메뉴 건너뛰기




Volumn 48, Issue 3, 2016, Pages 887-900

Rational modification of a dendrimeric peptide with antimicrobial activity: Consequences on membrane-binding and biological properties

Author keywords

Antimicrobial peptides; Biofilms; Dendrimers; Gram negative; Gram positive; Model membranes

Indexed keywords

DEN SB 056; DEN SB 056 1; DENDRIMER; LIN SB 056; LIN SB 056 1; PEPTIDE DERIVATIVE; PHOSPHATIDYLCHOLINE; SB 056; SODIUM CHLORIDE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 84958125731     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-015-2136-5     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 78751493646 scopus 로고    scopus 로고
    • Use of antimicrobial peptides against microbial biofilms: Advantages and limits
    • 21110801
    • Batoni G, Maisetta G, Brancatisano FL, Esin S, Campa M (2011) Use of antimicrobial peptides against microbial biofilms: advantages and limits. Curr Med Chem 18:256-2579
    • (2011) Curr Med Chem , vol.18 , pp. 256-2579
    • Batoni, G.1    Maisetta, G.2    Brancatisano, F.L.3    Esin, S.4    Campa, M.5
  • 2
    • 84898541314 scopus 로고    scopus 로고
    • Inhibitory effect of the human liver-derived antimicrobial peptide hepcidin 20 on biofilms of polysaccharide intercellular adhesin (PIA)-positive and PIA-negative strains of Staphylococcus epidermidis
    • 24645694
    • Brancatisano FL, Maisetta G, Di Luca M, Esin S, Bottai D, Bizzarri R, Campa M, Batoni G (2014) Inhibitory effect of the human liver-derived antimicrobial peptide hepcidin 20 on biofilms of polysaccharide intercellular adhesin (PIA)-positive and PIA-negative strains of Staphylococcus epidermidis. Biofouling 30:435-446
    • (2014) Biofouling , vol.30 , pp. 435-446
    • Brancatisano, F.L.1    Maisetta, G.2    Di Luca, M.3    Esin, S.4    Bottai, D.5    Bizzarri, R.6    Campa, M.7    Batoni, G.8
  • 3
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane
    • 9188693
    • Breukink E, Van Kraaij C, Demel RA, Siezen RJ, Kuipers OP, De Kruijff B (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    De Kruijff, B.6
  • 4
    • 78249271990 scopus 로고    scopus 로고
    • Synthesis, characterization, antimicrobial activity and LPS-interaction properties of SB041, a novel dendrimeric peptide with antimicrobial properties
    • 20438783
    • Bruschi M, Pirri G, Giuliani A, Nicoletto SF, Baster I, Scorciapino MA, Casu M, Rinaldi AC (2010) Synthesis, characterization, antimicrobial activity and LPS-interaction properties of SB041, a novel dendrimeric peptide with antimicrobial properties. Peptides 31:1459-1467
    • (2010) Peptides , vol.31 , pp. 1459-1467
    • Bruschi, M.1    Pirri, G.2    Giuliani, A.3    Nicoletto, S.F.4    Baster, I.5    Scorciapino, M.A.6    Casu, M.7    Rinaldi, A.C.8
  • 6
    • 79956054931 scopus 로고    scopus 로고
    • Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin
    • 21327963
    • Coccia C, Rinaldi AC, Luca V, Barra D, Bozzi A, Di Giulio A, Veerman EC, Mangoni ML (2011) Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin. Eur Biophys J 40:577-588
    • (2011) Eur Biophys J , vol.40 , pp. 577-588
    • Coccia, C.1    Rinaldi, A.C.2    Luca, V.3    Barra, D.4    Bozzi, A.5    Di Giulio, A.6    Veerman, E.C.7    Mangoni, M.L.8
  • 7
    • 84926176304 scopus 로고    scopus 로고
    • BaAMPs: The database of biofilm-active antimicrobial peptides
    • 25760404
    • Di Luca M, Maccari G, Maisetta G, Batoni G (2015) BaAMPs: the database of biofilm-active antimicrobial peptides. Biofouling 31:193-199
    • (2015) Biofouling , vol.31 , pp. 193-199
    • Di Luca, M.1    Maccari, G.2    Maisetta, G.3    Batoni, G.4
  • 8
    • 69249096200 scopus 로고    scopus 로고
    • The roles of antimicrobial peptides in innate host defense
    • 2750833 19601838
    • Diamond G, Beckloff N, Weinberg A, Kisich KO (2009) The roles of antimicrobial peptides in innate host defense. Curr Pharm Des 15:2377-2392
    • (2009) Curr Pharm Des , vol.15 , pp. 2377-2392
    • Diamond, G.1    Beckloff, N.2    Weinberg, A.3    Kisich, K.O.4
  • 9
    • 65949090768 scopus 로고    scopus 로고
    • Domains in bacterial membranes and the action of antimicrobial agents
    • 19462015
    • Epand RM, Epand RF (2009) Domains in bacterial membranes and the action of antimicrobial agents. Mol BioSyst 5:580-587
    • (2009) Mol BioSyst , vol.5 , pp. 580-587
    • Epand, R.M.1    Epand, R.F.2
  • 10
    • 33645737243 scopus 로고    scopus 로고
    • Membrane lipid composition and the interaction of pardaxin: The role of cholesterol
    • 16454662
    • Epand RF, Ramamoorthy A, Epand RM (2006) Membrane lipid composition and the interaction of pardaxin: the role of cholesterol. Protein Pept Lett 13:1-5
    • (2006) Protein Pept Lett , vol.13 , pp. 1-5
    • Epand, R.F.1    Ramamoorthy, A.2    Epand, R.M.3
  • 11
    • 77950646635 scopus 로고    scopus 로고
    • Design and in vitro evaluation of branched peptide conjugates: Turning nonspecific cytotoxic drugs into tumor-selective agents
    • 20222099
    • Falciani C, Brunetti J, Pagliuca C, Menichetti S, Vitellozzi L, Lelli B, Pini A, Bracci L (2010) Design and in vitro evaluation of branched peptide conjugates: turning nonspecific cytotoxic drugs into tumor-selective agents. ChemMedChem 5:567-574
    • (2010) ChemMedChem , vol.5 , pp. 567-574
    • Falciani, C.1    Brunetti, J.2    Pagliuca, C.3    Menichetti, S.4    Vitellozzi, L.5    Lelli, B.6    Pini, A.7    Bracci, L.8
  • 13
    • 79960950287 scopus 로고    scopus 로고
    • Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches
    • 21598022
    • Giuliani A, Rinaldi AC (2011) Beyond natural antimicrobial peptides: multimeric peptides and other peptidomimetic approaches. Cell Mol Life Sci 68:2255-2266
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2255-2266
    • Giuliani, A.1    Rinaldi, A.C.2
  • 15
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1892) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1892) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 84921523986 scopus 로고    scopus 로고
    • On the antimicrobial activity of various peptide-based dendrimers of similar architecture
    • 25574818
    • Lind TK, Polcyn P, Zielinska P, Cárdenas M, Urbanczyk-Lipkowska Z (2015) On the antimicrobial activity of various peptide-based dendrimers of similar architecture. Molecules 20:738-753
    • (2015) Molecules , vol.20 , pp. 738-753
    • Lind, T.K.1    Polcyn, P.2    Zielinska, P.3    Cárdenas, M.4    Urbanczyk-Lipkowska, Z.5
  • 18
    • 84880320843 scopus 로고    scopus 로고
    • Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa
    • 23503622
    • Luca V, Stringaro A, Colone M, Pini A, Mangoni ML (2013) Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa. Cell Mol Life Sci 70:2773-2786
    • (2013) Cell Mol Life Sci , vol.70 , pp. 2773-2786
    • Luca, V.1    Stringaro, A.2    Colone, M.3    Pini, A.4    Mangoni, M.L.5
  • 19
    • 76949084904 scopus 로고    scopus 로고
    • Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparin sulfate
    • 20083141
    • Luganini A, Giuliani A, Pirri G, Pizzuto L, Landolfo S, Gribaudo G (2010) Peptide-derivatized dendrimers inhibit human cytomegalovirus infection by blocking virus binding to cell surface heparin sulfate. Antiviral Res 85:532-540
    • (2010) Antiviral Res , vol.85 , pp. 532-540
    • Luganini, A.1    Giuliani, A.2    Pirri, G.3    Pizzuto, L.4    Landolfo, S.5    Gribaudo, G.6
  • 20
    • 1042290508 scopus 로고    scopus 로고
    • Functional characterisation of the 1-18 fragment of esculentin-1b, an antimicrobial peptide from Rana esculenta
    • 15019209
    • Mangoni ML, Fiocco D, Mignogna G, Barra D, Simmaco M (2003) Functional characterisation of the 1-18 fragment of esculentin-1b, an antimicrobial peptide from Rana esculenta. Peptides 24:1771-1777
    • (2003) Peptides , vol.24 , pp. 1771-1777
    • Mangoni, M.L.1    Fiocco, D.2    Mignogna, G.3    Barra, D.4    Simmaco, M.5
  • 23
    • 70349238995 scopus 로고    scopus 로고
    • Esculentin-1b(1-18)-a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli
    • 19725877
    • Marcellini L, Borro M, Gentile G, Rinaldi AC, Stella L, Aimola P, Barra D, Mangoni ML (2009) Esculentin-1b(1-18)-a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli. FEBS J 276:5647-5664
    • (2009) FEBS J , vol.276 , pp. 5647-5664
    • Marcellini, L.1    Borro, M.2    Gentile, G.3    Rinaldi, A.C.4    Stella, L.5    Aimola, P.6    Barra, D.7    Mangoni, M.L.8
  • 24
    • 36749025072 scopus 로고    scopus 로고
    • Bad drugs need more drugs
    • Opar A (2007) Bad drugs need more drugs. Nature Rev Drug Discov 6:943-944
    • (2007) Nature Rev Drug Discov , vol.6 , pp. 943-944
    • Opar, A.1
  • 25
    • 84927761581 scopus 로고    scopus 로고
    • Healthcare-associated infections, medical devices and biofilms: Risk, tolerance and control
    • 25670813
    • Percival SL, Suleman L, Vuotto C, Donelli G (2015) Healthcare-associated infections, medical devices and biofilms: risk, tolerance and control. J Med Microbiol 64:323-334
    • (2015) J Med Microbiol , vol.64 , pp. 323-334
    • Percival, S.L.1    Suleman, L.2    Vuotto, C.3    Donelli, G.4
  • 26
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • 16778838
    • Peschel A, Sahl HG (2006) The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat Rev Microbiol 4:529-536
    • (2006) Nat Rev Microbiol , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 28
    • 84879673393 scopus 로고    scopus 로고
    • Novel antimicrobial peptide dendrimers with amphiphilic surface and their interactions with phospholipids - Insights from mass spectrometry
    • 23778121
    • Polcyn P, Zielinska P, Zimnicka M, Troć A, Kalicki P, Solecka J, Laskowska A, Urbanczyk-Lipkowska Z (2013) Novel antimicrobial peptide dendrimers with amphiphilic surface and their interactions with phospholipids - insights from mass spectrometry. Molecules 18:7120-7144
    • (2013) Molecules , vol.18 , pp. 7120-7144
    • Polcyn, P.1    Zielinska, P.2    Zimnicka, M.3    Troć, A.4    Kalicki, P.5    Solecka, J.6    Laskowska, A.7    Urbanczyk-Lipkowska, Z.8
  • 29
    • 67649295450 scopus 로고    scopus 로고
    • Antimicrobial peptide mimics for improved therapeutic properties
    • 19028449
    • Rotem S, Mor A (2009) Antimicrobial peptide mimics for improved therapeutic properties. Biochim Biophys Acta 1788:1582-1592
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1582-1592
    • Rotem, S.1    Mor, A.2
  • 30
    • 0036177932 scopus 로고    scopus 로고
    • Peptide dendrimers: Applications and synthesis
    • Sadler K, Tam JP (2002) Peptide dendrimers: applications and synthesis. Rev Mol Biotechnol 90:195-229
    • (2002) Rev Mol Biotechnol , vol.90 , pp. 195-229
    • Sadler, K.1    Tam, J.P.2
  • 31
    • 84874083043 scopus 로고    scopus 로고
    • Antimicrobial peptidomimetics: Reinterpreting nature to deliver innovative therapeutics
    • Scorciapino MA, Rinaldi AC (2012) Antimicrobial peptidomimetics: reinterpreting nature to deliver innovative therapeutics. Front Immunol 3:1-4
    • (2012) Front Immunol , vol.3 , pp. 1-4
    • Scorciapino, M.A.1    Rinaldi, A.C.2
  • 33
    • 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
  • 34
    • 0016377375 scopus 로고
    • Lipid composition as a guide to the classification of bacteria
    • 4213752
    • Shaw N (1974) Lipid composition as a guide to the classification of bacteria. Adv Appl Microbiol 17:63-108
    • (1974) Adv Appl Microbiol , vol.17 , pp. 63-108
    • Shaw, N.1
  • 35
    • 84911378146 scopus 로고    scopus 로고
    • Combining topology and sequence design for the discovery of potent antimicrobial peptide dendrimers against multidrug-resistant Pseudomonas aeruginosa
    • 25346278
    • Stach M, Siriwardena TN, Köhler T, van Delden C, Darbre T, Reymond JL (2014) Combining topology and sequence design for the discovery of potent antimicrobial peptide dendrimers against multidrug-resistant Pseudomonas aeruginosa. Angew Chem Int Ed Engl 53:12827-12831
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 12827-12831
    • Stach, M.1    Siriwardena, T.N.2    Köhler, T.3    Van Delden, C.4    Darbre, T.5    Reymond, J.L.6
  • 36
    • 0036183822 scopus 로고    scopus 로고
    • Antimicrobial dendrimeric peptides
    • 11846794
    • Tam JP, Lu YA, Yang JL (2002) Antimicrobial dendrimeric peptides. Eur J Biochem 269:923-932
    • (2002) Eur J Biochem , vol.269 , pp. 923-932
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 37
    • 84907736803 scopus 로고    scopus 로고
    • Collective antibiotic resistance: Mechanisms and implications
    • 4367450 25271119
    • Vega NM, Gore J (2014) Collective antibiotic resistance: mechanisms and implications. Curr Opin Microbiol 21:28-34
    • (2014) Curr Opin Microbiol , vol.21 , pp. 28-34
    • Vega, N.M.1    Gore, J.2
  • 38
    • 84892537987 scopus 로고    scopus 로고
    • Defensin-based anti-infective strategies
    • 24119539
    • Wilmes M, Sahl HG (2014) Defensin-based anti-infective strategies. Int J Med Microbiol 304:93-99
    • (2014) Int J Med Microbiol , vol.304 , pp. 93-99
    • Wilmes, M.1    Sahl, H.G.2
  • 39
    • 84901809320 scopus 로고    scopus 로고
    • WHO, Geneva. Accessed 16 Aug 2015
    • World Health Organization (2014) Antimicrobial resistance: global report on surveillance. WHO, Geneva. http://apps.who.int/iris/bitstream/10665/112642/1/9789241564748-eng.pdf?ua=1. Accessed 16 Aug 2015
    • (2014) Antimicrobial Resistance: Global Report on Surveillance
  • 40
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • 23302022
    • Yount NY, Yeaman MR (2013) Peptide antimicrobials: cell wall as a bacterial target. Ann N Y Acad Sci 1277:127-138
    • (2013) Ann N y Acad Sci , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 41
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • 11807545
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 42
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • 11991956
    • Zhao H, Kinnunen PK (2002) Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J Biol Chem 277:25170-25177
    • (2002) J Biol Chem , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.