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Volumn 6, Issue 5, 2010, Pages 612-620

Transdermal delivery enhanced by antimicrobial peptides

Author keywords

Antimicrobial pore forming peptide; Chemical enhancer; Magainin peptide; Skin; Transdermal drug delivery

Indexed keywords

ANTIMICROBIAL PEPTIDE; ANTIMICROBIAL PORE-FORMING PEPTIDE; CHEMICAL ENHANCER; HELICAL STRUCTURES; MAGAININ; N-LAUROYL SARCOSINE; OPTIMAL STRUCTURES; PEPTIDE STRUCTURES; SKIN PERMEABILITY; SKIN PERMEATION; STRATUM CORNEUM LIPIDS; TRANSDERMAL DELIVERY; TRANSDERMAL DRUG DELIVERY;

EID: 79953146084     PISSN: 15507033     EISSN: 15507041     Source Type: Journal    
DOI: 10.1166/jbn.2010.1158     Document Type: Article
Times cited : (25)

References (46)
  • 3
    • 39549117992 scopus 로고    scopus 로고
    • Synergistic enhancement of skin permeability by N-lauroyl sarcosine and ethanol
    • Y. C. Kim, J. H. Park, P. J. Ludovice, and M. R. Prausnitz. Synergistic enhancement of skin permeability by N-lauroyl sarcosine and ethanol. Int. J. Pharm. 352, 129 (2008).
    • (2008) Int. J. Pharm. , vol.352 , pp. 129
    • Kim, Y.C.1    Park, J.H.2    Ludovice, P.J.3    Prausnitz, M.R.4
  • 7
    • 34548640798 scopus 로고    scopus 로고
    • Transdermal delivery enhanced by magainin pore-forming peptide
    • Y. C. Kim, P. J. Ludovice, and M. R. Prausnitz, Transdermal delivery enhanced by magainin pore-forming peptide. J. Control. Release 122, 375 (2007).
    • (2007) J. Control. Release , vol.122 , pp. 375
    • Kim, Y.C.1    Ludovice, P.J.2    Prausnitz, M.R.3
  • 8
    • 50249085100 scopus 로고    scopus 로고
    • Biochemical enhancement of transdermal delivery with magainin peptide: Modification of electrostatic interactions by changing pH
    • Y. C. Kim, S. Late, A. K. Banga, P. J. Ludovice, and M. R. Prausnitz, Biochemical enhancement of transdermal delivery with magainin peptide: Modification of electrostatic interactions by changing pH. Int. J. Pharm. 362, 20 (2008).
    • (2008) Int. J. Pharm. , vol.362 , pp. 20
    • Kim, Y.C.1    Late, S.2    Banga, A.K.3    Ludovice, P.J.4    Prausnitz, M.R.5
  • 9
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin-2, across lipid bilayers by forming a pore
    • K. Matsuzaki, O. Murase, N. Fujii, and K. Miyajima. Translocation of a channel-forming antimicrobial peptide, magainin-2, across lipid bilayers by forming a pore. Biochemistry 34, 6521 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6521
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 10
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • A. Tossi, L. Sandri, and A. Giangaspero, Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55, 4 (2000).
    • (2000) Biopolymers , vol.55 , pp. 4
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 11
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff, Antimicrobial peptides of multicellular organisms. Nature 415, 389 (2002).
    • (2002) Nature , vol.415 , pp. 389
    • Zasloff, M.1
  • 14
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R. M. Epand and H. J. Vogel, Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462, 11 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11
    • Epand, R.M.1    Vogel, H.J.2
  • 16
    • 0013812406 scopus 로고
    • Mechanism of percutaneous adsorption. I. Routes of penetration and influence of solubility
    • R. Scheuplein, Mechanism of percutaneous adsorption. I. Routes of penetration and influence of solubility. J. Invest. Dermatol. 45, 334 (1965).
    • (1965) J. Invest. Dermatol. , vol.45 , pp. 334
    • Scheuplein, R.1
  • 17
    • 0035003716 scopus 로고    scopus 로고
    • Final report on the safety assessment of cocoyl sarcosine, lauroyl sarcosine, myristoyl sarcosine, oleoyl sarcosine, stearoyl sarcosine, sodium cocoyl sarcosinate, sodium lauroyl sarcosinate, sodium myristoyl sarcosinate, ammonium cocoyl sarcosinate
    • R. S. Lanigan, Final report on the safety assessment of cocoyl sarcosine, lauroyl sarcosine, myristoyl sarcosine, oleoyl sarcosine, stearoyl sarcosine, sodium cocoyl sarcosinate, sodium lauroyl sarcosinate, sodium myristoyl sarcosinate, ammonium cocoyl sarcosinate. Int. J. Toxicol. 20, 1 (2001).
    • (2001) Int. J. Toxicol. , vol.20 , pp. 1
    • Lanigan, R.S.1
  • 18
    • 0029015468 scopus 로고
    • Effect of vitamin-E on keratinocyte-modulation induced by lauroylsarcosine
    • T. Shimizu, A. Aioi, T. Horiguchi, and K. Kuriyama. Effect of vitamin-E on keratinocyte-modulation induced by lauroylsarcosine. Jap. J. Pharmacol. 67, 291 (1995).
    • (1995) Jap. J. Pharmacol. , vol.67 , pp. 291
    • Shimizu, T.1    Aioi, A.2    Horiguchi, T.3    Kuriyama, K.4
  • 20
    • 0028810329 scopus 로고
    • Fourier-transform raman-spectroscopy of interactions between the penetration enhancer dimethyl-sulfoxide and human stratum-corneum
    • A. N. C. Anigbogu, A. C. Williams, B. W. Barry, and H. G. M. Edwards, Fourier-transform raman-spectroscopy of interactions between the penetration enhancer dimethyl-sulfoxide and human stratum-corneum. Int. J. Pharm. 125, 265 (1995).
    • (1995) Int. J. Pharm. , vol.125 , pp. 265
    • Anigbogu, A.N.C.1    Williams, A.C.2    Barry, B.W.3    Edwards, H.G.M.4
  • 21
    • 0029585859 scopus 로고
    • Mechanism of oleic acid-induced skin penetration enhancement in vivo in humans
    • A. Naik, L. Pechtold, R. O. Potts, and R. H. Guy, Mechanism of oleic acid-induced skin penetration enhancement in vivo in humans. J. Control. Release 37, 299 (1995).
    • (1995) J. Control. Release , vol.37 , pp. 299
    • Naik, A.1    Pechtold, L.2    Potts, R.O.3    Guy, R.H.4
  • 22
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    • M. Dathe, T. Wieprecht, H. Nikolenko, L. Handel, W. L. Maloy, D. L. MacDonald, M. Beyermann, and M. Bienert, Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Letters 403, 208 (1997).
    • (1997) FEBS Letters , vol.403 , pp. 208
    • Dathe, M.1    Wieprecht, T.2    Nikolenko, H.3    Handel, L.4    Maloy, W.L.5    MacDonald, D.L.6    Beyermann, M.7    Bienert, M.8
  • 23
    • 43449101880 scopus 로고    scopus 로고
    • Optimization of transdermal delivery using magainin pore-forming peptide
    • Y. C. Kim, P. J. Ludovice, and M. R. Prausnitz, Optimization of transdermal delivery using magainin pore-forming peptide. J. Phys. Chem. Solids 69, 1560 (2008).
    • (2008) J. Phys. Chem. Solids , vol.69 , pp. 1560
    • Kim, Y.C.1    Ludovice, P.J.2    Prausnitz, M.R.3
  • 24
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • T. Tachi, R. F. Epand, R. M. Epand, and K. Matsuzaki, Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry 41, 10723 (2002).
    • (2002) Biochemistry , vol.41 , pp. 10723
    • Tachi, T.1    Epand, R.F.2    Epand, R.M.3    Matsuzaki, K.4
  • 25
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from xenopus skin - Isolation, characterization of 2 active forms, and partial cDNA sequence of a precursor
    • M. Zasloff, Magainins, a class of antimicrobial peptides from xenopus skin - Isolation, characterization of 2 active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449
    • Zasloff, M.1
  • 26
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • M. Dathe, H. Nikolenko, J. Meyer, M. Beyermann, and M. Bienert, Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Letters 501, 146 (2001).
    • (2001) FEBS Letters , vol.501 , pp. 146
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 27
    • 0023735907 scopus 로고
    • Synthetic magainin analogs with improved antimicrobial activity
    • H. C. Chen, J. H. Brown, J. L. Morell, and C. M. Huang, Synthetic magainin analogs with improved antimicrobial activity. FEBS Letters 236, 462 (1988).
    • (1988) FEBS Letters , vol.236 , pp. 462
    • Chen, H.C.1    Brown, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 28
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • T. Wieprecht, M. Dathe, M. Beyermann, E. Krause, W. L. Maloy, D. L. MacDonald, and M. Bienert, Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 36, 6124 (1997).
    • (1997) Biochemistry , vol.36 , pp. 6124
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 29
  • 32
    • 0028950911 scopus 로고
    • The antimicrobial activity of hexapeptides derived from synthetic combinatorial libraries
    • S. E. Blondelle, E. Takahashi, K. T. Dinh, and R. A. Houghten, The antimicrobial activity of hexapeptides derived from synthetic combinatorial libraries. J. Appl. Bacteriol. 78, 39 (1995).
    • (1995) J. Appl. Bacteriol. , vol.78 , pp. 39
    • Blondelle, S.E.1    Takahashi, E.2    Dinh, K.T.3    Houghten, R.A.4
  • 33
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
    • P. Fehlbaum, P. Bulet, S. Chernysh, J. P. Briand, J. P. Roussel, L. Letellier, C. Hetru, and J. A. Hoffmann, Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. USA 93, 1221 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1221
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3    Briand, J.P.4    Roussel, J.P.5    Letellier, L.6    Hetru, C.7    Hoffmann, J.A.8
  • 34
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe-crab hemocytes, tachyplesin II, and polyphemusin I and polyphemusin II - Chemical structures and biological activity
    • T. Miyata, F. Tokunaga, T. Yoneya, K. Yoshikawa, S. Iwanaga, M. Niwa, T. Takao, and Y. Shimonishi, Antimicrobial peptides, isolated from horseshoe-crab hemocytes, tachyplesin II, and polyphemusin I and polyphemusin II - Chemical structures and biological activity. J. Biochem. 106, 663 (1989).
    • (1989) J. Biochem. , vol.106 , pp. 663
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 35
    • 0031567605 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
    • C. B. Park, J. H. Lee, I. Y. Park, M. S. Kim, and S. C. Kim, A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus. FEBS Letters 411, 173 (1997).
    • (1997) FEBS Letters , vol.411 , pp. 173
    • Park, C.B.1    Lee, J.H.2    Park, I.Y.3    Kim, M.S.4    Kim, S.C.5
  • 36
    • 0034613057 scopus 로고    scopus 로고
    • The antennapedia peptide penetratin translocates across lipid bilayers - The first direct observation
    • P. E. G. Thoren, D. Persson, M. Karlsson, and B. Norden, The antennapedia peptide penetratin translocates across lipid bilayers - The first direct observation. FEBS Letters 482, 265 (2000).
    • (2000) FEBS Letters , vol.482 , pp. 265
    • Thoren, P.E.G.1    Persson, D.2    Karlsson, M.3    Norden, B.4
  • 37
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus-tridentatus) - Isolation and chemical structure
    • T. Nakamura, H. Furunaka, T. Miyata, F. Tokunaga, T. Muta, S. Iwanaga, M. Niwa, T. Takao, and Y. Shimonishi, Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus-tridentatus) - Isolation and chemical structure. J. Biol. Chem. 263, 16709 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 42
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • M. Frohm, B. Agerberth, G. Ahangari, M. StahleBackdahl, S. Liden, H. Wigzell, and G. H. Gudmundsson, The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272, 15258 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    StahleBackdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 45
    • 0028177259 scopus 로고
    • The amphipathic alpha-helix concept - Application to the de-novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin
    • I. Cornut, K. Buttner, J. L. Dasseux, and J. Dufourcq, The amphipathic alpha-helix concept - Application to the de-novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin. FEBS Letters 349, 29 (1994).
    • (1994) FEBS Letters , vol.349 , pp. 29
    • Cornut, I.1    Buttner, K.2    Dasseux, J.L.3    Dufourcq, J.4
  • 46
    • 0020479123 scopus 로고
    • The structure of melittin. II. Interpretation of the structure
    • T. C. Terwilliger and D. Eisenberg, The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 257, 6016 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016
    • Terwilliger, T.C.1    Eisenberg, D.2


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