메뉴 건너뛰기




Volumn 2, Issue 1-2, 2011, Pages 27-38

Antimicrobial peptides from amphibians

Author keywords

amphibian antimicrobial peptides; design strategy; therapeutic applications

Indexed keywords

AMPHIBIA; ANIMALIA; ANURA;

EID: 84929584676     PISSN: 18685021     EISSN: 1868503X     Source Type: Journal    
DOI: 10.1515/bmc.2011.006     Document Type: Review
Times cited : (16)

References (134)
  • 1
    • 0028364262 scopus 로고
    • Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides
    • Simmaco M, Mignogna G, Barra D, Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. J Biol Chem 1994; 269: 11956-61.
    • (1994) J Biol Chem , vol.269 , pp. 11956-11961
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3    Bossa, F.4
  • 3
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: What do they tell us?
    • Simmaco M, Mignogna G, Barra D. Antimicrobial peptides from amphibian skin: what do they tell us? Biopolymers 1999; 47: 435-50.
    • (1999) Biopolymers , vol.47 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 5
    • 0030689711 scopus 로고    scopus 로고
    • The natural history of amphibian skin secretions, their normal functioning and potential medical applications
    • Clarke BT. The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol Rev Camb Philos Soc 1997; 72: 365-79.
    • (1997) Biol Rev Camb Philos Soc , vol.72 , pp. 365-379
    • Clarke, B.T.1
  • 6
    • 0023612372 scopus 로고
    • Further classification of skin alkaloids from neotropical poison frogs (Dendrobatidae), with a general survey of toxic/noxious substances in the Amphibia
    • Daly JW, Myers CW, Whittaker N. Further classification of skin alkaloids from neotropical poison frogs (Dendrobatidae), with a general survey of toxic/noxious substances in the Amphibia. Toxicon 1987; 25: 1023-95.
    • (1987) Toxicon , vol.25 , pp. 1023-1095
    • Daly, J.W.1    Myers, C.W.2    Whittaker, N.3
  • 7
    • 77957097677 scopus 로고
    • Chapter 5: Chemistry and pharmacology
    • Brossi A, editor. New York: Academic Press
    • Witkop B, Gössinger E. Chapter 5: Chemistry and Pharmacology, in: Brossi A, editor. The alkaloids. New York: Academic Press, 1983: 139-251.
    • (1983) The Alkaloids , pp. 139-251
    • Witkop, B.1    Gössinger, E.2
  • 9
    • 67649277612 scopus 로고    scopus 로고
    • The role of amphibian antimicrobial peptides in protection of amphibians from pathogens linked to global amphibian declines
    • Rollins-Smith LA. The role of amphibian antimicrobial peptides in protection of amphibians from pathogens linked to global amphibian declines. Biochim Biophys Acta 2009; 1788: 1593-9.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1593-1599
    • Rollins-Smith, L.A.1
  • 10
    • 0032560497 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and innate immunity
    • Barra D, Simmaco M, Boman HG. Gene-encoded peptide antibiotics and innate immunity. FEBS Lett 1998; 430: 130-4.
    • (1998) FEBS Lett , vol.430 , pp. 130-134
    • Barra, D.1    Simmaco, M.2    Boman, H.G.3
  • 13
    • 0025523974 scopus 로고
    • Expression of MHC class II antigens during Xenopus development
    • Pasquier DL, Flajnik M. Expression of MHC class II antigens during Xenopus development. Dev Immunol 1990; 1: 85-95.
    • (1990) Dev Immunol , vol.1 , pp. 85-95
    • Pasquier, D.L.1    Flajnik, M.2
  • 15
    • 0001637567 scopus 로고
    • Isolation and structure of a haemolytic polypeptide from the defensive secretion of European Bombina species
    • Csordas A, Michl H. Isolation and structure of a haemolytic polypeptide from the defensive secretion of European Bombina species. Monatsh Chem 1970; 101: 182-9.
    • (1970) Monatsh Chem , vol.101 , pp. 182-189
    • Csordas, A.1    Michl, H.2
  • 16
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987; 84: 5449-53.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 17
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff M, Martin B, Chen HC. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc Natl Acad Sci USA 1988; 85: 910-3.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.C.3
  • 20
    • 67649408946 scopus 로고    scopus 로고
    • Bombinins, antimicrobial peptides from Bombina species
    • Simmaco M, Kreil G, Barra D. Bombinins, antimicrobial peptides from Bombina species. Biochim Biophys Acta 2009; 1788: 1551-5.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1551-1555
    • Simmaco, M.1    Kreil, G.2    Barra, D.3
  • 22
    • 0036375765 scopus 로고    scopus 로고
    • An anionic antimicrobial peptide from toad Bombina maxima
    • Lai R, Liu H, Lee WH, Zhang Y. An anionic antimicrobial peptide from toad Bombina maxima. Biochem Biophys Res Commun 2002; 295: 796-9.
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 796-799
    • Lai, R.1    Liu, H.2    Lee, W.H.3    Zhang, Y.4
  • 23
    • 1242306544 scopus 로고    scopus 로고
    • Antimicrobial peptides from ranid frogs: Taxonomic and phylogenetic markers and a potential source of new therapeutic agents
    • Conlon JM, Kolodziejek J, Nowotny N. Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim Biophys Acta 2004; 1696: 1-14.
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 1-14
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3
  • 25
    • 0028009870 scopus 로고
    • Isolation and structure of novel defensive peptides from frog skin
    • Mor A, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. Eur J Biochem 1994; 219: 145-54.
    • (1994) Eur J Biochem , vol.219 , pp. 145-154
    • Mor, A.1    Nicolas, P.2
  • 26
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park CB, Kim MS, Kim SC. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem Biophys Res Commun 1996; 218: 408-13.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 27
    • 0036277312 scopus 로고    scopus 로고
    • Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimicrobial peptides
    • Duda TF Jr, Vanhoye D, Nicolas P. Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimicrobial peptides. Mol Biol Evol 2002; 19: 858-64.
    • (2002) Mol Biol Evol , vol.19 , pp. 858-864
    • Duda, T.F.1    Vanhoye, D.2    Nicolas, P.3
  • 28
    • 34249806711 scopus 로고    scopus 로고
    • Strategies for transformation of naturally-occurring amphibian antimicrobial peptides into therapeutically valuable anti-infective agents
    • Conlon JM, Al-Ghaferi N, Abraham B, Leprince J. Strategies for transformation of naturally-occurring amphibian antimicrobial peptides into therapeutically valuable anti-infective agents. Methods 2007; 42: 349-57.
    • (2007) Methods , vol.42 , pp. 349-357
    • Conlon, J.M.1    Al-Ghaferi, N.2    Abraham, B.3    Leprince, J.4
  • 29
    • 52049103111 scopus 로고    scopus 로고
    • Refections on a systematic nomenclature for antimicrobial peptides from the skins of frogs of the family Ranidae
    • Conlon JM. Refections on a systematic nomenclature for antimicrobial peptides from the skins of frogs of the family Ranidae. Peptides 2008; 29: 1815-9.
    • (2008) Peptides , vol.29 , pp. 1815-1819
    • Conlon, J.M.1
  • 31
    • 33750936381 scopus 로고    scopus 로고
    • Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis
    • Lu Y, Li JX, Yu HN, Xu XQ, Liang JG, Tian YQ, Ma DY, Lin GQ, Huang GQ, Lai R. Two families of antimicrobial peptides with multiple functions from skin of rufous-spotted torrent frog, Amolops loloensis. Peptides 2006; 27: 3085-91.
    • (2006) Peptides , vol.27 , pp. 3085-3091
    • Lu, Y.1    Li, J.X.2    Yu, H.N.3    Xu, X.Q.4    Liang, J.G.5    Tian, Y.Q.6    Ma, D.Y.7    Lin, G.Q.8    Huang, G.Q.9    Lai, R.10
  • 33
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bullet P, Stöcklin R, Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 2004; 198: 169-84.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bullet, P.1    Stöcklin, R.2    Menin, L.3
  • 36
    • 0030582631 scopus 로고    scopus 로고
    • CDNA cloning and characterization of Buforin I, an antimicrobial peptide: A cleavage product of histone H2A
    • Kim HS, Park CB, Kim MS, Kim SC. cDNA cloning and characterization of Buforin I, an antimicrobial peptide: a cleavage product of histone H2A. Biochem Biophys Res Commun 1996; 229: 381-7.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 381-387
    • Kim, H.S.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 37
    • 0029047938 scopus 로고
    • Amphibian skin: A promising resource for antimicrobial peptides
    • Barra D, Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol 1995; 13: 205-9.
    • (1995) Trends Biotechnol , vol.13 , pp. 205-209
    • Barra, D.1    Simmaco, M.2
  • 38
    • 0027069524 scopus 로고
    • A novel method for the release and collection of dermal, glandular secretions from the skin of frogs
    • Tyler MJ, Stone DJ, Bowie JH. A novel method for the release and collection of dermal, glandular secretions from the skin of frogs. J Pharmacol Toxicol Methods 1992; 28: 199-200.
    • (1992) J Pharmacol Toxicol Methods , vol.28 , pp. 199-200
    • Tyler, M.J.1    Stone, D.J.2    Bowie, J.H.3
  • 39
    • 0028707742 scopus 로고
    • Biosynthesis of defensins and other antimicrobial peptides
    • Ganz T. Biosynthesis of defensins and other antimicrobial peptides. Ciba Found Symp 1994; 186: 62-71.
    • (1994) Ciba Found Symp , vol.186 , pp. 62-71
    • Ganz, T.1
  • 40
    • 0032817470 scopus 로고    scopus 로고
    • The dermaseptin precursors: A protein family with a common preproregion and a variable C-terminal antimicrobial domain
    • Amiche M, Aurelia AS, Thierry NP, Nicolas P. The dermaseptin precursors: a protein family with a common preproregion and a variable C-terminal antimicrobial domain. FEBS Lett 1999; 456: 352-6.
    • (1999) FEBS Lett , vol.456 , pp. 352-356
    • Amiche, M.1    Aurelia, A.S.2    Thierry, N.P.3    Nicolas, P.4
  • 41
    • 0001462005 scopus 로고    scopus 로고
    • Host defence antibacterial peptides from skin secretions of Australian amphibians. The relationship between structure and activity
    • Bowie JH, Wegener KL, Chia BCS, Wabnitz PA, Carver JA, Tyler MJ, Wallace JC. Host defence antibacterial peptides from skin secretions of Australian amphibians. The relationship between structure and activity. Peptides 1999; 6: 259-69.
    • (1999) Peptides , vol.6 , pp. 259-269
    • Bowie, J.H.1    Wegener, K.L.2    Chia, B.C.S.3    Wabnitz, P.A.4    Carver, J.A.5    Tyler, M.J.6    Wallace, J.C.7
  • 42
    • 0026048043 scopus 로고
    • A novel endopeptidase from Xenopus that recognizes α-helical secondary structure
    • Resnick NM, Maloy WL, Guy HR, Zasloff M. A novel endopeptidase from Xenopus that recognizes α-helical secondary structure. Cell 1991; 66: 541-54.
    • (1991) Cell , vol.66 , pp. 541-554
    • Resnick, N.M.1    Maloy, W.L.2    Guy, H.R.3    Zasloff, M.4
  • 43
    • 33748919831 scopus 로고    scopus 로고
    • Membrane interactions of antimicrobial peptides from Australian tree frogs
    • Boland MP, Separovic F. Membrane interactions of antimicrobial peptides from Australian tree frogs. Biochim Biophys Acta 2006; 1758: 1178-83.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1178-1183
    • Boland, M.P.1    Separovic, F.2
  • 46
    • 0142183723 scopus 로고    scopus 로고
    • Ribosomally synthesized peptides with antimicrobial properties: Biosynthesis, structure, function, and applications
    • Papagianni M. Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol Adv 2003; 21: 465-99.
    • (2003) Biotechnol Adv , vol.21 , pp. 465-499
    • Papagianni, M.1
  • 47
    • 0027096816 scopus 로고
    • Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa
    • Morikawa N, Hagiwara K, Nakajima T. Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. Biochem Biophys Res Commun 1992; 189: 184-90.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 184-190
    • Morikawa, N.1    Hagiwara, K.2    Nakajima, T.3
  • 48
    • 0023226518 scopus 로고
    • D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor
    • Richter K, Egger R, Kreil G. D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor. Science 1987; 238: 200-2.
    • (1987) Science , vol.238 , pp. 200-202
    • Richter, K.1    Egger, R.2    Kreil, G.3
  • 49
    • 0027370683 scopus 로고
    • Antibacterial and haemolytic peptides containing D-allo-isoleucine from the skin of Bombina variegate
    • Mignogna G, Simmaco M, Kreil G, Barra D. Antibacterial and haemolytic peptides containing D-allo-isoleucine from the skin of Bombina variegate. EMBO J 1993; 12: 4829-32.
    • (1993) EMBO J , vol.12 , pp. 4829-4832
    • Mignogna, G.1    Simmaco, M.2    Kreil, G.3    Barra, D.4
  • 50
    • 77449144486 scopus 로고    scopus 로고
    • Combined peptidomics and genomics approach to the isolation of amphibian antimicrobial peptides
    • Lai R. Combined peptidomics and genomics approach to the isolation of amphibian antimicrobial peptides. Methods Mol Biol 2010; 615: 177-90.
    • (2010) Methods Mol Biol , vol.615 , pp. 177-190
    • Lai, R.1
  • 51
    • 0034693283 scopus 로고    scopus 로고
    • Induction of synthesis of an antimicrobial peptide in the skin of the freezetolerant frog, Rana sylvatica in response to environmental stimuli
    • Matutte B, Storey KB, Knoop C, Conlon JM. Induction of synthesis of an antimicrobial peptide in the skin of the freezetolerant frog, Rana sylvatica in response to environmental stimuli. FEBS Lett 2000; 483: 135-8.
    • (2000) FEBS Lett , vol.483 , pp. 135-138
    • Matutte, B.1    Storey, K.B.2    Knoop, C.3    Conlon, J.M.4
  • 52
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • Rinaldi AC. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr Opin Chem Biol 2002; 6: 799-804.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 799-804
    • Rinaldi, A.C.1
  • 54
    • 67349193554 scopus 로고    scopus 로고
    • Purification, characterization and cloning of two novel tigerinin-like peptides from skin secretions of Fejervarya cancrivora
    • Song Y, Lu Y, Wang L, Yang H, Zhang K, Lai R. Purification, characterization and cloning of two novel tigerinin-like peptides from skin secretions of Fejervarya cancrivora. Peptides 2009; 30: 1228-32.
    • (2009) Peptides , vol.30 , pp. 1228-1232
    • Song, Y.1    Lu, Y.2    Wang, L.3    Yang, H.4    Zhang, K.5    Lai, R.6
  • 55
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock REW, Diamond G. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol 2000; 8: 402-10.
    • (2000) Trends Microbiol , vol.8 , pp. 402-410
    • Hancock, R.E.W.1    Diamond, G.2
  • 57
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers JP, Hancock RE. The relationship between peptide structure and antibacterial activity. Peptides 2003; 24: 1681-91.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 58
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG. Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 1995; 13: 61-92.
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 59
    • 0032511047 scopus 로고    scopus 로고
    • Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics
    • Charpentier S, Amiche M, Mester J, Vouille V, Caer JPL, Nicolas P, Delfour A. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. J Biol Chem 1998; 273: 14690-7.
    • (1998) J Biol Chem , vol.273 , pp. 14690-14697
    • Charpentier, S.1    Amiche, M.2    Mester, J.3    Vouille, V.4    Caer, J.P.L.5    Nicolas, P.6    Delfour, A.7
  • 60
    • 0008328133 scopus 로고
    • Ubiquitous natural antibiotics
    • Gabay JE. Ubiquitous natural antibiotics. Science 1994; 64: 229-30.
    • (1994) Science , vol.64 , pp. 229-230
    • Gabay, J.E.1
  • 61
    • 0026354641 scopus 로고
    • Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis
    • Gibson BW, Tang D, Mandrell R, Kelly M, Spindel ER. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. J Biol Chem 1991; 266: 23103-11.
    • (1991) J Biol Chem , vol.266 , pp. 23103-23111
    • Gibson, B.W.1    Tang, D.2    Mandrell, R.3    Kelly, M.4    Spindel, E.R.5
  • 62
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas P, Mor A. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu Rev Microbiol 1995; 49: 277-304.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 63
    • 0032578602 scopus 로고    scopus 로고
    • Ranatuerins: Antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana
    • Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Biochem Biophys Res Commun 1998; 250: 589-92.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 589-592
    • Goraya, J.1    Knoop, F.C.2    Conlon, J.M.3
  • 64
    • 0033973411 scopus 로고    scopus 로고
    • Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs, Rana luteiventris, Rana berlandieri and Rana pipiens
    • Goraya J, Wang Y, Li Z, O'Flaherty M, Knoop FC, Platz JE, Conlon JM. Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs, Rana luteiventris, Rana berlandieri and Rana pipiens. Eur J Biochem 2000; 267: 894-900.
    • (2000) Eur J Biochem , vol.267 , pp. 894-900
    • Goraya, J.1    Wang, Y.2    Li, Z.3    O'Flaherty, M.4    Knoop, F.C.5    Platz, J.E.6    Conlon, J.M.7
  • 65
    • 0033859322 scopus 로고    scopus 로고
    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. The solution structure of aurein 1.2
    • Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. The solution structure of aurein 1.2. Eur J Biochem 2000; 267: 5330-41.
    • (2000) Eur J Biochem , vol.267 , pp. 5330-5341
    • Rozek, T.1    Wegener, K.L.2    Bowie, J.H.3    Olver, I.N.4    Carver, J.A.5    Wallace, J.C.6    Tyler, M.J.7
  • 66
    • 0034109713 scopus 로고    scopus 로고
    • Maculatin 1.1, an antimicrobial peptide from the Australian tree frog, Litoria genimaculata - Solution structure and biological activity
    • Chia BCS, Carver JA, Mulhern TD, Bowie JH. Maculatin 1.1, an antimicrobial peptide from the Australian tree frog, Litoria genimaculata - solution structure and biological activity. Eur J Biochem 2000; 267: 1894-908.
    • (2000) Eur J Biochem , vol.267 , pp. 1894-1908
    • Chia, B.C.S.1    Carver, J.A.2    Mulhern, T.D.3    Bowie, J.H.4
  • 67
    • 0034801156 scopus 로고    scopus 로고
    • Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: Sequence determination by electrospray mass spectrometry
    • Wegener KL, Brinkworth CS, Bowie JH, Wallace JC, Tyler MJ. Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry. Rapid Commun Mass Spectrom 2001; 15: 1726-34.
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 1726-1734
    • Wegener, K.L.1    Brinkworth, C.S.2    Bowie, J.H.3    Wallace, J.C.4    Tyler, M.J.5
  • 69
    • 14044268292 scopus 로고    scopus 로고
    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor
    • Wang G, Li Y, Li X. Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor. J Biol Chem 2005; 280: 5803-11.
    • (2005) J Biol Chem , vol.280 , pp. 5803-5811
    • Wang, G.1    Li, Y.2    Li, X.3
  • 70
    • 0028003782 scopus 로고
    • Antimicrobial peptides from the skin of a Korean frog, Rana rugosa
    • Park JM, Jung JE, Lee BJ. Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. Biochem Biophys Res Commun 1994; 205: 948-54.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 948-954
    • Park, J.M.1    Jung, J.E.2    Lee, B.J.3
  • 71
    • 0034733959 scopus 로고    scopus 로고
    • Purification and characterization of antimicrobial peptides from skin extracts and skin secretions of the North American pig frog Rana grylio
    • Kim JB, Halverson T, Basir YJ, Dulka J, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from skin extracts and skin secretions of the North American pig frog Rana grylio. Regul Pept 2000; 90: 53-60.
    • (2000) Regul Pept , vol.90 , pp. 53-60
    • Kim, J.B.1    Halverson, T.2    Basir, Y.J.3    Dulka, J.4    Knoop, F.C.5    Conlon, J.M.6
  • 72
    • 0034018231 scopus 로고    scopus 로고
    • Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans
    • Halverson T, Basir YJ, Knoop FC, Conlon JM. Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans. Peptides 2000; 21: 469-76.
    • (2000) Peptides , vol.21 , pp. 469-476
    • Halverson, T.1    Basir, Y.J.2    Knoop, F.C.3    Conlon, J.M.4
  • 73
  • 74
    • 67649277614 scopus 로고    scopus 로고
    • Action mechanism and structural requirements of the antimicrobial peptides, gaegurins
    • Won HS, Kang SJ, Lee BJ. Action mechanism and structural requirements of the antimicrobial peptides, gaegurins. Biochim Biophys Acta 2009; 1788: 1620-9.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1620-1629
    • Won, H.S.1    Kang, S.J.2    Lee, B.J.3
  • 76
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H, Hancock REW. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob Agents Chemother 2001; 45: 1558-60.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.W.2
  • 77
    • 0035984779 scopus 로고    scopus 로고
    • Design and activity of antimicrobial peptides against sporogonic-stage parasites causing murine malarias
    • Arrighi RB, Nakamura C, Miyake J, Hurd H, Burgess JG. Design and activity of antimicrobial peptides against sporogonic-stage parasites causing murine malarias. Antimicrob Agents Chemother 2002; 46: 2104-10.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 2104-2110
    • Arrighi, R.B.1    Nakamura, C.2    Miyake, J.3    Hurd, H.4    Burgess, J.G.5
  • 78
    • 0025860280 scopus 로고
    • Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation
    • Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci USA 1991; 88: 3792-6.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3792-3796
    • Cruciani, R.A.1    Barker, J.L.2    Zasloff, M.3    Chen, H.C.4    Colamonici, O.5
  • 79
    • 0027166016 scopus 로고
    • Anticancer efficacy of magainin 2 and analogue peptides
    • Baker MA, Maloy WL, Zasloff M, Jacob LS. Anticancer efficacy of magainin 2 and analogue peptides. Cancer Res 1993; 53: 3052-7.
    • (1993) Cancer Res , vol.53 , pp. 3052-3057
    • Baker, M.A.1    Maloy, W.L.2    Zasloff, M.3    Jacob, L.S.4
  • 80
    • 34547753063 scopus 로고    scopus 로고
    • Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides
    • Li JX, Zhang C, Xu XQ, Wang J, Yu HN, Lai R, Gong WM. Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides. FASEB J 2007; 21: 2466-73.
    • (2007) FASEB J , vol.21 , pp. 2466-2473
    • Li, J.X.1    Zhang, C.2    Xu, X.Q.3    Wang, J.4    Yu, H.N.5    Lai, R.6    Gong, W.M.7
  • 81
    • 0031761654 scopus 로고    scopus 로고
    • In vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria
    • Giacometti A, Cirioni O, Greganti G, Quarta M, Scalise G. In vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria. Antimicrob Agents Chemother 1998; 42: 3320-4.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3320-3324
    • Giacometti, A.1    Cirioni, O.2    Greganti, G.3    Quarta, M.4    Scalise, G.5
  • 82
    • 0028216606 scopus 로고
    • Activity of two synthetic amphiphilic peptides and magainin-2 against herpes simplex virus types 1 and 2
    • Aboudy Y, Mendelson E, Shalit I, Bessalle R, Fridkin M. Activity of two synthetic amphiphilic peptides and magainin-2 against herpes simplex virus types 1 and 2. Int J Pept Protein Res 1994; 43: 573-82.
    • (1994) Int J Pept Protein Res , vol.43 , pp. 573-582
    • Aboudy, Y.1    Mendelson, E.2    Shalit, I.3    Bessalle, R.4    Fridkin, M.5
  • 83
    • 2342584711 scopus 로고    scopus 로고
    • Preclinical evaluation of magainin-A as a contraceptive antimicrobial agent
    • Clara A, Manjramkar DD, Reddy VK. Preclinical evaluation of magainin-A as a contraceptive antimicrobial agent. Fertil Steril 2004; 81: 1357-65.
    • (2004) Fertil Steril , vol.81 , pp. 1357-1365
    • Clara, A.1    Manjramkar, D.D.2    Reddy, V.K.3
  • 87
    • 71149119140 scopus 로고    scopus 로고
    • Dermaseptins and magainins: Antimicrobial peptides from frogs' skin - New sources for a promising spermicides sicrobicides - A mini review
    • Zairi A, Tangy F, Bouassida K, Hani K. Dermaseptins and magainins: antimicrobial peptides from frogs' skin - new sources for a promising spermicides sicrobicides - a mini review. J Biomed Biotechnol 2009; 2009: 452567.
    • (2009) J Biomed Biotechnol , vol.2009 , pp. 452567
    • Zairi, A.1    Tangy, F.2    Bouassida, K.3    Hani, K.4
  • 88
    • 77149155289 scopus 로고    scopus 로고
    • Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database
    • Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. Antimicrob Agents Chemother 2010; 54: 1343-6.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1343-1346
    • Wang, G.1    Watson, K.M.2    Peterkofsky, A.3    Buckheit, R.W.4
  • 89
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin DW, Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim Biophys Acta 2008; 1778: 357-75.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 90
    • 0033569805 scopus 로고    scopus 로고
    • Host defense peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1
    • Wegener KL, Wabnitz PA, Carver JA, Bowie JH, Chia BCS, Wallace JC, Tyler MJ. Host defense peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. Eur J Biochem 1999; 265: 627-37.
    • (1999) Eur J Biochem , vol.265 , pp. 627-637
    • Wegener, K.L.1    Wabnitz, P.A.2    Carver, J.A.3    Bowie, J.H.4    Chia, B.C.S.5    Wallace, J.C.6    Tyler, M.J.7
  • 91
    • 0028177604 scopus 로고
    • Ranalexin A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin
    • Clark DP, Durell S, Maloy WL, Zasloff M. Ranalexin A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. J Biol Chem 1994; 269: 10849-55.
    • (1994) J Biol Chem , vol.269 , pp. 10849-10855
    • Clark, D.P.1    Durell, S.2    Maloy, W.L.3    Zasloff, M.4
  • 92
    • 0034007516 scopus 로고    scopus 로고
    • Anticryptosporidial activity of ranalexin, lasalocid and azithromycin alone and in combination in cell lines
    • Giacometti A, Cirioni O, Barchiesi F, Scalise G. Anticryptosporidial activity of ranalexin, lasalocid and azithromycin alone and in combination in cell lines. J Antimicrob Agents 2000; 45: 375-7.
    • (2000) J Antimicrob Agents , vol.45 , pp. 375-377
    • Giacometti, A.1    Cirioni, O.2    Barchiesi, F.3    Scalise, G.4
  • 93
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki K, Sugishita K, Harada M, Fujii N, Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim Biophys Acta 1997; 1327: 119-30.
    • (1997) Biochim Biophys Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 95
    • 0029871082 scopus 로고    scopus 로고
    • Spermicidal activity of Magainins: In vitro and in vivo studies
    • Reddy KV, Shahani SK, Meherji PK. Spermicidal activity of Magainins: in vitro and in vivo studies. Contraception 1996; 53: 205-10.
    • (1996) Contraception , vol.53 , pp. 205-210
    • Reddy, K.V.1    Shahani, S.K.2    Meherji, P.K.3
  • 96
    • 0034939013 scopus 로고    scopus 로고
    • Embryotoxicity of magainin-2-amide and its enhancement by cyclodextrin, albumin, hydrogen peroxide and acidification
    • Mystkowska ET, Niemierko A, Komar A, Sawicki W. Embryotoxicity of magainin-2-amide and its enhancement by cyclodextrin, albumin, hydrogen peroxide and acidification. Hum Reprod 2001; 16: 1457-63.
    • (2001) Hum Reprod , vol.16 , pp. 1457-1463
    • Mystkowska, E.T.1    Niemierko, A.2    Komar, A.3    Sawicki, W.4
  • 97
    • 33646766410 scopus 로고    scopus 로고
    • Histamine-releasing and antimicrobial peptides from the skin secretions of the Dusky Gopher frog, Rana sevosa
    • Graham C, Richter SC, McClean S, O'Kane E, Flatt PR, Shaw C. Histamine-releasing and antimicrobial peptides from the skin secretions of the Dusky Gopher frog, Rana sevosa. Peptides 2006; 27: 1313-9.
    • (2006) Peptides , vol.27 , pp. 1313-1319
    • Graham, C.1    Richter, S.C.2    McClean, S.3    O'Kane, E.4    Flatt, P.R.5    Shaw, C.6
  • 98
    • 55949094899 scopus 로고    scopus 로고
    • A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity
    • Abdel-Wahab YHA, Power GJ, Flatt PR, Woodhams DC, Rollins-Smith LA, Conlon JM. A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity. Peptides 2008; 29: 2136-43.
    • (2008) Peptides , vol.29 , pp. 2136-2143
    • Abdel-Wahab, Y.H.A.1    Power, G.J.2    Flatt, P.R.3    Woodhams, D.C.4    Rollins-Smith, L.A.5    Conlon, J.M.6
  • 100
    • 71549152200 scopus 로고    scopus 로고
    • Gaegurin-6 stimulates insulin secretion through calcium influx in pancreatic βrin5mf cells
    • Kim JH, Lee JO, Jung JH, Lee SK, You GY, Park SH, Kim HS. Gaegurin-6 stimulates insulin secretion through calcium influx in pancreatic βRin5mf cells. Regul Pept 2010; 159: 123-8.
    • (2010) Regul Pept , vol.159 , pp. 123-128
    • Kim, J.H.1    Lee, J.O.2    Jung, J.H.3    Lee, S.K.4    You, G.Y.5    Park, S.H.6    Kim, H.S.7
  • 101
    • 67349147008 scopus 로고    scopus 로고
    • A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae)
    • Conlon JM, Abdel-Wahab YH, Flatt PR, Leprince J, Vaudry H, Jouenne T, Condamine E. A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae). Peptides 2009; 30: 888-92.
    • (2009) Peptides , vol.30 , pp. 888-892
    • Conlon, J.M.1    Abdel-Wahab, Y.H.2    Flatt, P.R.3    Leprince, J.4    Vaudry, H.5    Jouenne, T.6    Condamine, E.7
  • 102
    • 38649103176 scopus 로고    scopus 로고
    • Insulin-releasing properties of the frog skin peptide pseudin-2 and its wLys18x-substituted analogue
    • Abdel-Wahab YH, Power GJ, Ng MT, Flatt PR, Conlon JM. Insulin-releasing properties of the frog skin peptide pseudin-2 and its wLys18x-substituted analogue. Biol Chem 2008; 389: 143-8.
    • (2008) Biol Chem , vol.389 , pp. 143-148
    • Abdel-Wahab, Y.H.1    Power, G.J.2    Ng, M.T.3    Flatt, P.R.4    Conlon, J.M.5
  • 103
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
    • Eng J, Kleinman WA, Singh L, Singh G, Raufman JP. Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas. J Biol Chem 1992; 267: 7402-5.
    • (1992) J Biol Chem , vol.267 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.P.5
  • 105
    • 34548675371 scopus 로고    scopus 로고
    • Insulin releasing properties of the temporin family of antimicrobial peptides
    • Abdel-Wahab YH, Marenah L, Flatt PR, Conlon JM. Insulin releasing properties of the temporin family of antimicrobial peptides. Protein Pept Lett 2007; 14: 702-7.
    • (2007) Protein Pept Lett , vol.14 , pp. 702-707
    • Abdel-Wahab, Y.H.1    Marenah, L.2    Flatt, P.R.3    Conlon, J.M.4
  • 106
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-95.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 107
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005; 3: 238-50.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 108
    • 28044443162 scopus 로고    scopus 로고
    • Antibacterial peptides and proteins with multiple cellular targets
    • Otvos L. Antibacterial peptides and proteins with multiple cellular targets. J Pept Sci 2005; 11: 697-706.
    • (2005) J Pept Sci , vol.11 , pp. 697-706
    • Otvos, L.1
  • 109
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bila
    • Ehrenstein G, Lecar H. Electrically gated ionic channels in lipid bila. Q Rev Biophys 1977; 10: 1-34.
    • (1977) Q Rev Biophys , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 110
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren Z, Shai Y. Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 1998; 47: 451-63.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 111
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1999; 1462: 55-70.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 112
    • 3042772810 scopus 로고    scopus 로고
    • Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering
    • Spaar A, Munster C, Salditt T. Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering. Biophys J 2004; 87: 396-407.
    • (2004) Biophys J , vol.87 , pp. 396-407
    • Spaar, A.1    Munster, C.2    Salditt, T.3
  • 113
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He K, Ludtke SJ, Huang HW, Worcester DL. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 1995; 34: 15614-8.
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4
  • 114
    • 0034859096 scopus 로고    scopus 로고
    • Barrelstave model or toroidal model? A case study on melittin pores
    • Yang L, Harroun TA, Weiss TM, Ding L, Huang HW. Barrelstave model or toroidal model? A case study on melittin pores. Biophys J 2001; 81: 1475-85.
    • (2001) Biophys J , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 115
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He K, Ludtke SJ, Worcester DL, Huang HW. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys J 1996; 70: 2659-66.
    • (1996) Biophys J , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 116
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solidstate NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solidstate NMR spectroscopy. Biochim Biophys Acta 1999; 1462: 157-83.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 117
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi S, Huster D, Waring A, Lehrer RI, Kearney W, Tack BF, Hong M. Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy. Biophys J 2001; 81: 2203-14.
    • (2001) Biophys J , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 118
    • 0026969265 scopus 로고    scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 1999; 31: 12416-23.
    • (1999) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 119
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin
    • Yamaguchi S, Hong T. Solid-state NMR investigations of peptide-lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin. Biochemistry 2002; 41: 9852-62.
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2
  • 120
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki K, Murase O, Fujii N, Miyajima K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 1996; 35: 11361-8.
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 121
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock KJ, Lee DK, Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys J 2003; 84: 3052-60.
    • (2003) Biophys J , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 122
    • 0030602175 scopus 로고    scopus 로고
    • Solution structure of an antimicrobial peptide buforin II
    • Yi G-S, Park CB, Kim SC, Cheong C. Solution structure of an antimicrobial peptide buforin II. FEBS Lett 1996; 398: 87-90.
    • (1996) FEBS Lett , vol.398 , pp. 87-90
    • Yi, G.-S.1    Park, C.B.2    Kim, S.C.3    Cheong, C.4
  • 124
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki K, Sugishita K, Harada M, Fujii N, Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim Biophys Acta 1997; 1327: 119-30.
    • (1997) Biochim Biophys Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 125
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang HW, Chen FY, Lee MT. Molecular mechanism of peptide-induced pores in membranes. Phys Rev Lett 2004; 92: 198304.
    • (2004) Phys Rev Lett , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 126
    • 0024396374 scopus 로고
    • Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis
    • Juretić D, Chen HC, Brown JH, Morell JL, Hendler RW, Westerhoff HV. Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis. FEBS Lett 1989; 249: 219-23.
    • (1989) FEBS Lett , vol.249 , pp. 219-223
    • Juretić, D.1    Chen, H.C.2    Brown, J.H.3    Morell, J.L.4    Hendler, R.W.5    Westerhoff, H.V.6
  • 127
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy WL, Kari UP. Structure-activity studies on magainins and other host defense peptides. Biopolymers 1995; 37: 105-22.
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 128
    • 0032497377 scopus 로고    scopus 로고
    • Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta
    • Kwon MY, Hong SY, Lee KH. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. Biochim Biophys Acta 1998; 1387: 239-48.
    • (1998) Biochim Biophys Acta , vol.1387 , pp. 239-248
    • Kwon, M.Y.1    Hong, S.Y.2    Lee, K.H.3
  • 129
    • 0036467404 scopus 로고    scopus 로고
    • General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides
    • Dathe M, Meyer J, Beyermann M, Maul B, Hoischen C, Bienerta M. General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides. Biochim Biophys Acta 2002; 1558: 171-86.
    • (2002) Biochim Biophys Acta , vol.1558 , pp. 171-186
    • Dathe, M.1    Meyer, J.2    Beyermann, M.3    Maul, B.4    Hoischen, C.5    Bienerta, M.6
  • 130
    • 33744908288 scopus 로고    scopus 로고
    • Host-defence peptides from the glandular secretions of amphibians: Structure and activity
    • Pukala TL, Bowie JH, Maselli VM, Musgrave IF, Tyler MJ. Host-defence peptides from the glandular secretions of amphibians: structure and activity. Nat Prod Rep 2006; 23: 368-93.
    • (2006) Nat Prod Rep , vol.23 , pp. 368-393
    • Pukala, T.L.1    Bowie, J.H.2    Maselli, V.M.3    Musgrave, I.F.4    Tyler, M.J.5
  • 131
    • 1542289126 scopus 로고    scopus 로고
    • Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its wLys-8x-substituted analog
    • Sonnevend A, Knoop FC, Patel M, Pál T, Soto AM, Conlon JM. Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its wLys-8x-substituted analog. Peptides 2004; 25: 29-36.
    • (2004) Peptides , vol.25 , pp. 29-36
    • Sonnevend, A.1    Knoop, F.C.2    Patel, M.3    Pál, T.4    Soto, A.M.5    Conlon, J.M.6
  • 132
    • 0035984825 scopus 로고    scopus 로고
    • Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: Design of analogs with improved activity and their action on clinical bacterial isolates
    • Sitaram N, Sai KP, Singh S, Sankaran K, Nagaraj R. Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: design of analogs with improved activity and their action on clinical bacterial isolates. Antimicrob Agents Chemother 2000; 46: 2279-83.
    • (2000) Antimicrob Agents Chemother , vol.46 , pp. 2279-2283
    • Sitaram, N.1    Sai, K.P.2    Singh, S.3    Sankaran, K.4    Nagaraj, R.5
  • 133
    • 33645538062 scopus 로고    scopus 로고
    • Effect of natural L- to D-amino acid conversion on the organization, membrane binding, and biological function of the antimicrobial peptides bombinins H
    • Mangoni ML, Papo N, Saugar JM, Barra D, Shai Y, Simmaco M, Rivas L. Effect of natural L- to D-amino acid conversion on the organization, membrane binding, and biological function of the antimicrobial peptides bombinins H. Biochemistry 2006; 45: 4266-76.
    • (2006) Biochemistry , vol.45 , pp. 4266-4276
    • Mangoni, M.L.1    Papo, N.2    Saugar, J.M.3    Barra, D.4    Shai, Y.5    Simmaco, M.6    Rivas, L.7
  • 134
    • 0037223304 scopus 로고    scopus 로고
    • Antimicrobial activity of magainin analogues against anaerobic oral pathogens
    • Genco CA, Maloy WL, Kari UP, Motley M. Antimicrobial activity of magainin analogues against anaerobic oral pathogens. Int J Antimicrob Agents 2003; 21: 75-8.
    • (2003) Int J Antimicrob Agents , vol.21 , pp. 75-78
    • Genco, C.A.1    Maloy, W.L.2    Kari, U.P.3    Motley, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.