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Volumn 9, Issue 7, 2014, Pages 1613-1621

Hydrophobicity and helicity regulate the antifungal activity of 14-helical β-peptides

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; ANTIFUNGAL AGENT; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 84904578022     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500203e     Document Type: Article
Times cited : (55)

References (84)
  • 1
    • 27944505093 scopus 로고    scopus 로고
    • Systemic fungal infections caused by Candida species: Epidemiology, infection process and virulence attributes
    • DOI 10.2174/138945005774912735
    • Mavor, A. L., Thewes, S., and Hube, B. (2005) Systemic fungal infections caused by Candida species: Epidemiology, infection process and virulence attributes Curr. Drug Targets 6, 863-874 (Pubitemid 41672448)
    • (2005) Current Drug Targets , vol.6 , Issue.8 , pp. 863-874
    • Mavor, A.L.1    Thewes, S.2    Hube, B.3
  • 2
    • 84860789699 scopus 로고    scopus 로고
    • Tackling human fungal infections
    • Brown, G. D., Denning, D. W., and Levitz, S. M. (2012) Tackling human fungal infections Science 336, 647-647
    • (2012) Science , vol.336 , pp. 647-647
    • Brown, G.D.1    Denning, D.W.2    Levitz, S.M.3
  • 3
    • 37349073878 scopus 로고    scopus 로고
    • Infection in solid-organ transplant recipients
    • DOI 10.1056/NEJMra064928
    • Fishman, J. A. (2007) Infection in solid-organ transplant recipients N. Engl. J. Med. 357, 2601-2614 (Pubitemid 350294226)
    • (2007) New England Journal of Medicine , vol.357 , Issue.25 , pp. 2601-2614
    • Fishman, J.A.1
  • 4
    • 33646826630 scopus 로고    scopus 로고
    • Changing incidence of Candida bloodstream infections among NICU patients in the United States: 1995-2004
    • DOI 10.1542/peds.2005-1996
    • Fridkin, S. K., Kaufman, D., Edwards, J. R., Shetty, S., and Horan, T. (2006) Changing incidence of Candida bloodstream infections among NICU patients in the United States: 1995-2004 Pediatrics 117, 1680-1687 (Pubitemid 46071397)
    • (2006) Pediatrics , vol.117 , Issue.5 , pp. 1680-1687
    • Fridkin, S.K.1    Kaufman, D.2    Edwards, J.R.3    Shetty, S.4    Horan, T.5
  • 7
    • 58749083534 scopus 로고    scopus 로고
    • Epidemiology and outcome of invasive fungal infection in adult hematopoietic stem cell transplant recipients: Analysis of multicenter prospective antifungal therapy (PATH) alliance registry
    • Neofytos, D., Horn, D., Anaissie, E., Steinbach, W., Olyaei, A., Fishman, J., Pfaller, M., Chang, C., Webster, K., and Marr, K. (2009) Epidemiology and outcome of invasive fungal infection in adult hematopoietic stem cell transplant recipients: Analysis of multicenter prospective antifungal therapy (PATH) alliance registry Clin. Infect. Dis. 48, 265-273
    • (2009) Clin. Infect. Dis. , vol.48 , pp. 265-273
    • Neofytos, D.1    Horn, D.2    Anaissie, E.3    Steinbach, W.4    Olyaei, A.5    Fishman, J.6    Pfaller, M.7    Chang, C.8    Webster, K.9    Marr, K.10
  • 8
    • 0037369002 scopus 로고    scopus 로고
    • Fungal infections in the recipients of solid organ transplantation
    • DOI 10.1016/S0891-5520(02)00067-3
    • Singh, N. (2003) Fungal infections in the recipients of solid organ transplantation Infect. Dis. Clin. North Am. 17, 113-134 (Pubitemid 36514573)
    • (2003) Infectious Disease Clinics of North America , vol.17 , Issue.1 , pp. 113-134
    • Singh, N.1
  • 10
    • 0033302528 scopus 로고    scopus 로고
    • Emerging fungal pathogens: Evolving challenges to immunocompromised patients for the twenty-first century
    • Walsh, T. J. and Groll, A. H. (1999) Emerging fungal pathogens: Evolving challenges to immunocompromised patients for the twenty-first century Transpl. Infect. Dis. 1, 247-261
    • (1999) Transpl. Infect. Dis. , vol.1 , pp. 247-261
    • Walsh, T.J.1    Groll, A.H.2
  • 12
    • 20944439684 scopus 로고    scopus 로고
    • Candida biofilm: A well-designed protected environment
    • DOI 10.1080/13693780500107554
    • Mukherjee, P. K., Zhou, G. Y., Munyon, R., and Ghannoum, M. A. (2005) Candida biofilm: A well-designed protected environment Med. Mycol. 43, 191-208 (Pubitemid 40867493)
    • (2005) Medical Mycology , vol.43 , Issue.3 , pp. 191-208
    • Mukherjee, P.K.1    Zhou, G.2    Munyon, R.3    Ghannoum, M.A.4
  • 13
    • 2042519310 scopus 로고    scopus 로고
    • Candida Infections of Medical Devices
    • DOI 10.1128/CMR.17.2.255-267.2004
    • Kojic, E. M. and Darouiche, R. O. (2004) Candida infections of medical devices Clin. Microbiol. Rev. 17, 255-267 (Pubitemid 38534029)
    • (2004) Clinical Microbiology Reviews , vol.17 , Issue.2 , pp. 255-267
    • Kojic, E.M.1    Darouiche, R.O.2
  • 14
    • 0029135076 scopus 로고
    • Resistance of Candida-albicans biofilms to antifungal agents in-vitro
    • Hawser, S. P. and Douglas, L. J. (1995) Resistance of Candida-albicans biofilms to antifungal agents in-vitro Antimicrob. Agents Chemother. 39, 2128-2131
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2128-2131
    • Hawser, S.P.1    Douglas, L.J.2
  • 15
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • Ganz, T. (2003) Defensins: Antimicrobial peptides of innate immunity Nat. Rev. Immunol. 3, 710-720 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 16
    • 0142058024 scopus 로고    scopus 로고
    • Endogenous production of antimicrobial peptides in innate immunity and human disease
    • Gallo, R. L. and Nizet, V. (2003) Endogenous production of antimicrobial peptides in innate immunity and human disease Curr. Allergy Asthma Rep. 3, 402-409 (Pubitemid 38899107)
    • (2003) Current Allergy and Asthma Reports , vol.3 , Issue.5 , pp. 402-409
    • Gallo, R.L.1    Nizet, V.2
  • 17
    • 0346157290 scopus 로고    scopus 로고
    • Innate immunity: An overview
    • DOI 10.1016/j.molimm.2003.10.005
    • Beutler, B. (2004) Innate immunity: an overview Mol. Immunol. 40, 845-859 (Pubitemid 38035204)
    • (2004) Molecular Immunology , vol.40 , Issue.12 , pp. 845-859
    • Beutler, B.1
  • 18
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • DOI 10.1016/S0167-7799(97)01156-6, PII S0167779997011566
    • Hancock, R. E. W. and Lehrer, R. (1998) Cationic peptides: a new source of antibiotics Trends Biotechnol. 16, 82-88 (Pubitemid 28055477)
    • (1998) Trends in Biotechnology , vol.16 , Issue.2 , pp. 82-88
    • Hancock, R.E.W.1    Lehrer, R.2
  • 19
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms Nature 415, 389-395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 21
    • 85067748385 scopus 로고    scopus 로고
    • Antimicrobial Peptide Database.
    • Antimicrobial Peptide Database (http://aps.unmc.edu/AP/main.php).
  • 23
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • DOI 10.1016/S0092-8674(00)81099-5
    • Smith, J. J., Travis, S. M., Greenberg, E. P., and Welsh, M. J. (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid Cell 85, 229-236 (Pubitemid 26118164)
    • (1996) Cell , vol.85 , Issue.2 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 25
    • 0030949875 scopus 로고    scopus 로고
    • Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • DOI 10.1016/S0092-8674(00)81895-4
    • Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., Zasloff, M., and Wilson, J. M. (1997) Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis Cell 88, 553-560 (Pubitemid 27154420)
    • (1997) Cell , vol.88 , Issue.4 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 26
    • 79960292952 scopus 로고    scopus 로고
    • Inhibitory effects and mechanisms of physiological conditions on the activity of enantiomeric forms of an alpha-helical antibacterial peptide against bacteria
    • Huang, J. F., Hao, D. M., Chen, Y., Xu, Y. M., Tan, J. J., Huang, Y. B., Li, F., and Chen, Y. X. (2011) Inhibitory effects and mechanisms of physiological conditions on the activity of enantiomeric forms of an alpha-helical antibacterial peptide against bacteria Peptides 32, 1488-1495
    • (2011) Peptides , vol.32 , pp. 1488-1495
    • Huang, J.F.1    Hao, D.M.2    Chen, Y.3    Xu, Y.M.4    Tan, J.J.5    Huang, Y.B.6    Li, F.7    Chen, Y.X.8
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • DOI 10.1124/pr.55.1.2
    • Yeaman, M. R. and Yount, N. Y. (2003) Mechanisms of antimicrobial peptide action and resistance Pharmacol. Rev. 55, 27-55 (Pubitemid 36268398)
    • (2003) Pharmacological Reviews , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta, Biomembr. 1462, 55-70
    • (1999) Biochim. Biophys. Acta, Biomembr. , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 29
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • DOI 10.1021/bi000946l
    • Huang, H. W. (2000) Action of antimicrobial peptides: Two-state model Biochemistry 39, 8347-8352 (Pubitemid 30489931)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 30
    • 25144434489 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of human bacterial pathogens
    • Nizet, V. (2006) Antimicrobial peptide resistance mechanisms of human bacterial pathogens Curr. Issues Mol. Biol. 8, 11-26 (Pubitemid 43141388)
    • (2006) Current Issues in Molecular Biology , vol.8 , Issue.1 , pp. 11-26
    • Nizet, V.1
  • 31
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • DOI 10.1046/j.1365-2958.2002.03146.x
    • Schmidtchen, A., Frick, I. M., Andersson, E., Tapper, H., and Bjorck, L. (2002) Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37 Mol. Microbiol. 46, 157-168 (Pubitemid 35238020)
    • (2002) Molecular Microbiology , vol.46 , Issue.1 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.-M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 32
    • 77949569493 scopus 로고    scopus 로고
    • Antibiotic resistance and its cost: Is it possible to reverse resistance?
    • Andersson, D. I. and Hughes, D. (2010) Antibiotic resistance and its cost: is it possible to reverse resistance? Nat. Rev. Microbiol. 8, 260-271
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 260-271
    • Andersson, D.I.1    Hughes, D.2
  • 33
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • Brogden, K. A. (2005) Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 34
    • 84887915050 scopus 로고    scopus 로고
    • Immune modulation by multifaceted cationic host defense (antimicrobial) peptides
    • Hilchie, A. L., Wuerth, K., and Hancock, R. E. W. (2013) Immune modulation by multifaceted cationic host defense (antimicrobial) peptides Nat. Chem. Biol. 9, 761-768
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 761-768
    • Hilchie, A.L.1    Wuerth, K.2    Hancock, R.E.W.3
  • 38
    • 28044446984 scopus 로고    scopus 로고
    • Novel lysine-peptoid hybrids with antibacterial properties
    • DOI 10.1002/psc.705
    • Ryge, T. S. and Hansen, P. R. (2005) Novel lysine-peptoid hybrids with antibacterial properties J. Pept. Sci. 11, 727-734 (Pubitemid 41684259)
    • (2005) Journal of Peptide Science , vol.11 , Issue.11 , pp. 727-734
    • Ryge, T.S.1    Hansen, P.R.2
  • 40
    • 57049185166 scopus 로고    scopus 로고
    • De novo designed synthetic mimics of antimicrobial peptides
    • Scott, R. W., DeGrado, W. F., and Tew, G. N. (2008) De novo designed synthetic mimics of antimicrobial peptides Curr. Opin. Biotechnol. 19, 620-627
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 620-627
    • Scott, R.W.1    Degrado, W.F.2    Tew, G.N.3
  • 42
    • 84896524967 scopus 로고    scopus 로고
    • Structure-activity relationships among antifungal nylon-3 polymers: Identification of materials active against drug-resistant strains of Candida albicans
    • Liu, R. H., Chen, X. Y., Falk, S. P., Mowery, B. P., Karlsson, A. J., Weisblum, B., Palecek, S. P., Masters, K. S., and Gellman, S. H. (2014) Structure-activity relationships among antifungal nylon-3 polymers: Identification of materials active against drug-resistant strains of Candida albicans J. Am. Chem. Soc. 136, 4333-4342
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 4333-4342
    • Liu, R.H.1    Chen, X.Y.2    Falk, S.P.3    Mowery, B.P.4    Karlsson, A.J.5    Weisblum, B.6    Palecek, S.P.7    Masters, K.S.8    Gellman, S.H.9
  • 43
    • 84885949501 scopus 로고    scopus 로고
    • Molecular design, structures, and activity of antimicrobial peptide-mimetic polymers
    • Takahashi, H., Palermo, E. F., Yasuhara, K., Caputo, G. A., and Kuroda, K. (2013) Molecular design, structures, and activity of antimicrobial peptide-mimetic polymers Macromol. Biosci. 13, 1285-1299
    • (2013) Macromol. Biosci. , vol.13 , pp. 1285-1299
    • Takahashi, H.1    Palermo, E.F.2    Yasuhara, K.3    Caputo, G.A.4    Kuroda, K.5
  • 44
    • 84884506099 scopus 로고    scopus 로고
    • Polymers with tunable side-chain amphiphilicity as non-hemolytic antibacterial agents
    • Uppu, D., Akkapeddi, P., Manjunath, G. B., Yarlagadda, V., Hoque, J., and Haldar, J. (2013) Polymers with tunable side-chain amphiphilicity as non-hemolytic antibacterial agents Chem. Commun. 49, 9389-9391
    • (2013) Chem. Commun. , vol.49 , pp. 9389-9391
    • Uppu, D.1    Akkapeddi, P.2    Manjunath, G.B.3    Yarlagadda, V.4    Hoque, J.5    Haldar, J.6
  • 45
    • 80053955350 scopus 로고    scopus 로고
    • Block versus random amphiphilic copolymers as antibacterial agents
    • Oda, Y., Kanaoka, S., Sato, T., Aoshima, S., and Kuroda, K. (2011) Block versus random amphiphilic copolymers as antibacterial agents Biomacromolecules 12, 3581-3591
    • (2011) Biomacromolecules , vol.12 , pp. 3581-3591
    • Oda, Y.1    Kanaoka, S.2    Sato, T.3    Aoshima, S.4    Kuroda, K.5
  • 46
    • 16244400792 scopus 로고    scopus 로고
    • Amphiphilic polymethacrylate derivatives as antimicrobial agents
    • DOI 10.1021/ja044205+
    • Kuroda, K. and DeGrado, W. F. (2005) Amphiphilic polymethacrylate derivatives as antimicrobial agents J. Am. Chem. Soc. 127, 4128-4129 (Pubitemid 40463011)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.12 , pp. 4128-4129
    • Kuroda, K.1    DeGrado, W.F.2
  • 48
    • 33748929313 scopus 로고    scopus 로고
    • Role of membrane lipids in the mechanism of bacterial species selective toxicity by two α/β-antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.01.018, PII S0005273606000356
    • Epand, R. F., Schmitt, M. A., Gellman, S. H., and Epand, R. M. (2006) Role. of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides Biochim. Biophys. Acta, Biomembr. 1758, 1343-1350 (Pubitemid 44436066)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1343-1350
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Epand, R.M.4
  • 49
    • 29744438602 scopus 로고    scopus 로고
    • Bacterial species selective toxicity of two isomeric α/β- peptides: Role of membrane lipids
    • DOI 10.1080/09687860500370562
    • Epand, R. F., Schmitt, M. A., Gellman, S. H., Sen, A., Auger, M., Hughes, D. W., and Epand, R. M. (2005) Bacterial species selective toxicity of two isomeric alpha/beta-peptides: Role of membrane lipids Mol. Membr. Biol. 22, 457-469 (Pubitemid 43030902)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.6 , pp. 457-469
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Sen, A.4    Auger, M.5    Hughes, D.W.6    Epand, R.M.7
  • 50
    • 0030785114 scopus 로고    scopus 로고
    • Beta-peptides: A surprise at every turn
    • Seebach, D. and Matthews, J. L. (1997) Beta-peptides: a surprise at every turn Chem. Commun. 2015-2022
    • (1997) Chem. Commun. , pp. 2015-2022
    • Seebach, D.1    Matthews, J.L.2
  • 51
    • 0035471135 scopus 로고    scopus 로고
    • Beta-peptides: From structure to function
    • Cheng, R. P., Gellman, S. H., and DeGrado, W. F. (2001) Beta-peptides: From structure to function Chem. Rev. 101, 3219-3232
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    Degrado, W.F.3
  • 52
    • 0000466569 scopus 로고    scopus 로고
    • The biological stability of β-peptides: No interactions between α- and β-peptidic structures?
    • Hintermann, T. and Seebach, D. (1997) The biological stability of beta-peptides: No interactions between alpha- and beta-peptidic structures Chimia 51, 244-247 (Pubitemid 127386096)
    • (1997) Chimia , vol.51 , Issue.5 , pp. 244-247
    • Hintermann, T.1    Seebach, D.2
  • 53
    • 0037202210 scopus 로고    scopus 로고
    • Structure - Activity studies of 14-helical antimicrobial β-peptides: Probing the relationship between conformational stability and antimicrobial potency
    • DOI 10.1021/ja0270423
    • Raguse, T. L., Porter, E. A., Weisblum, B., and Gellman, S. H. (2002) Structure-activity studies of 14-helical antimicrobial beta-peptides: Probing the relationship between conformational stability and antimicrobial potency J. Am. Chem. Soc. 124, 12774-12785 (Pubitemid 35216001)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.43 , pp. 12774-12785
    • Raguse, T.L.1    Porter, E.A.2    Weisblum, B.3    Gellman, S.H.4
  • 54
    • 0034802565 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of antimicrobial beta-peptides
    • Liu, D. H. and DeGrado, W. F. (2001) De novo design, synthesis, and characterization of antimicrobial beta-peptides J. Am. Chem. Soc. 123, 7553-7559
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7553-7559
    • Liu, D.H.1    Degrado, W.F.2
  • 55
    • 0033616105 scopus 로고    scopus 로고
    • De novo design of antibacterial beta-peptides
    • Hamuro, Y., Schneider, J. P., and DeGrado, W. F. (1999) De novo design of antibacterial beta-peptides J. Am. Chem. Soc. 121, 12200-12201
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12200-12201
    • Hamuro, Y.1    Schneider, J.P.2    Degrado, W.F.3
  • 57
    • 67650806449 scopus 로고    scopus 로고
    • Effect of sequence and structural properties on 14-helical beta-peptide activity against Candida albicans planktonic cells and biofilms
    • Karlsson, A. J., Pomerantz, W. C., Neilsen, K. J., Gellman, S. H., and Palecek, S. P. (2009) Effect of sequence and structural properties on 14-helical beta-peptide activity against Candida albicans planktonic cells and biofilms ACS Chem. Biol. 4, 567-579
    • (2009) ACS Chem. Biol. , vol.4 , pp. 567-579
    • Karlsson, A.J.1    Pomerantz, W.C.2    Neilsen, K.J.3    Gellman, S.H.4    Palecek, S.P.5
  • 59
    • 0345074088 scopus 로고    scopus 로고
    • Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins
    • DOI 10.1046/j.1432-1033.2003.03484.x
    • Epand, R. F., Umezawa, N., Porter, E. A., Gellman, S. H., and Epand, R. M. (2003) Interactions of the antimicrobial beta-peptide beta-17 with phospholipid vesicles differ from membrane interactions of magainins Eur. J. Biochem. 270, 1240-1248 (Pubitemid 36384456)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1240-1248
    • Epand, R.F.1    Umezawa, N.2    Porter, E.A.3    Gellman, S.H.4    Epand, R.M.5
  • 60
    • 0037178109 scopus 로고    scopus 로고
    • Mimicry of host-defense peptides by unnatural oligomers: Antimicrobial β-peptides
    • DOI 10.1021/ja0260871
    • Porter, E. A., Weisblum, B., and Gellman, S. H. (2002) Mimicry of host-defense peptides by unnatural oligomers: Antimicrobial beta-peptides J. Am. Chem. Soc. 124, 7324-7330 (Pubitemid 34670441)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.25 , pp. 7324-7330
    • Porter, E.A.1    Weisblum, B.2    Gellman, S.H.3
  • 61
    • 17344384874 scopus 로고    scopus 로고
    • Antibiotics - Non-haemolytic beta-amino-acid oligomers
    • Porter, E. A., Wang, X. F., Lee, H. S., Weisblum, B., and Gellman, S. H. (2000) Antibiotics-Non-haemolytic beta-amino-acid oligomers Nature 404, 565-565
    • (2000) Nature , vol.404 , pp. 565-565
    • Porter, E.A.1    Wang, X.F.2    Lee, H.S.3    Weisblum, B.4    Gellman, S.H.5
  • 62
    • 0347417960 scopus 로고    scopus 로고
    • 3 Peptide Capable of Folding into a 12/10-Helical Secondary Structure
    • DOI 10.1002/cbic.200300698
    • Arvidsson, P. I., Ryder, N. S., Weiss, H. M., Gross, G., Kretz, O., Woessner, R., and Seebach, D. (2003) Antibiotic and hemolytic activity of a beta(2)/beta(3) peptide capable of folding into a 12/10-helical secondary structure ChemBioChem 4, 1345-1347 (Pubitemid 38036417)
    • (2003) ChemBioChem , vol.4 , Issue.12 , pp. 1345-1347
    • Arvidsson, P.I.1    Ryder, N.S.2    Weiss, H.M.3    Gross, G.4    Kretz, O.5    Woessner, R.6    Seebach, D.7
  • 63
    • 0023055775 scopus 로고
    • New hydrophiliity scale derived from high-performance liquid-chromatography peptide retention data - Correlation of predicted surface residues with antigenicity and x-ray derived accessible sites
    • Parker, J. M. R., Guo, D., and Hodges, R. S. (1986) New hydrophiliity scale derived from high-performance liquid-chromatography peptide retention data-correlation of predicted surface residues with antigenicity and x-ray derived accessible sites Biochemistry 25, 5425-5432
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.R.1    Guo, D.2    Hodges, R.S.3
  • 64
    • 0020427613 scopus 로고
    • The isolation of peptides by high-performance liquid chromatography using predicted elution positions
    • DOI 10.1016/0003-2697(82)90238-X
    • Browne, C. A., Bennett, H. P. J., and Solomon, S. (1982) The isolation of peptides by high-performance liquid-chromatography using predicted elution positions Anal. Biochem. 124, 201-208 (Pubitemid 13250026)
    • (1982) Analytical Biochemistry , vol.124 , Issue.1 , pp. 201-208
    • Browne, C.A.1    Bennett, H.P.J.2    Solomon, S.3
  • 65
    • 0019631920 scopus 로고
    • The behavior of peptides on reverse-phase supports during high-pressure liquid-chromatorraphy
    • Wilson, K. J., Honegger, A., Stotzel, R. P., and Hughes, G. J. (1981) The behavior of peptides on reverse-phase supports during high-pressure liquid-chromatorraphy Biochem. J. 199, 31-41
    • (1981) Biochem. J. , vol.199 , pp. 31-41
    • Wilson, K.J.1    Honegger, A.2    Stotzel, R.P.3    Hughes, G.J.4
  • 66
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewski, L. H., Jelokhani-Niaraki, M., Farmer, S. W., Lix, B., Kay, C. M., Sykes, B. D., Hancock, R. E. W., and Hodges, R. S. (1999) Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity J. Biol. Chem. 274, 13181-13192
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondejewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.W.7    Hodges, R.S.8
  • 67
    • 27744493759 scopus 로고    scopus 로고
    • Correlation between the activities of α-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times
    • DOI 10.1016/j.peptides.2005.04.007, PII S0196978105001774
    • Kim, S., Kim, S. S., and Lee, B. J. (2005) Correlation between the activities of alpha-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times Peptides 26, 2050-2056 (Pubitemid 41584066)
    • (2005) Peptides , vol.26 , Issue.11 , pp. 2050-2056
    • Kim, S.1    Kim, S.S.2    Lee, B.J.3
  • 69
    • 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. (1987) 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. U.S.A. 84, 5449-5453 (Pubitemid 17129018)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.15 , pp. 5449-5453
    • Zasloff, M.1
  • 70
    • 0027135521 scopus 로고
    • Sequences of two cDNA clones from the medfly ceratitis-capitata encoding antibacterial peptides of the ceropin family
    • Rosetto, M., Manetti, A. G. O., Marchini, D., Dallai, R., Telford, J. L., and Baldari, C. T. (1993) Sequences of two cDNA clones from the medfly ceratitis-capitata encoding antibacterial peptides of the ceropin family Gene 134, 241-243
    • (1993) Gene , vol.134 , pp. 241-243
    • Rosetto, M.1    Manetti, A.G.O.2    Marchini, D.3    Dallai, R.4    Telford, J.L.5    Baldari, C.T.6
  • 71
    • 0028009870 scopus 로고
    • Isolation and structure of novel defensive peptides from frog skin
    • Mor, A. and Nicolas, P. (1994) Isolation and structure of novel defensive pepptides from frog-skin Eur. J. Biochem. 219, 145-154 (Pubitemid 24053627)
    • (1994) European Journal of Biochemistry , vol.219 , Issue.1-2 , pp. 145-154
    • Mor, A.1    Nicolas, P.2
  • 72
    • 0015787259 scopus 로고
    • Structure of melittin isolated from two species of honey bees
    • Kreil, G. (1973) Structure of melittin isolated from two species of honey bees FEBS Lett. 33, 241-244
    • (1973) FEBS Lett. , vol.33 , pp. 241-244
    • Kreil, G.1
  • 73
    • 0028834275 scopus 로고
    • CDNA sequences of three sheep myeloid cathelicidins
    • Bagella, L., Scocchi, M., and Zanetti, M. (1995) cDNA sequences of three sheep myeloid cathelicidins FEBS Lett. 376, 225-228
    • (1995) FEBS Lett. , vol.376 , pp. 225-228
    • Bagella, L.1    Scocchi, M.2    Zanetti, M.3
  • 74
    • 0026666034 scopus 로고
    • Purification and characterization of a novel antimicrobial peptide from maize(Zea-mays L.) kernels
    • Duvick, J. P., Rood, T., Rao, A. G., and Marshak, D. R. (1992) Purification and characterization of a novel antimicrobial peptide from maize(Zea-mays L.) kernels J. Biol. Chem. 267, 18814-18820
    • (1992) J. Biol. Chem. , vol.267 , pp. 18814-18820
    • Duvick, J.P.1    Rood, T.2    Rao, A.G.3    Marshak, D.R.4
  • 76
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • DOI 10.1021/bi9619987
    • Wieprecht, T., Dathe, M., Beyermann, M., Krause, E., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997) Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes Biochemistry 36, 6124-6132 (Pubitemid 27257879)
    • (1997) Biochemistry , vol.36 , Issue.20 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 77
  • 78
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y. X., Mant, C. T., Farmer, S. W., Hancock, R. E. W., Vasil, M. L., and Hodges, R. S. (2005) Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index J. Biol. Chem. 280, 12316-12329
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.X.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 79
    • 0023735907 scopus 로고
    • Synthetic magainin analogs with improved antimicrobial activity
    • Chen, H. C., Brown, J. H., Morell, J. L., and Huang, C. M. (1988) Synthetic magainin analogs with improved antimicrobial activity FEBS Lett. 236, 462-466
    • (1988) FEBS Lett. , vol.236 , pp. 462-466
    • Chen, H.C.1    Brown, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 80
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides
    • Zhang, L. J., Benz, R., and Hancock, R. E. W. (1999) Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides Biochemistry 38, 8102-8111
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.J.1    Benz, R.2    Hancock, R.E.W.3
  • 82
    • 17844395169 scopus 로고    scopus 로고
    • Application of microwave irradiation to the synthesis of 14-helical β-peptides
    • DOI 10.1021/ol0501727
    • Murray, J. K. and Gellman, S. H. (2005) Application of microwave irradiation to the synthesis of 14-helical beta-peptides Org. Lett. 7, 1517-1520 (Pubitemid 40585920)
    • (2005) Organic Letters , vol.7 , Issue.8 , pp. 1517-1520
    • Murray, J.K.1    Gellman, S.H.2


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