메뉴 건너뛰기




Volumn 27, Issue 5, 2014, Pages 935-948

Bovine and human lactoferricin peptides: Chimeras and new cyclic analogs

Author keywords

Click chemistry; Lactoferricin; Lactoferrin; Peptide cyclization; Sortase A

Indexed keywords

DISULFIDE; LACTOFERRICIN; SORTASE; ANTIMICROBIAL CATIONIC PEPTIDE; CYCLOPEPTIDE; HYBRID PROTEIN; LACTOFERRICIN B; LACTOFERRIN; LIPOSOME; PEPTIDE FRAGMENT;

EID: 84910004130     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-014-9753-4     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 84861398752 scopus 로고    scopus 로고
    • Lactoferrin: An alternative view of its role in human biological fluids
    • 10.1139/O2012-013 1:CAS:528:DC%2BC38XntlWmsrc%3D 22553915
    • Alexander DB, Iigo M, Yamauchi K, Suzui M (2012) Lactoferrin: an alternative view of its role in human biological fluids. Biochem Cell Biol 90:279-306. doi: 10.1139/O2012-013
    • (2012) Biochem Cell Biol , vol.90 , pp. 279-306
    • Alexander, D.B.1    Iigo, M.2    Yamauchi, K.3    Suzui, M.4
  • 2
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • 10.1016/0076-6879(66)08014-5 1:CAS:528:DyaF1cXhvFeksQ%3D%3D
    • Ames BN, Neufeld EF, Ginsberg V (1966) Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol 8:115-118. doi: 10.1016/0076-6879(66)08014-5
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1    Neufeld, E.F.2    Ginsberg, V.3
  • 3
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • 1:CAS:528:DyaE2sXkvVWit70%3D 327545
    • Arnold RR, Cole MF, McGhee JR (1977) A bactericidal effect for human lactoferrin. Science 197:263-265
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 4
    • 0020003674 scopus 로고
    • Bactericidal activity of human lactoferrin: Differentiation from the stasis of iron deprivation
    • 1:CAS:528:DyaL38XhsF2itbw%3D 351118 6802759
    • Arnold RR, Russell JE, Champion WJ et al (1982) Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation. Infect Immun 35:792-799
    • (1982) Infect Immun , vol.35 , pp. 792-799
    • Arnold, R.R.1    Russell, J.E.2    Champion, W.J.3
  • 5
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • 10.1016/j.biochi.2008.05.006 1:CAS:528:DC%2BD1MXktF2gsg%3D%3D 18541155
    • Baker EN, Baker HM (2009) A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 91:3-10. doi: 10.1016/j.biochi.2008.05.006
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.N.1    Baker, H.M.2
  • 6
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • 1:CAS:528:DyaK3sXkt1Cnt7g%3D 1490908
    • Bellamy W, Takase M, Wakabayashi H et al (1992a) Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 73:472-479
    • (1992) J Appl Bacteriol , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3
  • 7
    • 0026716132 scopus 로고
    • Identification of the bactericidal domain of lactoferrin
    • 1:CAS:528:DyaK38XkvVKmt7s%3D 1599934
    • Bellamy W, Takase M, Yamauchi K et al (1992b) Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta 1121:130-136
    • (1992) Biochim Biophys Acta , vol.1121 , pp. 130-136
    • Bellamy, W.1    Takase, M.2    Yamauchi, K.3
  • 8
    • 58149127828 scopus 로고    scopus 로고
    • Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides
    • 10.1016/j.biochi.2008.05.019 1:CAS:528:DC%2BD1MXktF2htg%3D%3D 18573310
    • Bolscher JGM, Adão R, Nazmi K et al (2009) Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides. Biochimie 91:123-132. doi: 10.1016/j.biochi.2008.05.019
    • (2009) Biochimie , vol.91 , pp. 123-132
    • Bolscher, J.G.M.1    Adão, R.2    Nazmi, K.3
  • 9
    • 80051675805 scopus 로고    scopus 로고
    • Sortase A as a tool for high-yield histatin cyclization
    • 10.1096/fj.11-182212 1:CAS:528:DC%2BC3MXpvFers7o%3D 21525488
    • Bolscher JGM, Oudhoff MJ, Nazmi K et al (2011) Sortase A as a tool for high-yield histatin cyclization. FASEB J 25:2650-2658. doi: 10.1096/fj.11-182212
    • (2011) FASEB J , vol.25 , pp. 2650-2658
    • Bolscher, J.G.M.1    Oudhoff, M.J.2    Nazmi, K.3
  • 10
    • 0018899060 scopus 로고
    • Lactoferrin in human milk: Its role in iron absorption and protection against enteric infection in the newborn infant
    • 1:CAS:528:DyaL3cXlsVKqsr4%3D 1626933 7002055
    • Brock JH (1980) Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch Dis Child 55:417-421
    • (1980) Arch Dis Child , vol.55 , pp. 417-421
    • Brock, J.H.1
  • 11
    • 0021689157 scopus 로고
    • Influence of lipid composition and ionic strength on the stability of liposomes
    • 1:CAS:528:DyaL2MXitVSjsQ%3D%3D 6520758
    • Crommelin DJA (1984) Influence of lipid composition and ionic strength on the stability of liposomes. J Pharm Sci 73:1559-1563
    • (1984) J Pharm Sci , vol.73 , pp. 1559-1563
    • Crommelin, D.J.A.1
  • 12
    • 3142691160 scopus 로고    scopus 로고
    • Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides
    • 10.1021/bi035948v 1:CAS:528:DC%2BD2cXltFSqt7k%3D 15248771
    • Dathe M, Nikolenko H, Klose J, Bienert M (2004) Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides. Biochemistry 43:9140-9150. doi: 10.1021/bi035948v
    • (2004) Biochemistry , vol.43 , pp. 9140-9150
    • Dathe, M.1    Nikolenko, H.2    Klose, J.3    Bienert, M.4
  • 13
    • 42149116252 scopus 로고    scopus 로고
    • What can light scattering spectroscopy do for membrane-active peptide studies?
    • 10.1002/psc 1:CAS:528:DC%2BD1cXkslyjtrc%3D 18189339
    • Domingues MM, Castanho MARB, Santos NC (2008) What can light scattering spectroscopy do for membrane-active peptide studies? J Pept Sci 14:394-400. doi: 10.1002/psc
    • (2008) J Pept Sci , vol.14 , pp. 394-400
    • Domingues, M.M.1    Castanho, M.2    Santos, N.C.3
  • 14
    • 84856081379 scopus 로고    scopus 로고
    • Lactoferrin-lipopolysaccharide (LPS) binding as key to antibacterial and antiendotoxic effects
    • 10.1016/j.intimp.2011.11.002 1:CAS:528:DC%2BC38Xht1aht7w%3D 22101278
    • Drago-Serrano ME, de la Garza-Amaya M, Luna JS, Campos-Rodríguez R (2012) Lactoferrin-lipopolysaccharide (LPS) binding as key to antibacterial and antiendotoxic effects. Int Immunopharmacol 12:1-9. doi: 10.1016/j.intimp.2011.11.002
    • (2012) Int Immunopharmacol , vol.12 , pp. 1-9
    • Drago-Serrano, M.E.1    De La Garza-Amaya, M.2    Luna, J.S.3    Campos-Rodríguez, R.4
  • 15
    • 77956132155 scopus 로고    scopus 로고
    • Depolarization, bacterial membrane composition, and the antimicrobial action of ceragenins
    • 10.1128/AAC.00380-10 1:CAS:528:DC%2BC3cXht12ktL7L 2934994 20585129
    • Epand RF, Pollard JE, Wright JO et al (2010) Depolarization, bacterial membrane composition, and the antimicrobial action of ceragenins. Antimicrob Agents Chemother 54:3708-3713. doi: 10.1128/AAC.00380-10
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 3708-3713
    • Epand, R.F.1    Pollard, J.E.2    Wright, J.O.3
  • 16
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: A lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • 10.1007/s00018-005-5373-z 1:CAS:528:DC%2BD2MXhtlSms7vP 16261252
    • Gifford JL, Hunter HN, Vogel HJ (2005) Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell Mol Life Sci 62:2588-2598. doi: 10.1007/s00018-005-5373-z
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 17
    • 84855798186 scopus 로고    scopus 로고
    • Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin
    • 10.1016/j.bbamem.2011.11.023 1:CAS:528:DC%2BC38XhvFeisLs%3D 22155682
    • Haney EF, Nazmi K, Bolscher JGM, Vogel HJ (2012) Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin. Biochim Biophys Acta 1818:762-775. doi: 10.1016/j.bbamem.2011.11.023
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 762-775
    • Haney, E.F.1    Nazmi, K.2    Bolscher, J.G.M.3    Vogel, H.J.4
  • 18
    • 0035941062 scopus 로고    scopus 로고
    • The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
    • 1:CAS:528:DC%2BD3MXos1Khtbg%3D 11728458
    • Haukland HH, Ulvatne H, Sandvik K, Vorland LH (2001) The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett 508:389-393
    • (2001) FEBS Lett , vol.508 , pp. 389-393
    • Haukland, H.H.1    Ulvatne, H.2    Sandvik, K.3    Vorland, L.H.4
  • 19
    • 79956131018 scopus 로고    scopus 로고
    • Maintaining biological activity by using triazoles as disulfide bond mimetics
    • 10.1002/anie.201005846 1:CAS:528:DC%2BC3MXmtFymuro%3D
    • Holland-Nell K, Meldal M (2011) Maintaining biological activity by using triazoles as disulfide bond mimetics. Angew Chemie 50:5204-5206. doi: 10.1002/anie.201005846
    • (2011) Angew Chemie , vol.50 , pp. 5204-5206
    • Holland-Nell, K.1    Meldal, M.2
  • 20
    • 23044463641 scopus 로고    scopus 로고
    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
    • 10.1128/AAC.49.8.3387 1:CAS:528:DC%2BD2MXntFChurY%3D 1196233 16048952
    • Hunter HN, Demcoe AR, Jenssen H et al (2005) Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob Agents Chemother 49:3387-3395. doi: 10.1128/AAC.49.8.3387
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3387-3395
    • Hunter, H.N.1    Demcoe, A.R.2    Jenssen, H.3
  • 21
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • 10.1021/bi972323m 1:CAS:528:DyaK1cXhsVOlurk%3D 9521752
    • Hwang PM, Zhou N, Shan X et al (1998) Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37:4288-4298. doi: 10.1021/bi972323m
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3
  • 22
    • 58149113170 scopus 로고    scopus 로고
    • Antimicrobial properties of lactoferrin
    • 10.1016/j.biochi.2008.05.015 1:CAS:528:DC%2BD1MXktF2huw%3D%3D 18573312
    • Jenssen H, Hancock REW (2009) Antimicrobial properties of lactoferrin. Biochimie 91:19-29. doi: 10.1016/j.biochi.2008.05.015
    • (2009) Biochimie , vol.91 , pp. 19-29
    • Jenssen, H.1    Hancock, R.E.W.2
  • 23
    • 0034617196 scopus 로고    scopus 로고
    • Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines
    • 1:CAS:528:DC%2BD3cXkvVyiu7k%3D 10877842
    • Krijgsveld J, Zaat SAJ, Van Veelen PA et al (2000) Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines. J Biol Chem 275:20374-20381
    • (2000) J Biol Chem , vol.275 , pp. 20374-20381
    • Krijgsveld, J.1    Zaat, S.A.J.2    Van Veelen, P.A.3
  • 24
    • 84861394265 scopus 로고    scopus 로고
    • LF immunomodulatory strategies: Mastering
    • 10.1139/O11-059 1:CAS:528:DC%2BC38XntlSmtbk%3D 22300429
    • Latorre D, Berlutti F, Valenti P et al (2012) LF immunomodulatory strategies: mastering. Biochem Cell Biol 90:269-278. doi: 10.1139/O11-059
    • (2012) Biochem Cell Biol , vol.90 , pp. 269-278
    • Latorre, D.1    Berlutti, F.2    Valenti, P.3
  • 25
    • 28444462150 scopus 로고    scopus 로고
    • Lactoferrin: A modulator of immune and inflammatory responses
    • 10.1007/s00018-005-5370-2 1:CAS:528:DC%2BD2MXhtlSms7vM 16261255
    • Legrand D, Elass E, Carpentier M, Mazurier J (2005) Lactoferrin: a modulator of immune and inflammatory responses. Cell Mol Life Sci 62:2549-2559. doi: 10.1007/s00018-005-5370-2
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2549-2559
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 26
    • 84883195229 scopus 로고    scopus 로고
    • Click chemistry in peptide-based drug design
    • 10.3390/molecules18089797 1:CAS:528:DC%2BC3sXhtlKlsrbN 23959192
    • Li H, Aneja R, Chaiken I (2013) Click chemistry in peptide-based drug design. Molecules 18:9797-9817. doi: 10.3390/molecules18089797
    • (2013) Molecules , vol.18 , pp. 9797-9817
    • Li, H.1    Aneja, R.2    Chaiken, I.3
  • 27
    • 83555172221 scopus 로고    scopus 로고
    • Comparative antimicrobial activity and mechanism of action of bovine lactoferricin-derived synthetic peptides
    • 10.1007/s10534-011-9465-y 1:CAS:528:DC%2BC3MXhsVKhsrnI 21607695
    • Liu Y, Han F, Xie Y, Wang Y (2011) Comparative antimicrobial activity and mechanism of action of bovine lactoferricin-derived synthetic peptides. Biometals 24:1069-1078. doi: 10.1007/s10534-011-9465-y
    • (2011) Biometals , vol.24 , pp. 1069-1078
    • Liu, Y.1    Han, F.2    Xie, Y.3    Wang, Y.4
  • 28
    • 77958581350 scopus 로고    scopus 로고
    • Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs
    • 10.1371/journal.pone.0012684
    • Nguyen LT, Chau JK, Perry NA et al (2010) Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs. PLoS ONE 5:11-18. doi: 10.1371/journal.pone.0012684
    • (2010) PLoS ONE , vol.5 , pp. 11-18
    • Nguyen, L.T.1    Chau, J.K.2    Perry, N.A.3
  • 29
    • 0002554841 scopus 로고    scopus 로고
    • The role of outer membrane and efflux pumps in the resistance of gram-negative bacteria. Can we improve drug access?
    • 10.1016/S1368-7646(98)80023-X 1:CAS:528:DyaK1MXhtlyntLs%3D 16904394
    • Nikaido H (1998) The role of outer membrane and efflux pumps in the resistance of gram-negative bacteria. Can we improve drug access? Drug Resist Updat 1:93-98. doi: 10.1016/S1368-7646(98)80023-X
    • (1998) Drug Resist Updat , vol.1 , pp. 93-98
    • Nikaido, H.1
  • 30
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • 10.1128/MMBR.67.4.593 1:CAS:528:DC%2BD2cXmt1Sqsg%3D%3D 309051 14665678
    • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67:593-656. doi: 10.1128/MMBR.67.4.593
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 31
    • 0034705132 scopus 로고    scopus 로고
    • Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: Effect on structure, interaction with model membranes, and biological function
    • 10.1021/bi992408i 1:CAS:528:DC%2BD3cXislygsLY%3D 10821683
    • Oren Z, Shai Y (2000) Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function. Biochemistry 39:6103-6114. doi: 10.1021/bi992408i
    • (2000) Biochemistry , vol.39 , pp. 6103-6114
    • Oren, Z.1    Shai, Y.2
  • 32
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • 10.1073/pnas.150518097 1:CAS:528:DC%2BD3cXlt1Ggt7w%3D 26932 10890923
    • Park CB, Yi KS, Matsuzaki K et al (2000) Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc Natl Acad Sci USA 97:8245-8250. doi: 10.1073/pnas.150518097
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3
  • 33
    • 27944474777 scopus 로고    scopus 로고
    • "Clickable" agarose for affinity chromatography
    • 10.1021/bc0501496 1:CAS:528:DC%2BD2MXpvFaitLY%3D 16287252
    • Punna S, Kaltgrad E, Finn MG (2005) "Clickable" agarose for affinity chromatography. Bioconjug Chem 16:1536-1541. doi: 10.1021/bc0501496
    • (2005) Bioconjug Chem , vol.16 , pp. 1536-1541
    • Punna, S.1    Kaltgrad, E.2    Finn, M.G.3
  • 34
  • 35
    • 0038064554 scopus 로고    scopus 로고
    • Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity
    • 10.1139/O01-236 11908644
    • Strøm MB, Haug BE, Rekdal Ø et al (2002) Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity. Biochem Cell Biol 80:65-74. doi: 10.1139/O01-236
    • (2002) Biochem Cell Biol , vol.80 , pp. 65-74
    • Strøm, M.B.1    Haug, B.E.2    Rekdal Ø3
  • 36
    • 0028037262 scopus 로고
    • A review: The active peptide of lactoferrin
    • 1:CAS:528:DyaK2MXis1Snt7k%3D 7825467
    • Tomita M, Takase M, Bellamy W, Shimamura S (1994) A review: the active peptide of lactoferrin. Acta Paediatr Jpn 36:585-591
    • (1994) Acta Paediatr Jpn , vol.36 , pp. 585-591
    • Tomita, M.1    Takase, M.2    Bellamy, W.3    Shimamura, S.4
  • 37
    • 0035831078 scopus 로고    scopus 로고
    • Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes
    • 1:CAS:528:DC%2BD3MXhvVansbs%3D 11248238
    • Ulvatne H, Haukland HH, Olsvik O, Vorland LH (2001) Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes. FEBS Lett 492:62-65
    • (2001) FEBS Lett , vol.492 , pp. 62-65
    • Ulvatne, H.1    Haukland, H.H.2    Olsvik, O.3    Vorland, L.H.4
  • 38
    • 4143102460 scopus 로고    scopus 로고
    • Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis
    • 10.1016/j.femsle.2004.07.001 1:CAS:528:DC%2BD2cXmsVGiurg%3D 15321686
    • Ulvatne H, Samuelsen Ø, Haukland HH et al (2004) Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis. FEMS Microbiol Lett 237:377-384. doi: 10.1016/j.femsle.2004.07.001
    • (2004) FEMS Microbiol Lett , vol.237 , pp. 377-384
    • Ulvatne, H.1    Samuelsen Ø2    Haukland, H.H.3
  • 39
    • 33748941585 scopus 로고    scopus 로고
    • Interactions of bovine lactoferricin with acidic phospholipid bilayers and its antimicrobial activity as studied by solid-state NMR
    • 10.1016/j.bbamem.2006.06.014 1:CAS:528:DC%2BD28XhtVamsr7P 16884683
    • Umeyama M, Kira A, Nishimura K, Naito A (2006) Interactions of bovine lactoferricin with acidic phospholipid bilayers and its antimicrobial activity as studied by solid-state NMR. Biochim Biophys Acta 1758:1523-1528. doi: 10.1016/j.bbamem.2006.06.014
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1523-1528
    • Umeyama, M.1    Kira, A.2    Nishimura, K.3    Naito, A.4
  • 40
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • 10.1007/s00018-005-5372-0 1:CAS:528:DC%2BD2MXhtlSms7vO 16261253
    • Valenti P, Antonini G (2005) Lactoferrin: an important host defence against microbial and viral attack. Cell Mol Life Sci 62:2576-2587. doi: 10.1007/s00018-005-5372-0
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 41
    • 0025659446 scopus 로고
    • Interaction of lactoferrin with Escherichia coli cells and correlation with antibacterial activity
    • 1:CAS:528:DyaK3MXltlWktL4%3D 2093835
    • Visca P, Dalmastri C, Verzili D et al (1990) Interaction of lactoferrin with Escherichia coli cells and correlation with antibacterial activity. Med Microbiol Immunol 179:323-333
    • (1990) Med Microbiol Immunol , vol.179 , pp. 323-333
    • Visca, P.1    Dalmastri, C.2    Verzili, D.3
  • 42
    • 84861361791 scopus 로고    scopus 로고
    • Lactoferrin, a bird's eye view
    • 10.1139/O2012-016 1:CAS:528:DC%2BC38XntlSmur8%3D 22540735
    • Vogel HJ (2012) Lactoferrin, a bird's eye view. Biochem Cell Biol 90:233-244. doi: 10.1139/O2012-016
    • (2012) Biochem Cell Biol , vol.90 , pp. 233-244
    • Vogel, H.J.1
  • 43
    • 0032411892 scopus 로고    scopus 로고
    • Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin
    • 1:STN:280:DyaK1M7mtl2guw%3D%3D 10066056
    • Vorland LH, Ulvatne H, Andersen J et al (1998) Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin. Scand J Infect Dis 30:513-517
    • (1998) Scand J Infect Dis , vol.30 , pp. 513-517
    • Vorland, L.H.1    Ulvatne, H.2    Andersen, J.3
  • 44
    • 79959580534 scopus 로고    scopus 로고
    • Contemporary strategies for peptide macrocyclization
    • 10.1038/nchem.1062 1:CAS:528:DC%2BC3MXnvFWjtrc%3D 21697871
    • White CJ, Yudin AK (2011) Contemporary strategies for peptide macrocyclization. Nat Chem 3:509-524. doi: 10.1038/nchem.1062
    • (2011) Nat Chem , vol.3 , pp. 509-524
    • White, C.J.1    Yudin, A.K.2
  • 45
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • 10.1038/nprot.2007.521 1:CAS:528:DC%2BD1cXhvVyls78%3D 18274517
    • Wiegand I, Hilpert K, Hancock REW (2008) Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat Protoc 3:163-175. doi: 10.1038/nprot.2007.521
    • (2008) Nat Protoc , vol.3 , pp. 163-175
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.