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Volumn 20, Issue 1, 2015, Pages 1210-1227

Pro-moieties of antimicrobial peptide prodrugs

Author keywords

Antibody; Antimicrobial; Charge; PEG; Peptides; Prodrug

Indexed keywords

ANTIINFECTIVE AGENT; PEPTIDE; PRODRUG;

EID: 84921691389     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules20011210     Document Type: Review
Times cited : (38)

References (65)
  • 1
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R.E.; Sahl, H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24, 1551-1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock, R.E. Cationic peptides: Effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 2001, 1, 156-164.
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 0030048076 scopus 로고    scopus 로고
    • Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica
    • Brogden, K.A.; de Lucca, A.J.; Bland, J.; Elliott, S. Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica. Proc. Natl. Acad. Sci. USA 1996, 93, 412-416.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 412-416
    • Brogden, K.A.1    De Lucca, A.J.2    Bland, J.3    Elliott, S.4
  • 5
    • 0036842381 scopus 로고    scopus 로고
    • Antimicrobial peptides from animals: Focus on invertebrates
    • Vizioli, J.; Salzet, M. Antimicrobial peptides from animals: Focus on invertebrates. Trends Pharmacol. Sci. 2002, 23, 494-496.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 494-496
    • Vizioli, J.1    Salzet, M.2
  • 6
    • 0037016020 scopus 로고    scopus 로고
    • Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7
    • Sadler, K.; Eom, K.D.; Yang, J.L.; Dimitrova, Y.; Tam, J.P. Translocating proline-rich peptides from the antimicrobial peptide bactenecin 7. Biochemistry 2002, 41, 14150-14157.
    • (2002) Biochemistry , vol.41 , pp. 14150-14157
    • Sadler, K.1    Eom, K.D.2    Yang, J.L.3    Dimitrova, Y.4    Tam, J.P.5
  • 8
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • Yeaman, M.R.; Bayer, A.S.; Koo, S.P.; Foss, W.; Sullam, P.M. Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action. J. Clin. Investig. 1998, 101, 178-187.
    • (1998) J. Clin. Investig. , vol.101 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.P.3    Foss, W.4    Sullam, P.M.5
  • 9
    • 80053184140 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in preventing multidrug-resistant bacterial infections and biofilm formation
    • Park, S.C.; Park, Y.; Hahm, K.S. The role of antimicrobial peptides in preventing multidrug-resistant bacterial infections and biofilm formation. Int. J. Mol. Sci. 2011, 12, 5971-5992.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 5971-5992
    • Park, S.C.1    Park, Y.2    Hahm, K.S.3
  • 13
    • 84874221218 scopus 로고    scopus 로고
    • Targeted antimicrobial peptides
    • Devocelle, M. Targeted antimicrobial peptides. Front. Immunol. 2012, 3, 309.
    • (2012) Front. Immunol. , vol.3 , pp. 309
    • Devocelle, M.1
  • 14
    • 84921676971 scopus 로고    scopus 로고
    • Eds.; Cambridge University Press: New York, NY, USA
    • Mammalian Host Defence Peptides; Hancock, R., Devine, D., Eds.; Cambridge University Press: New York, NY, USA, 2004; pp. 39-68.
    • (2004) Mammalian Host Defence Peptides , pp. 39-68
    • Hancock, R.1    Devine, D.2
  • 15
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel, A.; Sahl, H.G. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 2006, 4, 529-536.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 16
    • 2942670459 scopus 로고    scopus 로고
    • Can innate immunity be enhanced to treat microbial infections?
    • Finlay, B.B.; Hancock, R.E. Can innate immunity be enhanced to treat microbial infections? Nat. Rev. Microbiol. 2004, 2, 497-504.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 497-504
    • Finlay, B.B.1    Hancock, R.E.2
  • 17
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • Vandamme, D.; Landuyt, B.; Luyten, W.; Schoofs, L. A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell. Immunol. 2012, 280, 22-35.
    • (2012) Cell. Immunol. , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 18
    • 84856460625 scopus 로고    scopus 로고
    • Therapeutic potential of host defense peptides in antibiotic-resistant infections
    • Afacan, N.J.; Yeung, A.T.; Pena, O.M.; Hancock, R.E. Therapeutic potential of host defense peptides in antibiotic-resistant infections. Curr. Pharm. Des. 2012, 18, 807-819.
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 807-819
    • Afacan, N.J.1    Yeung, A.T.2    Pena, O.M.3    Hancock, R.E.4
  • 19
    • 84855865471 scopus 로고    scopus 로고
    • Emerging themes and therapeutic prospects for anti-infective peptides
    • Yount, N.Y.; Yeaman, M.R. Emerging themes and therapeutic prospects for anti-infective peptides. Annu. Rev. Pharmacol. Toxicol. 2012, 52, 337-360.
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 337-360
    • Yount, N.Y.1    Yeaman, M.R.2
  • 21
    • 68949117860 scopus 로고    scopus 로고
    • LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline
    • Bergsson, G.; Reeves, E.P.; McNally, P.; Chotirmall, S.H.; Greene, C.M.; Greally, P.; Murphy, P.; O'Neill, S.J.; McElvaney, N.G. LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline. J. Immunol. 2009, 183, 543-551.
    • (2009) J. Immunol. , vol.183 , pp. 543-551
    • Bergsson, G.1    Reeves, E.P.2    McNally, P.3    Chotirmall, S.H.4    Greene, C.M.5    Greally, P.6    Murphy, P.7    O'Neill, S.J.8    McElvaney, N.G.9
  • 22
    • 84863994637 scopus 로고    scopus 로고
    • Beyond conventional antibiotics for the future treatment of methicillin-resistant Staphylococcus aureus infections: Two novel alternatives
    • Fitzgerald-Hughes, D.; Devocelle, M.; Humphreys, H. Beyond conventional antibiotics for the future treatment of methicillin-resistant Staphylococcus aureus infections: Two novel alternatives. FEMS Immunol. Med. Microbiol. 2012, 65, 399-412.
    • (2012) FEMS Immunol. Med. Microbiol. , vol.65 , pp. 399-412
    • Fitzgerald-Hughes, D.1    Devocelle, M.2    Humphreys, H.3
  • 23
    • 79960950287 scopus 로고    scopus 로고
    • Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches
    • Giuliani, A.; Rinaldi, A.C. Beyond natural antimicrobial peptides: Multimeric peptides and other peptidomimetic approaches. Cell. Mol. Life Sci. 2011, 68, 2255-2266.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2255-2266
    • Giuliani, A.1    Rinaldi, A.C.2
  • 24
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: An overview of a promising class of therapeutics
    • Giuliani, A.; Pirri, G.; Nicoletto, S. Antimicrobial peptides: An overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2007, 2, 1-33.
    • (2007) Cent. Eur. J. Biol. , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.3
  • 25
    • 0034727645 scopus 로고    scopus 로고
    • Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers
    • Zhang, L.; Scott, M.G.; Yan, H.; Mayer, L.D.; Hancock, R.E. Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers. Biochemistry 2000, 39, 14504-14514.
    • (2000) Biochemistry , vol.39 , pp. 14504-14514
    • Zhang, L.1    Scott, M.G.2    Yan, H.3    Mayer, L.D.4    Hancock, R.E.5
  • 28
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen, O.E.; Follin, P.; Johnsen, A.H.; Calafat, J.; Tjabringa, G.S.; Hiemstra, P.S.; Borregaard, N. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001, 97, 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 29
    • 84883311713 scopus 로고    scopus 로고
    • Sensitization of Gram-negative bacteria by targeting the membrane potential
    • Goldberg, K.; Sarig, H.; Zaknoon, F.; Epand, R.F.; Epand, R.M.; Mor, A. Sensitization of Gram-negative bacteria by targeting the membrane potential. FASEB J. 2013, 27, 3818-3826.
    • (2013) FASEB J. , vol.27 , pp. 3818-3826
    • Goldberg, K.1    Sarig, H.2    Zaknoon, F.3    Epand, R.F.4    Epand, R.M.5    Mor, A.6
  • 30
    • 17644389620 scopus 로고    scopus 로고
    • Colistin: The revival of polymyxins for the management of multidrug-resistant Gram-negative bacterial infections
    • Falagas, M.E.; Kasiakou, S.K. Colistin: The revival of polymyxins for the management of multidrug-resistant Gram-negative bacterial infections. Clin. Infect. Dis. 2005, 40, 1333-1341.
    • (2005) Clin. Infect. Dis. , vol.40 , pp. 1333-1341
    • Falagas, M.E.1    Kasiakou, S.K.2
  • 31
    • 84878293341 scopus 로고    scopus 로고
    • Pharmacology of polymyxins: New insights into an 'old' class of antibiotics
    • Velkov, T.; Roberts, K.D.; Nation, R.L.; Thompson, P.E.; Li, J. Pharmacology of polymyxins: New insights into an 'old' class of antibiotics. Future Microbiol. 2013, 8, 711-724.
    • (2013) Future Microbiol. , vol.8 , pp. 711-724
    • Velkov, T.1    Roberts, K.D.2    Nation, R.L.3    Thompson, P.E.4    Li, J.5
  • 32
    • 84877877188 scopus 로고    scopus 로고
    • Inhaled antibiotics for the treatment of chronic bronchopulmonary Pseudomonas aeruginosa infection in cystic fibrosis: Systematic review of randomised controlled trials
    • Maiz, L.; Giron, R.M.; Olveira, C.; Quintana, E.; Lamas, A.; Pastor, D.; Canton, R.; Mensa, J. Inhaled antibiotics for the treatment of chronic bronchopulmonary Pseudomonas aeruginosa infection in cystic fibrosis: Systematic review of randomised controlled trials. Expert Opin. Pharmacother. 2013, doi:10.1517/14656566.2013.790366.
    • (2013) Expert Opin. Pharmacother.
    • Maiz, L.1    Giron, R.M.2    Olveira, C.3    Quintana, E.4    Lamas, A.5    Pastor, D.6    Canton, R.7    Mensa, J.8
  • 33
    • 84862523978 scopus 로고    scopus 로고
    • Challenges with current inhaled treatments for chronic Pseudomonas aeruginosa infection in patients with cystic fibrosis
    • Greally, P.; Whitaker, P.; Peckham, D. Challenges with current inhaled treatments for chronic Pseudomonas aeruginosa infection in patients with cystic fibrosis. Curr. Med. Res. Opin. 2012, 28, 1059-1067.
    • (2012) Curr. Med. Res. Opin. , vol.28 , pp. 1059-1067
    • Greally, P.1    Whitaker, P.2    Peckham, D.3
  • 34
    • 33744454666 scopus 로고    scopus 로고
    • Colistin methanesulfonate is an inactive prodrug of colistin against Pseudomonas aeruginosa
    • Bergen, P.J.; Li, J.; Rayner, C.R.; Nation, R.L. Colistin methanesulfonate is an inactive prodrug of colistin against Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 2006, 50, 1953-1958.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1953-1958
    • Bergen, P.J.1    Li, J.2    Rayner, C.R.3    Nation, R.L.4
  • 36
    • 0035118424 scopus 로고    scopus 로고
    • In vitro pharmacodynamic properties of colistin and colistin methanesulfonate against Pseudomonas aeruginosa isolates from patients with cystic fibrosis
    • Li, J.; Turnidge, J.; Milne, R.; Nation, R.L.; Coulthard, K. In vitro pharmacodynamic properties of colistin and colistin methanesulfonate against Pseudomonas aeruginosa isolates from patients with cystic fibrosis. Antimicrob. Agents Chemother. 2001, 45, 781-785.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 781-785
    • Li, J.1    Turnidge, J.2    Milne, R.3    Nation, R.L.4    Coulthard, K.5
  • 39
    • 84893519181 scopus 로고    scopus 로고
    • Potential of host defense peptide prodrugs as neutrophil elastase-dependent anti-infective agents for cystic fibrosis
    • Forde, E.; Humphreys, H.; Greene, C.M.; Fitzgerald-Hughes, D.; Devocelle, M. Potential of host defense peptide prodrugs as neutrophil elastase-dependent anti-infective agents for cystic fibrosis. Antimicrob. Agents Chemother. 2014, 58, 978-985.
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 978-985
    • Forde, E.1    Humphreys, H.2    Greene, C.M.3    Fitzgerald-Hughes, D.4    Devocelle, M.5
  • 40
    • 79955466299 scopus 로고    scopus 로고
    • Enhancement of the cancer targeting specificity of buforin IIb by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker
    • Jang, J.H.; Kim, M.Y.; Lee, J.W.; Kim, S.C.; Cho, J.H. Enhancement of the cancer targeting specificity of buforin IIb by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker. Peptides 2011, 32, 895-899.
    • (2011) Peptides , vol.32 , pp. 895-899
    • Jang, J.H.1    Kim, M.Y.2    Lee, J.W.3    Kim, S.C.4    Cho, J.H.5
  • 41
    • 0035884376 scopus 로고    scopus 로고
    • In vitro targeted killing of prostate tumor cells by a synthetic amoebapore helix 3 peptide modified with two gamma-linked glutamate residues at the COOH terminus
    • Warren, P.; Li, L.; Song, W.; Holle, E.; Wei, Y.; Wagner, T.; Yu, X. In vitro targeted killing of prostate tumor cells by a synthetic amoebapore helix 3 peptide modified with two gamma-linked glutamate residues at the COOH terminus. Cancer Res. 2001, 61, 6783-6787.
    • (2001) Cancer Res. , vol.61 , pp. 6783-6787
    • Warren, P.1    Li, L.2    Song, W.3    Holle, E.4    Wei, Y.5    Wagner, T.6    Yu, X.7
  • 42
    • 69249093854 scopus 로고    scopus 로고
    • In vivo targeted killing of prostate tumor cells by a synthetic amoebapore helix 3 peptide modified with two gamma-linked glutamate residues at the COOH terminus
    • Holle, L.; Song, W.; Holle, E.; Nilsson, J.; Wei, Y.; Li, J.; Wagner, T.E.; Yu, X. In vivo targeted killing of prostate tumor cells by a synthetic amoebapore helix 3 peptide modified with two gamma-linked glutamate residues at the COOH terminus. Mol. Med. Rep. 2009, 2, 399-403.
    • (2009) Mol. Med. Rep. , vol.2 , pp. 399-403
    • Holle, L.1    Song, W.2    Holle, E.3    Nilsson, J.4    Wei, Y.5    Li, J.6    Wagner, T.E.7    Yu, X.8
  • 43
    • 84875969630 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-prodrug conjugates: Concept, design, and applications
    • Banerjee, S.S.; Aher, N.; Patil, R.; Khandare, J. Poly(ethylene glycol)-prodrug conjugates: Concept, design, and applications. J. Drug Deliv. 2012, 2012, doi:10.1155/2012/103973.
    • (2012) J. Drug Deliv. , vol.2012
    • Banerjee, S.S.1    Aher, N.2    Patil, R.3    Khandare, J.4
  • 44
    • 33747840618 scopus 로고    scopus 로고
    • Polymer conjugates as anticancer nanomedicines
    • Duncan, R. Polymer conjugates as anticancer nanomedicines. Nat. Rev. Cancer 2006, 6, 688-701.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 688-701
    • Duncan, R.1
  • 45
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris, J.M.; Chess, R.B. Effect of PEGylation on pharmaceuticals. Nat. Rev. Drug Discov. 2003, 2, 214-221.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 46
    • 0344063545 scopus 로고    scopus 로고
    • Polyacetal-doxorubicin conjugates designed for pH-dependent degradation
    • Tomlinson, R.; Heller, J.; Brocchini, S.; Duncan, R. Polyacetal-doxorubicin conjugates designed for pH-dependent degradation. Bioconjugate Chem. 2003, 14, 1096-1106.
    • (2003) Bioconjugate Chem. , vol.14 , pp. 1096-1106
    • Tomlinson, R.1    Heller, J.2    Brocchini, S.3    Duncan, R.4
  • 47
    • 20844460357 scopus 로고    scopus 로고
    • PEG-doxorubicin conjugates: Influence of polymer structure on drug release, in vitro cytotoxicity, biodistribution, and antitumor activity
    • Veronese, F.M.; Schiavon, O.; Pasut, G.; Mendichi, R.; Andersson, L.; Tsirk, A.; Ford, J.; Wu, G.; Kneller, S.; Davies, J.; et al. PEG-doxorubicin conjugates: Influence of polymer structure on drug release, in vitro cytotoxicity, biodistribution, and antitumor activity. Bioconjugate Chem. 2005, 16, 775-784.
    • (2005) Bioconjugate Chem. , vol.16 , pp. 775-784
    • Veronese, F.M.1    Schiavon, O.2    Pasut, G.3    Mendichi, R.4    Andersson, L.5    Tsirk, A.6    Ford, J.7    Wu, G.8    Kneller, S.9    Davies, J.10
  • 48
    • 0023141221 scopus 로고
    • Anticancer agents coupled to N-(2-hydroxypropyl)methacrylamide copolymers. I. Evaluation of daunomycin and puromycin conjugates in vitro
    • Duncan, R.; Kopeckova-Rejmanova, P.; Strohalm, J.; Hume, I.; Cable, H.C.; Pohl, J.; Lloyd, J.B.; Kopecek, J. Anticancer agents coupled to N-(2-hydroxypropyl)methacrylamide copolymers. I. Evaluation of daunomycin and puromycin conjugates in vitro. Br. J. Cancer 1987, 55, 165-174.
    • (1987) Br. J. Cancer , vol.55 , pp. 165-174
    • Duncan, R.1    Kopeckova-Rejmanova, P.2    Strohalm, J.3    Hume, I.4    Cable, H.C.5    Pohl, J.6    Lloyd, J.B.7    Kopecek, J.8
  • 49
    • 0037458920 scopus 로고    scopus 로고
    • Hpma copolymers with pH-controlled release of doxorubicin: In vitro cytotoxicity and in vivo antitumor activity
    • Ulbrich, K.; Etrych, T.; Chytil, P.; Jelinkova, M.; Rihova, B. Hpma copolymers with pH-controlled release of doxorubicin: In vitro cytotoxicity and in vivo antitumor activity. J. Control. Release 2003, 87, 33-47.
    • (2003) J. Control. Release , vol.87 , pp. 33-47
    • Ulbrich, K.1    Etrych, T.2    Chytil, P.3    Jelinkova, M.4    Rihova, B.5
  • 51
    • 34948886156 scopus 로고    scopus 로고
    • Action mechanism of PEGylated magainin 2 analogue peptide
    • Imura, Y.; Nishida, M.; Matsuzaki, K. Action mechanism of PEGylated magainin 2 analogue peptide. Biochim. Biophys. Acta 2007, 1768, 2578-2585.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2578-2585
    • Imura, Y.1    Nishida, M.2    Matsuzaki, K.3
  • 52
    • 84898652791 scopus 로고    scopus 로고
    • Effects of PEGylation on membrane and lipopolysaccharide interactions of host defense peptides
    • Singh, S.; Papareddy, P.; Morgelin, M.; Schmidtchen, A.; Malmsten, M. Effects of PEGylation on membrane and lipopolysaccharide interactions of host defense peptides. Biomacromolecules 2014, 15, 1337-1345.
    • (2014) Biomacromolecules , vol.15 , pp. 1337-1345
    • Singh, S.1    Papareddy, P.2    Morgelin, M.3    Schmidtchen, A.4    Malmsten, M.5
  • 53
    • 84861133663 scopus 로고    scopus 로고
    • PEGylation of antimicrobial peptides maintains the active peptide conformation, model membrane interactions, and antimicrobial activity while improving lung tissue biocompatibility following airway delivery
    • Morris, C.J.; Beck, K.; Fox, M.A.; Ulaeto, D.; Clark, G.C.; Gumbleton, M. PEGylation of antimicrobial peptides maintains the active peptide conformation, model membrane interactions, and antimicrobial activity while improving lung tissue biocompatibility following airway delivery. Antimicrob. Agents Chemother. 2012, 56, 3298-3308.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 3298-3308
    • Morris, C.J.1    Beck, K.2    Fox, M.A.3    Ulaeto, D.4    Clark, G.C.5    Gumbleton, M.6
  • 54
    • 57749180588 scopus 로고    scopus 로고
    • Modification of antimicrobial peptide with low molar mass poly(ethylene glycol)
    • Zhang, G.; Han, B.; Lin, X.; Wu, X.; Yan, H. Modification of antimicrobial peptide with low molar mass poly(ethylene glycol). J. Biochem. 2008, 144, 781-788.
    • (2008) J. Biochem. , vol.144 , pp. 781-788
    • Zhang, G.1    Han, B.2    Lin, X.3    Wu, X.4    Yan, H.5
  • 55
    • 84880124033 scopus 로고    scopus 로고
    • Controlled systemic release of therapeutic peptides from PEGylated prodrugs by serum proteases
    • Nollmann, F.I.; Goldbach, T.; Berthold, N.; Hoffmann, R. Controlled systemic release of therapeutic peptides from PEGylated prodrugs by serum proteases. Angew. Chem. Int. Ed. Engl. 2013, 52, 7597-7599.
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 7597-7599
    • Nollmann, F.I.1    Goldbach, T.2    Berthold, N.3    Hoffmann, R.4
  • 58
    • 33746141286 scopus 로고    scopus 로고
    • Design of a peptibody consisting of the antimicrobial peptide dhvar5 and a llama variable heavy-chain antibody fragment
    • Szynol, A.; de Haard, J.J.; Veerman, E.C.; de Soet, J.J.; van Nieuw Amerongen, A.V. Design of a peptibody consisting of the antimicrobial peptide dhvar5 and a llama variable heavy-chain antibody fragment. Chem. Biol. Drug Des. 2006, 67, 425-431.
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 425-431
    • Szynol, A.1    De Haard, J.J.2    Veerman, E.C.3    De Soet, J.J.4    Van Nieuw Amerongen, A.V.5
  • 59
    • 33750584025 scopus 로고    scopus 로고
    • Targeted killing of Streptococcus mutans by a pheromone-guided "smart" antimicrobial peptide
    • Eckert, R.; He, J.; Yarbrough, D.K.; Qi, F.; Anderson, M.H.; Shi, W. Targeted killing of Streptococcus mutans by a pheromone-guided "smart" antimicrobial peptide. Antimicrob. Agents Chemother. 2006, 50, 3651-3657.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3651-3657
    • Eckert, R.1    He, J.2    Yarbrough, D.K.3    Qi, F.4    Anderson, M.H.5    Shi, W.6
  • 60
    • 10744228928 scopus 로고    scopus 로고
    • An engineered multidomain bactericidal peptide as a model for targeted antibiotics against specific bacteria
    • Qiu, X.Q.; Wang, H.; Lu, X.F.; Zhang, J.; Li, S.F.; Cheng, G.; Wan, L.; Yang, L.; Zuo, J.Y.; Zhou, Y.Q.; et al. An engineered multidomain bactericidal peptide as a model for targeted antibiotics against specific bacteria. Nat. Biotechnol. 2003, 21, 1480-1485.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1480-1485
    • Qiu, X.Q.1    Wang, H.2    Lu, X.F.3    Zhang, J.4    Li, S.F.5    Cheng, G.6    Wan, L.7    Yang, L.8    Zuo, J.Y.9    Zhou, Y.Q.10
  • 61
    • 14744272033 scopus 로고    scopus 로고
    • A novel engineered peptide, a narrow-spectrum antibiotic, is effective against vancomycin-resistant Enterococcus faecalis
    • Qiu, X.Q.; Zhang, J.; Wang, H.; Wu, G.Y. A novel engineered peptide, a narrow-spectrum antibiotic, is effective against vancomycin-resistant Enterococcus faecalis. Antimicrob. Agents Chemother. 2005, 49, 1184-1189.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1184-1189
    • Qiu, X.Q.1    Zhang, J.2    Wang, H.3    Wu, G.Y.4
  • 62
    • 64549112594 scopus 로고    scopus 로고
    • Design and activity of a "dual-targeted" antimicrobial peptide
    • He, J.; Anderson, M.H.; Shi, W.; Eckert, R. Design and activity of a "dual-targeted" antimicrobial peptide. Int. J. Antimicrob. Agents 2009, 33, 532-537.
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 532-537
    • He, J.1    Anderson, M.H.2    Shi, W.3    Eckert, R.4
  • 63
    • 84863097110 scopus 로고    scopus 로고
    • Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides
    • Arnusch, C.J.; Pieters, R.J.; Breukink, E. Enhanced membrane pore formation through high-affinity targeted antimicrobial peptides. PLoS One 2012, 7, e39768.
    • (2012) PLoS One , vol.7 , pp. e39768
    • Arnusch, C.J.1    Pieters, R.J.2    Breukink, E.3
  • 65
    • 82255179791 scopus 로고    scopus 로고
    • Synthesis of mutual azo prodrugs of anti-inflammatory agents and peptides facilitated by alpha-aminoisobutyric acid
    • Kennedy, D.A.; Vembu, N.; Fronczek, F.R.; Devocelle, M. Synthesis of mutual azo prodrugs of anti-inflammatory agents and peptides facilitated by alpha-aminoisobutyric acid. J. Org. Chem. 2011, 76, 9641-9647.
    • (2011) J. Org. Chem. , vol.76 , pp. 9641-9647
    • Kennedy, D.A.1    Vembu, N.2    Fronczek, F.R.3    Devocelle, M.4


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