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Volumn 5, Issue 3, 2009, Pages 352-358

Leishmanicidal Activity and Immobilization of dermaseptin 01 antimicrobial peptides in ultrathin films for nanomedicine applications

Author keywords

Antimicrobial peptides; Biosensors; Electrochemistry; Leishmania; Nanotechnology

Indexed keywords

ACTIVE MATERIAL; ANTIMICROBIAL PEPTIDE; ANTIMICROBIAL PEPTIDES; BIOLOGICAL MOLECULE; BIONANOSTRUCTURES; CONDUCTIVE ELECTRODES; ELECTRO-ACTIVITY; ELECTROACTIVE; ELECTROCHEMICAL EXPERIMENTS; ELECTROLYTIC SOLUTION; HELIX STRUCTURES; HOST ORGANISM; INNATE IMMUNE SYSTEMS; LAYERED FILMS; LEISHMANIA; NANO-STRUCTURED; NANOMEDICINES; NANOSTRUCTURED FILMS; OXIDATION CURRENTS; OXIDATION PEAK; PHARMACEUTICAL INDUSTRY; POSITIVE CHARGES; PROMASTIGOTES;

EID: 69249246960     PISSN: 15499634     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nano.2008.11.001     Document Type: Article
Times cited : (42)

References (40)
  • 1
    • 0142243423 scopus 로고    scopus 로고
    • Bed occupancy and overcrowding as determinant factors in the incidence of MRSA infections within general ward settings
    • Borg M.A. Bed occupancy and overcrowding as determinant factors in the incidence of MRSA infections within general ward settings. J Hosp Infect 54 (2003) 316-318
    • (2003) J Hosp Infect , vol.54 , pp. 316-318
    • Borg, M.A.1
  • 2
    • 0042389540 scopus 로고    scopus 로고
    • Molecular design of multifunctional antibacterial agents against methicillin resistant Staphylococcus aureus (MRSA)
    • Kubo I., Fujita K.I., and Nihei K.I. Molecular design of multifunctional antibacterial agents against methicillin resistant Staphylococcus aureus (MRSA). Bioorg Med Chem Lett 11 (2003) 4255-4262
    • (2003) Bioorg Med Chem Lett , vol.11 , pp. 4255-4262
    • Kubo, I.1    Fujita, K.I.2    Nihei, K.I.3
  • 3
    • 33645803815 scopus 로고    scopus 로고
    • Antimicrobial peptides: therapeutic potential
    • Zhang L., and Falla T.J. Antimicrobial peptides: therapeutic potential. Exp Opin Pharmacother 7 (2006) 653-663
    • (2006) Exp Opin Pharmacother , vol.7 , pp. 653-663
    • Zhang, L.1    Falla, T.J.2
  • 6
    • 2942592590 scopus 로고    scopus 로고
    • Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides
    • Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D., and Rollins-Smith L. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology 323 (2004) 268-275
    • (2004) Virology , vol.323 , pp. 268-275
    • Chinchar, V.G.1    Bryan, L.2    Silphadaung, U.3    Noga, E.4    Wade, D.5    Rollins-Smith, L.6
  • 7
    • 15244349233 scopus 로고    scopus 로고
    • The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro
    • Lorin C., Saidi H., Belaid A., Zairi A., Baleux F., Hocini H., et al. The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro. Virology 334 (2005) 264-275
    • (2005) Virology , vol.334 , pp. 264-275
    • Lorin, C.1    Saidi, H.2    Belaid, A.3    Zairi, A.4    Baleux, F.5    Hocini, H.6
  • 8
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms
    • Mor A., Hani K., and Nicolas P. The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J Biol Chem 269 (1994) 31635-31641
    • (1994) J Biol Chem , vol.269 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 9
    • 0037147330 scopus 로고    scopus 로고
    • Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells
    • Brand G.D., Leite J.R.S.A., Silva L.P., Albuquerque S., Prates M.V., Azevedo R.B., et al. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J Biol Chem 277 (2002) 49332-49340
    • (2002) J Biol Chem , vol.277 , pp. 49332-49340
    • Brand, G.D.1    Leite, J.R.S.A.2    Silva, L.P.3    Albuquerque, S.4    Prates, M.V.5    Azevedo, R.B.6
  • 10
    • 0031646792 scopus 로고    scopus 로고
    • Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin
    • De Lucca A.J., Bland J.M., Jacks T.J., Grimm C., and Walsh T.J. Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin. Med Mycol 36 (1998) 291-298
    • (1998) Med Mycol , vol.36 , pp. 291-298
    • De Lucca, A.J.1    Bland, J.M.2    Jacks, T.J.3    Grimm, C.4    Walsh, T.J.5
  • 11
    • 0037025297 scopus 로고    scopus 로고
    • Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture
    • Efron L., Dagan A., Gaidukov L., Ginsburg H., and Mor A. Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture. J Biol Chem 277 (2002) 24067-24072
    • (2002) J Biol Chem , vol.277 , pp. 24067-24072
    • Efron, L.1    Dagan, A.2    Gaidukov, L.3    Ginsburg, H.4    Mor, A.5
  • 13
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock R.E.W., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol 16 (1998) 82-87
    • (1998) Trends Biotechnol , vol.16 , pp. 82-87
    • Hancock, R.E.W.1    Lehrer, R.2
  • 14
    • 0345306671 scopus 로고    scopus 로고
    • Synthetic peptides in the form of dendrimers become resistant to protease activity
    • Bracci L., Falciani C., Lelli B., Lozzi L., Runci Y., Pini A., et al. Synthetic peptides in the form of dendrimers become resistant to protease activity. J Biol Chem 278 (2003) 46590-46595
    • (2003) J Biol Chem , vol.278 , pp. 46590-46595
    • Bracci, L.1    Falciani, C.2    Lelli, B.3    Lozzi, L.4    Runci, Y.5    Pini, A.6
  • 15
    • 0036183822 scopus 로고    scopus 로고
    • Antimicrobial dendrimeric peptides
    • Tam P.J., Lu Y.A., and Yang J.L. Antimicrobial dendrimeric peptides. Eur J Biochem 269 (2002) 923-932
    • (2002) Eur J Biochem , vol.269 , pp. 923-932
    • Tam, P.J.1    Lu, Y.A.2    Yang, J.L.3
  • 16
    • 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., Lelli B., et al. Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification. Antimicrob Agents Chemother 49 (2005) 2665-2672
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2665-2672
    • Pini, A.1    Giuliani, A.2    Falciani, C.3    Runci, Y.4    Ricci, C.5    Lelli, B.6
  • 19
    • 33847674028 scopus 로고    scopus 로고
    • Using capacitance measurements as the detection method in antigen-containing layer-by-layer films for biosensing
    • Zucolotto V., Daghastanli K.R.P., Hayasaka C.O., Riul Jr. A., Ciancaglini P., and Oliveira Jr. O.N. Using capacitance measurements as the detection method in antigen-containing layer-by-layer films for biosensing. Anal Chem 79 (2007) 2163-2167
    • (2007) Anal Chem , vol.79 , pp. 2163-2167
    • Zucolotto, V.1    Daghastanli, K.R.P.2    Hayasaka, C.O.3    Riul Jr., A.4    Ciancaglini, P.5    Oliveira Jr., O.N.6
  • 20
    • 36648999564 scopus 로고    scopus 로고
    • Natural gum-assisted phthalocyanine immobilization in electroactive nanocomposites: physicochemical characterization and sensing applications
    • Zampa M.F., Brito A.C.F., Kitagawa I.L., Constantino C.J.L., Oliveira Jr. O.N., Cunha H.N., et al. Natural gum-assisted phthalocyanine immobilization in electroactive nanocomposites: physicochemical characterization and sensing applications. Biomacromolecules 8 (2007) 3408-3413
    • (2007) Biomacromolecules , vol.8 , pp. 3408-3413
    • Zampa, M.F.1    Brito, A.C.F.2    Kitagawa, I.L.3    Constantino, C.J.L.4    Oliveira Jr., O.N.5    Cunha, H.N.6
  • 23
    • 0345659212 scopus 로고    scopus 로고
    • Leishmania/HIV co-infections: epidemiology in Europe
    • Desjeux P., and Alvar J. Leishmania/HIV co-infections: epidemiology in Europe. Ann Trop Med Parasitology 97 (2003) 3-15
    • (2003) Ann Trop Med Parasitology , vol.97 , pp. 3-15
    • Desjeux, P.1    Alvar, J.2
  • 24
    • 0027957621 scopus 로고
    • Human visceral leishmaniasis in Alpes-Maritimes, France: epidemiological characteristics for the period 1985-1992
    • Marty P., Le Fichoux Y., Pratlong F., and Gari-Toussaint M. Human visceral leishmaniasis in Alpes-Maritimes, France: epidemiological characteristics for the period 1985-1992. Trans R Soc Trop Med Hyg 88 (1994) 33-34
    • (1994) Trans R Soc Trop Med Hyg , vol.88 , pp. 33-34
    • Marty, P.1    Le Fichoux, Y.2    Pratlong, F.3    Gari-Toussaint, M.4
  • 25
    • 0026674542 scopus 로고
    • Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms
    • Bates P.A., Robertson C.D., Tetley L., and Coombs G.H. Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms. Parasitology 105 (1992) 193-202
    • (1992) Parasitology , vol.105 , pp. 193-202
    • Bates, P.A.1    Robertson, C.D.2    Tetley, L.3    Coombs, G.H.4
  • 26
    • 0029978872 scopus 로고    scopus 로고
    • Stage-regulated expression of cruzipain, the major cysteine-proteinase of Trypanosoma cruzi is independent of the level of RNA
    • Tomás A.M., and Kelly J.M. Stage-regulated expression of cruzipain, the major cysteine-proteinase of Trypanosoma cruzi is independent of the level of RNA. Mol Biochem Parasitol 76 (1996) 91-104
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 91-104
    • Tomás, A.M.1    Kelly, J.M.2
  • 27
    • 0024303873 scopus 로고
    • Efficient oxygen reduction in alkaline solution with platinum phthalocyanine on porous carbon
    • Shukla A.K., Paliteiro C., Manoharan R., Hamnett A., and Goodenough J.B. Efficient oxygen reduction in alkaline solution with platinum phthalocyanine on porous carbon. J Appl Electrochem 19 (1899) 105
    • (1899) J Appl Electrochem , vol.19 , pp. 105
    • Shukla, A.K.1    Paliteiro, C.2    Manoharan, R.3    Hamnett, A.4    Goodenough, J.B.5
  • 28
    • 37449023691 scopus 로고    scopus 로고
    • Trypanocidal and leishmanicidal activities of different antimicrobial peptides (AMPs) isolated from aquatic animals
    • Löfgren S.E., Miletti L.C., Steindel M., Bachère E., and Barracco M.A. Trypanocidal and leishmanicidal activities of different antimicrobial peptides (AMPs) isolated from aquatic animals. Exp Parasitol 118 (2008) 197-202
    • (2008) Exp Parasitol , vol.118 , pp. 197-202
    • Löfgren, S.E.1    Miletti, L.C.2    Steindel, M.3    Bachère, E.4    Barracco, M.A.5
  • 29
    • 0034862968 scopus 로고    scopus 로고
    • N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide
    • Chicharro C., Granata C., Lozano R., Andreu D., and Rivas L. N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide. Antimicrob Agents Chemother 45 (2001) 2441-2449
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2441-2449
    • Chicharro, C.1    Granata, C.2    Lozano, R.3    Andreu, D.4    Rivas, L.5
  • 30
    • 0034635367 scopus 로고    scopus 로고
    • Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity
    • Feder R., Dagan A., and Mor A. Structure-activity relationship study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity. J Biol Chem 275 (2000) 4230-4238
    • (2000) J Biol Chem , vol.275 , pp. 4230-4238
    • Feder, R.1    Dagan, A.2    Mor, A.3
  • 31
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva P.I., Daffre S., and Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J Biol Chem 275 (2000) 33464-33470
    • (2000) J Biol Chem , vol.275 , pp. 33464-33470
    • Silva, P.I.1    Daffre, S.2    Bulet, P.3
  • 33
    • 0029566096 scopus 로고
    • Activity of lytic peptides against intracellular Trypanosoma cruzi amastigotes in vitro and parasitemias in mice
    • Barr S.C., Rose D., and Jaynes J.M. Activity of lytic peptides against intracellular Trypanosoma cruzi amastigotes in vitro and parasitemias in mice. J Parasitol 81 (1995) 974-978
    • (1995) J Parasitol , vol.81 , pp. 974-978
    • Barr, S.C.1    Rose, D.2    Jaynes, J.M.3
  • 34
    • 20044381842 scopus 로고    scopus 로고
    • Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus
    • Leite J.R.S.A., Silva L.P., Rodrigues M.I.S., Prates M.V., Brand G.D., Lacava B.M., et al. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. Peptides 26 (2005) 565-573
    • (2005) Peptides , vol.26 , pp. 565-573
    • Leite, J.R.S.A.1    Silva, L.P.2    Rodrigues, M.I.S.3    Prates, M.V.4    Brand, G.D.5    Lacava, B.M.6
  • 35
    • 31944435787 scopus 로고    scopus 로고
    • A 'toolbox' for chemical and biological monitoring requirements for the European Union's Water Framework Directive
    • Allan I.J., Vrana B., Greenwood R., Mills G.A., Roig B., and Gonzalez C. A 'toolbox' for chemical and biological monitoring requirements for the European Union's Water Framework Directive. Talanta 69 (2006) 302-322
    • (2006) Talanta , vol.69 , pp. 302-322
    • Allan, I.J.1    Vrana, B.2    Greenwood, R.3    Mills, G.A.4    Roig, B.5    Gonzalez, C.6
  • 36
    • 33748143348 scopus 로고    scopus 로고
    • Amperometric protein sensor-fabricated as a polypyrrole, poly-aminophenylboronic acid bilayer
    • Rick J., and Chou T.C. Amperometric protein sensor-fabricated as a polypyrrole, poly-aminophenylboronic acid bilayer. Biosensors Bioelectronics 22 (2006) 329-335
    • (2006) Biosensors Bioelectronics , vol.22 , pp. 329-335
    • Rick, J.1    Chou, T.C.2
  • 37
    • 34248509140 scopus 로고    scopus 로고
    • Optically responsive nanoparticle layers for the label-free analysis of biospecific interactions in array formats
    • Dahint R., Trileva E., Acunmana H., Konrad U., Zimmera M., Stadler V., et al. Optically responsive nanoparticle layers for the label-free analysis of biospecific interactions in array formats. Biosensors Bioelectronics 22 (2007) 3174-3181
    • (2007) Biosensors Bioelectronics , vol.22 , pp. 3174-3181
    • Dahint, R.1    Trileva, E.2    Acunmana, H.3    Konrad, U.4    Zimmera, M.5    Stadler, V.6
  • 39
    • 45649083830 scopus 로고    scopus 로고
    • An amperometric immunosensor with a thiolated Protein G scaffold
    • Fowler J.M., Stuart M.C., and Wong D.K.Y. An amperometric immunosensor with a thiolated Protein G scaffold. Electrochem Commun 10 (2008) 1020-1023
    • (2008) Electrochem Commun , vol.10 , pp. 1020-1023
    • Fowler, J.M.1    Stuart, M.C.2    Wong, D.K.Y.3
  • 40
    • 38449096649 scopus 로고    scopus 로고
    • A hydrogen peroxide biosensor based on peroxidase activity of hemoglobin in polymeric film
    • Kafi A.K., Lee D.Y., Park S.H., and Kwon Y.S. A hydrogen peroxide biosensor based on peroxidase activity of hemoglobin in polymeric film. J Nanosci Nanotechnol 7 (2007) 4005-4008
    • (2007) J Nanosci Nanotechnol , vol.7 , pp. 4005-4008
    • Kafi, A.K.1    Lee, D.Y.2    Park, S.H.3    Kwon, Y.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.