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Volumn 21, Issue 2, 2015, Pages 165-177

The design and functional characterization of the antimicrobial and antibiofilm activities of BMAP27-Melittin, a rationally designed hybrid peptide

Author keywords

Antibiofilm; Antimicrobial peptides; BMAP 27; Folding simulations; Hybrid peptide; Melittin

Indexed keywords


EID: 84939978885     PISSN: 15733149     EISSN: 15733904     Source Type: Journal    
DOI: 10.1007/s10989-014-9444-6     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 84861184381 scopus 로고    scopus 로고
    • Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog
    • 1:CAS:528:DC%2BC38Xlt1Kms7g%3D 22484288
    • Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C (2012) Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog. Peptides 35:291-299
    • (2012) Peptides , vol.35 , pp. 291-299
    • Almaaytah, A.1    Zhou, M.2    Wang, L.3    Chen, T.4    Walker, B.5    Shaw, C.6
  • 2
    • 0026570489 scopus 로고
    • Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity
    • 1:CAS:528:DyaK38Xht1Cktrk%3D 1733777
    • Andreu D, Ubach J, Boman A, Wåhlin B, Wade D, Merrifield RB, Boman HG (1992) Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett 296(2):190-194
    • (1992) FEBS Lett , vol.296 , Issue.2 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wåhlin, B.4    Wade, D.5    Merrifield, R.B.6    Boman, H.G.7
  • 3
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • 1:CAS:528:DC%2BD2cXhtFeis77I 15475354
    • Asthana N, Yadav SP, Ghosh JK (2004) Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J Biol Chem 279:55042-55050
    • (2004) J Biol Chem , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 6
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • 1:CAS:528:DC%2BD2MXhslGjtbo%3D
    • Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Micro 3:238-250
    • (2005) Nat Rev Micro , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 10
    • 0034914849 scopus 로고    scopus 로고
    • The MBEC assay system: multiple equivalent biofilms for antibiotic and biocide susceptibility testing
    • 1:CAS:528:DC%2BD3MXlsVygtbc%3D 11398443
    • Ceri H, Olson M, Morck D, Storey D, Read R, Buret A et al (2001) The MBEC assay system: multiple equivalent biofilms for antibiotic and biocide susceptibility testing. Methods Enzymol 337:377-385
    • (2001) Methods Enzymol , vol.337 , pp. 377-385
    • Ceri, H.1    Olson, M.2    Morck, D.3    Storey, D.4    Read, R.5    Buret, A.6
  • 11
    • 84939946747 scopus 로고    scopus 로고
    • Discovery Studio (2013) version 3.5 ed. Accelrys Inc., San Diego
    • Discovery Studio (2013) version 3.5 ed. Accelrys Inc., San Diego
  • 12
    • 84961985307 scopus 로고    scopus 로고
    • Development of a generalized born model parametrization for proteins and nucleic acids
    • 1:CAS:528:DyaK1MXitlKrtLo%3D
    • Dominy BN, Brooks CL (1999) Development of a generalized born model parametrization for proteins and nucleic acids. J Phys Chem B 103:3765-3773
    • (1999) J Phys Chem B , vol.103 , pp. 3765-3773
    • Dominy, B.N.1    Brooks, C.L.2
  • 13
    • 33645767676 scopus 로고    scopus 로고
    • Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp
    • 1426969 1:CAS:528:DC%2BD28XjvFOrsLg%3D 16569868
    • Eckert R, Qi F, Yarbrough DK, He J, Anderson MH, Shi W (2006) Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp. Antimicrob Agents Chemother 50:1480-1488
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1480-1488
    • Eckert, R.1    Qi, F.2    Yarbrough, D.K.3    He, J.4    Anderson, M.H.5    Shi, W.6
  • 14
    • 0003954314 scopus 로고
    • Structural studies of bee melittin
    • 1327300 1:STN:280:DC%2BC3croslSmsQ%3D%3D 19431375
    • Eisenberg D, Terwilliger TC, Tsui F (1980) Structural studies of bee melittin. Biophys J 32(1):252-254
    • (1980) Biophys J , vol.32 , Issue.1 , pp. 252-254
    • Eisenberg, D.1    Terwilliger, T.C.2    Tsui, F.3
  • 15
    • 84885356069 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 and its fragments possess both antimicrobial and antibiofilm activities against multidrug-resistant Acinetobacter baumannii
    • 1:CAS:528:DC%2BC3sXhslClsbjO 24071034
    • Feng X, Sambanthamoorthy K, Palys T, Paranavitana C (2013) The human antimicrobial peptide LL-37 and its fragments possess both antimicrobial and antibiofilm activities against multidrug-resistant Acinetobacter baumannii. Peptides 49:131-137
    • (2013) Peptides , vol.49 , pp. 131-137
    • Feng, X.1    Sambanthamoorthy, K.2    Palys, T.3    Paranavitana, C.4
  • 17
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a comeback
    • 1:CAS:528:DC%2BC3sXntF2qtr0%3D 23657384
    • Fox JL (2013) Antimicrobial peptides stage a comeback. Nat Biotechnol 31(5):379-382
    • (2013) Nat Biotechnol , vol.31 , Issue.5 , pp. 379-382
    • Fox, J.L.1
  • 18
    • 79955759821 scopus 로고    scopus 로고
    • Critical shortage of new antibiotics in development against multidrug-resistant bacteria - Time to react is now
    • 21435939
    • Freire-Moran L, Aronsson B, Manz C, Gyssens IC, So AD, Monnet DL et al (2011) Critical shortage of new antibiotics in development against multidrug-resistant bacteria - Time to react is now. Drug Resist Updat 14:118-124
    • (2011) Drug Resist Updat , vol.14 , pp. 118-124
    • Freire-Moran, L.1    Aronsson, B.2    Manz, C.3    Gyssens, I.C.4    So, A.D.5    Monnet, D.L.6
  • 19
    • 0346729747 scopus 로고    scopus 로고
    • Comparative activities of cecropin A, melittin, and cecropin A - melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii
    • 1:CAS:528:DC%2BD2cXptFaj 14706545
    • Giacometti A, Cirioni O, Kamysz W, D'Amato G, Silvestri C, Del Prete MS et al (2003) Comparative activities of cecropin A, melittin, and cecropin A - melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii. Peptides 24:1315-1318
    • (2003) Peptides , vol.24 , pp. 1315-1318
    • Giacometti, A.1    Cirioni, O.2    Kamysz, W.3    D'Amato, G.4    Silvestri, C.5    Del Prete, M.S.6
  • 20
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: an overview of a promising class of therapeutics
    • 1:CAS:528:DC%2BD2sXns1aqtL8%3D
    • Giuliani A, Pirri G, Nicoletto S (2007) Antimicrobial peptides: an overview of a promising class of therapeutics. Central Eur J Biol 2:1-33
    • (2007) Central Eur J Biol , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.3
  • 22
    • 79953148897 scopus 로고    scopus 로고
    • Alpha-helical cationic antimicrobial peptides: relationships of structure and function
    • 1:CAS:528:DC%2BC3cXmtlKkur0%3D 21203984
    • Huang Y, Huang J, Chen Y (2010) Alpha-helical cationic antimicrobial peptides: relationships of structure and function. Protein Cell 1:143-152
    • (2010) Protein Cell , vol.1 , pp. 143-152
    • Huang, Y.1    Huang, J.2    Chen, Y.3
  • 23
    • 84925884356 scopus 로고    scopus 로고
    • Role of helicity of α-helical antimicrobial peptides to improve specificity
    • 4130925 1:CAS:528:DC%2BC2cXnslGrtb0%3D 24805306
    • Huang Y, He L, Li G, Zhai N, Jiang H, Chen Y (2014) Role of helicity of α-helical antimicrobial peptides to improve specificity. Protein Cell 5:631-642
    • (2014) Protein Cell , vol.5 , pp. 631-642
    • Huang, Y.1    He, L.2    Li, G.3    Zhai, N.4    Jiang, H.5    Chen, Y.6
  • 24
    • 33746532309 scopus 로고    scopus 로고
    • Peptide antimicrobial agents
    • 1539102 1:CAS:528:DC%2BD28XosVaqsrk%3D 16847082
    • Jenssen H, Hamill P, Hancock REW (2006) Peptide antimicrobial agents. Clin Microbiol Rev 19:491-511
    • (2006) Clin Microbiol Rev , vol.19 , pp. 491-511
    • Jenssen, H.1    Hamill, P.2    Hancock, R.E.W.3
  • 25
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: obstacles and realistic outlook
    • 1:CAS:528:DC%2BD28XpsVWrs7s%3D 16890021
    • Marr AK, Gooderham WJ, Hancock REW (2006) Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Curr Opin Pharmacol 6:468-472
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.W.3
  • 26
    • 36749053991 scopus 로고    scopus 로고
    • Bactericidal action of daptomycin against stationary-phase and nondividing Staphylococcus aureus cells
    • 2167999 1:CAS:528:DC%2BD2sXhsVWisLfI 17923487
    • Mascio CTM, Alder JD, Silverman JA (2007) Bactericidal action of daptomycin against stationary-phase and nondividing Staphylococcus aureus cells. Antimicrob Agents Chemother 51:4255-4260
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 4255-4260
    • Mascio, C.T.M.1    Alder, J.D.2    Silverman, J.A.3
  • 27
    • 0036263259 scopus 로고    scopus 로고
    • Biofilm bacteria: formation and comparative susceptibility to antibiotics
    • 226988, 11989739
    • Olson ME, Ceri H, Morck DW, Buret AG, Read RR (2002) Biofilm bacteria: formation and comparative susceptibility to antibiotics. Can J Vet Res 66:86-92
    • (2002) Can J Vet Res , vol.66 , pp. 86-92
    • Olson, M.E.1    Ceri, H.2    Morck, D.W.3    Buret, A.G.4    Read, R.R.5
  • 28
    • 44449129941 scopus 로고    scopus 로고
    • Increased resistance to cationic antimicrobial peptide LL-37 in methicillin-resistant strains of Staphylococcus aureus
    • 2902849 1:CAS:528:DC%2BD1cXmtVajt7o%3D 18367458
    • Ouhara K, Komatsuzawa H, Kawai T, Nishi H, Fujiwara T, Fujiue Y et al (2008) Increased resistance to cationic antimicrobial peptide LL-37 in methicillin-resistant strains of Staphylococcus aureus. J Antimicrob Chemother 61:1266-1269
    • (2008) J Antimicrob Chemother , vol.61 , pp. 1266-1269
    • Ouhara, K.1    Komatsuzawa, H.2    Kawai, T.3    Nishi, H.4    Fujiwara, T.5    Fujiue, Y.6
  • 29
    • 1942454707 scopus 로고    scopus 로고
    • HP(2-9)-magainin 2(1-12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membrane
    • 1:CAS:528:DC%2BD2cXjtlOlur8%3D 15119592
    • Park Y, Lee DG, Hahm KS (2004) HP(2-9)-magainin 2(1-12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membrane. J Pept Sci 10(4):204-209
    • (2004) J Pept Sci , vol.10 , Issue.4 , pp. 204-209
    • Park, Y.1    Lee, D.G.2    Hahm, K.S.3
  • 30
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: key components of the innate immune system
    • 1:CAS:528:DC%2BC38XmsFOjtbY%3D 22074402
    • Pasupuleti M, Schmidtchen A, Malmsten M (2012) Antimicrobial peptides: key components of the innate immune system. Crit Rev Biotechnol 32:143-171
    • (2012) Crit Rev Biotechnol , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Schmidtchen, A.2    Malmsten, M.3
  • 31
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: primeval molecules or future drugs?
    • 2965748 21060861
    • Peters BM, Shirtliff ME, Jabra-Rizk MA (2010) Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog 6:e1001067
    • (2010) PLoS Pathog , vol.6
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 32
    • 80052783463 scopus 로고    scopus 로고
    • Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients
    • 1:CAS:528:DC%2BC3MXhtFGltbzN 21849157
    • Pompilio A, Scocchi M, Pomponio S, Guida F, Di Primio A, Fiscarelli E et al (2011) Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients. Peptides 32:1807-1814
    • (2011) Peptides , vol.32 , pp. 1807-1814
    • Pompilio, A.1    Scocchi, M.2    Pomponio, S.3    Guida, F.4    Di Primio, A.5    Fiscarelli, E.6
  • 33
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • 1:CAS:528:DyaE2sXktVGhsL4%3D
    • Ryckaert J-P, Ciccotti G, Berendsen HJC (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23:327-341
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 34
    • 84864381356 scopus 로고    scopus 로고
    • In vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillin-resistant, vancomycin-intermediate, vancomycin-resistant, daptomycin-nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus
    • 3421571 1:CAS:528:DC%2BC38XhtFajsL%2FN 22585222
    • Saravolatz LD, Pawlak J, Johnson L, Bonilla H, Fakih MG, Fugelli A et al (2012) In vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillin-resistant, vancomycin-intermediate, vancomycin-resistant, daptomycin-nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus. Antimicrob Agents Chemother 56:4478-4482
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 4478-4482
    • Saravolatz, L.D.1    Pawlak, J.2    Johnson, L.3    Bonilla, H.4    Fakih, M.G.5    Fugelli, A.6
  • 35
    • 0031832107 scopus 로고    scopus 로고
    • Cecropin A-magainin 2 hybrid peptides having potent antimicrobial activity with low hemolytic effect
    • 1:CAS:528:DyaK1cXjsVymurg%3D 9623765
    • Shin SY, Kang JH, Lee MK, Kim SY, Kim Y, Hahm KS (1998) Cecropin A-magainin 2 hybrid peptides having potent antimicrobial activity with low hemolytic effect. Biochem Mol Biol Int 44(6):1119-1126
    • (1998) Biochem Mol Biol Int , vol.44 , Issue.6 , pp. 1119-1126
    • Shin, S.Y.1    Kang, J.H.2    Lee, M.K.3    Kim, S.Y.4    Kim, Y.5    Hahm, K.S.6
  • 36
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • 1:CAS:528:DyaK28XmvVWqsLg%3D 8910461
    • Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M (1996) Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 271:28375-28381
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 37
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • 1329835 1:CAS:528:DyaL2sXhvFKh 3779000
    • Vogel H, Jaehnig F (1986) The structure of melittin in membranes. Biophys J 50(4):573
    • (1986) Biophys J , vol.50 , Issue.4 , pp. 573
    • Vogel, H.1    Jaehnig, F.2
  • 38
    • 84862830535 scopus 로고    scopus 로고
    • Effect of a novel antimicrobial peptide chrysophsin-1 on oral pathogens and Streptococcus mutans biofilms
    • 1:CAS:528:DC%2BC38XjtlOmsbY%3D 22281025
    • Wang W, Tao R, Tong Z, Ding Y, Kuang R, Zhai S et al (2012) Effect of a novel antimicrobial peptide chrysophsin-1 on oral pathogens and Streptococcus mutans biofilms. Peptides 33:212-219
    • (2012) Peptides , vol.33 , pp. 212-219
    • Wang, W.1    Tao, R.2    Tong, Z.3    Ding, Y.4    Kuang, R.5    Zhai, S.6
  • 39
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides: the ancient arm of the human immune system
    • 21178486
    • Wiesner J, Vilcinskas A (2010) Antimicrobial peptides: the ancient arm of the human immune system. Virulence 1:440-464
    • (2010) Virulence , vol.1 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2


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