I.4    Liedberg, B.5
  • 41
    • 55049107866 scopus 로고    scopus 로고
    • The effects of solution structure on the surface conformation and orientation of a cysteine-terminated antimicrobial peptide cecropin P1
    • Uzarski, J. R.; Tannous, A.; Morris, J. R.; Mello, C. M. The effects of solution structure on the surface conformation and orientation of a cysteine-terminated antimicrobial peptide cecropin P1 Colloids Surf., B 2008, 67, 157-165
    • (2008) Colloids Surf., B , vol.67 , pp. 157-165
    • Uzarski, J.R.1    Tannous, A.2    Morris, J.R.3    Mello, C.M.4
  • 42
    • 0022873754 scopus 로고
    • On the adsorption of beta-lactoglobulin on hydrophilic gold surfaces: Studies by infrared reflection absorption-spectroscopy and ellipsometry
    • Liedberg, B.; Ivarsson, B.; Hegg, P. O.; Lundstrom, I. On the adsorption of beta-lactoglobulin on hydrophilic gold surfaces: Studies by infrared reflection absorption-spectroscopy and ellipsometry J. Colloid Interface Sci. 1986, 114, 386-397
    • (1986) J. Colloid Interface Sci. , vol.114 , pp. 386-397
    • Liedberg, B.1    Ivarsson, B.2    Hegg, P.O.3    Lundstrom, I.4
  • 43
    • 33745304170 scopus 로고    scopus 로고
    • Formation of oriented polypeptides on Au(111) surface depends on the secondary structure controlled by peptide length
    • Sakurai, T.; Oka, S.; Kubo, A.; Nishiyama, K.; Taniguchi, I. Formation of oriented polypeptides on Au(111) surface depends on the secondary structure controlled by peptide length J. Pept. Sci. 2006, 12, 396-402
    • (2006) J. Pept. Sci. , vol.12 , pp. 396-402
    • Sakurai, T.1    Oka, S.2    Kubo, A.3    Nishiyama, K.4    Taniguchi, I.5
  • 44
    • 0028222975 scopus 로고
    • Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane
    • Abee, T.; Klaenhammer, T. R.; Letellier, L. Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane Appl. Environ. Microbiol. 1994, 60, 1006-13
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1006-1013
    • Abee, T.1    Klaenhammer, T.R.2    Letellier, L.3
  • 45
    • 0031717018 scopus 로고    scopus 로고
    • Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles
    • Chen, Y.; Ludescher, R. D.; Montville, T. J. Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles Appl. Environ. Microbiol. 1998, 64, 3530-2
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3530-3532
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 46
    • 0035316822 scopus 로고    scopus 로고
    • Biological activities and structural properties of the atypical bacteriocins mesenterocin 52b and leucocin b-ta33a
    • Corbier, C.; Krier, F.; Mulliert, G.; Vitoux, B.; Revol-Junelles, A. M. Biological activities and structural properties of the atypical bacteriocins mesenterocin 52b and leucocin b-ta33a Appl. Environ. Microbiol. 2001, 67, 1418-22
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1418-1422
    • Corbier, C.1    Krier, F.2    Mulliert, G.3    Vitoux, B.4    Revol-Junelles, A.M.5
  • 48
    • 69949137695 scopus 로고    scopus 로고
    • Class II one-peptide bacteriocins target a phylogenetically defined subgroup of mannose phosphotransferase systems on sensitive cells
    • Kjos, M.; Nes, I. F.; Diep, D. B. Class II one-peptide bacteriocins target a phylogenetically defined subgroup of mannose phosphotransferase systems on sensitive cells Microbiology 2009, 155, 2949-61
    • (2009) Microbiology , vol.155 , pp. 2949-2961
    • Kjos, M.1    Nes, I.F.2    Diep, D.B.3
  • 50
    • 70449635387 scopus 로고    scopus 로고
    • Binding, inactivation, and adhesion forces between antimicrobial peptide cecropin P1 and pathogenic E. coli
    • Strauss, J.; Kadilak, A.; Cronin, C.; Mello, C. M.; Camesano, T. A. Binding, inactivation, and adhesion forces between antimicrobial peptide cecropin P1 and pathogenic E. coli Colloids Surf., B 2010, 75, 156-164
    • (2010) Colloids Surf., B , vol.75 , pp. 156-164
    • Strauss, J.1    Kadilak, A.2    Cronin, C.3    Mello, C.M.4    Camesano, T.A.5
  • 51
    • 15444367184 scopus 로고    scopus 로고
    • Immobilization of Escherichia coli cells by use of the antimicrobial peptide cecropin P1
    • Gregory, K.; Mello, C. M. Immobilization of Escherichia coli cells by use of the antimicrobial peptide cecropin P1 Appl. Environ. Microbiol. 2005, 71, 1130-4
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1130-1134
    • Gregory, K.1    Mello, C.M.2
  • 53
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • Rusmini, F.; Zhong, Z.; Feijen, J. Protein immobilization strategies for protein biochips Biomacromolecules 2007, 8, 1775-89
    • (2007) Biomacromolecules , vol.8 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.