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Volumn 77, Issue 2, 2011, Pages 107-116

Antimicrobial β-Peptides and α-Peptoids

Author keywords

peptoids; peptide; Antibiotic resistance; Antimicrobial peptides; Drug design; Peptidomimetics

Indexed keywords

ALPHA AMINO ACID; ANTIMICROBIAL ALPHA PEPTOID; ANTIMICROBIAL BETA PEPTIDE; BACTERIAL PROTEIN; BETA AMINO ACID; CERAGENIN; CERASHIELD; DAPTOMYCIN; LTX 109; LYTIXAR; OMIGANAN; PEPTIDOMIMETIC AGENT; PMX 30036; POLYMYXIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 79251509263     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2010.01067.x     Document Type: Review
Times cited : (109)

References (96)
  • 1
    • 13844254907 scopus 로고    scopus 로고
    • Outpatient antibiotic use in Europe and association with resistance: a cross-national database study
    • Goossens H., Ferech M., Stichele R.V., Elseviers M. (2005) Outpatient antibiotic use in Europe and association with resistance: a cross-national database study. Lancet;365:579-587.
    • (2005) Lancet , vol.365 , pp. 579-587
    • Goossens, H.1    Ferech, M.2    Stichele, R.V.3    Elseviers, M.4
  • 2
    • 58149187882 scopus 로고    scopus 로고
    • APD2: the updated antimicrobial peptide database and its application in peptide design
    • Wang G., Li X., Wang Z. (2009) APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res;37:D933-D937.
    • (2009) Nucleic Acids Res , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 3
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. (2003) Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol;3:710-720.
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 5
    • 67449132232 scopus 로고    scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity (Reprinted from Nature, vol 292, pg 246-248, 1981)
    • Steiner H., Hultmark D., Engstrom A., Bennich H., Boman H.G. (2009) Sequence and specificity of two antibacterial proteins involved in insect immunity (Reprinted from Nature, vol 292, pg 246-248, 1981). J Immunol;182:6635-6637.
    • (2009) J Immunol , vol.182 , pp. 6635-6637
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 6
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., Wieprecht T. (1999) Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim Biophys Acta;1462:71-87.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 8
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides - a systematic study of the effects of structural and physical properties on biological activity
    • Giangaspero A., Sandri L., Tossi A. (2001) Amphipathic alpha helical antimicrobial peptides - a systematic study of the effects of structural and physical properties on biological activity. Eur J Biochem;268:5589-5600.
    • (2001) Eur J Biochem , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 9
    • 41349103509 scopus 로고    scopus 로고
    • Antimicrobial activities of twenty lysine-peptoid hybrids against clinically relevant bacteria and fungi
    • Ryge T.S., Frimodt-Moller N., Hansen P.R. (2008) Antimicrobial activities of twenty lysine-peptoid hybrids against clinically relevant bacteria and fungi. Chemotherapy;54:152-156.
    • (2008) Chemotherapy , vol.54 , pp. 152-156
    • Ryge, T.S.1    Frimodt-Moller, N.2    Hansen, P.R.3
  • 10
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E.W., Sahl H.G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol;24:1551-1557.
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 11
    • 79251521467 scopus 로고    scopus 로고
    • Clinical development of peptide antibiotics
    • Jenssen H. (2009) Clinical development of peptide antibiotics. PharmaChem;10:22-26.
    • (2009) PharmaChem , vol.10 , pp. 22-26
    • Jenssen, H.1
  • 12
    • 77950482392 scopus 로고    scopus 로고
    • Therapeutic potential of HDPs as immunomodulatory agents
    • Jenssen H., Hancock R.E.W. (2010) Therapeutic potential of HDPs as immunomodulatory agents. Methods Mol Biol;618:329-347.
    • (2010) Methods Mol Biol , vol.618 , pp. 329-347
    • Jenssen, H.1    Hancock, R.E.W.2
  • 13
    • 0032877184 scopus 로고    scopus 로고
    • Therapeutic peptides revisited
    • Latham P.W. (1999) Therapeutic peptides revisited. Nat Biotechnol;17:755-757.
    • (1999) Nat Biotechnol , vol.17 , pp. 755-757
    • Latham, P.W.1
  • 14
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. (2003) Antibacterial peptides: basic facts and emerging concepts. J Intern Med;254:197-215.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 15
    • 67649295450 scopus 로고    scopus 로고
    • Antimicrobial peptide mimics for improved therapeutic properties
    • Rotem S., Mor A. (2009) Antimicrobial peptide mimics for improved therapeutic properties. Biochim Biophys Acta;1788:1582-1592.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1582-1592
    • Rotem, S.1    Mor, A.2
  • 16
    • 0034025733 scopus 로고    scopus 로고
    • Design and synthesis of novel antimicrobial pseudopeptides with selective membrane-perturbation activity
    • Lee K.H., Oh J.E. (2000) Design and synthesis of novel antimicrobial pseudopeptides with selective membrane-perturbation activity. Bioorg Med Chem;8:833-839.
    • (2000) Bioorg Med Chem , vol.8 , pp. 833-839
    • Lee, K.H.1    Oh, J.E.2
  • 17
    • 9444226868 scopus 로고    scopus 로고
    • The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components
    • Seebach D., Beck A.K., Bierbaum D.J. (2004) The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components. Chem Biodivers;1:1111-1239.
    • (2004) Chem Biodivers , vol.1 , pp. 1111-1239
    • Seebach, D.1    Beck, A.K.2    Bierbaum, D.J.3
  • 18
    • 17344384874 scopus 로고    scopus 로고
    • Non-haemolytic beta-amino-acid oligomers
    • Erratum: 2000,405(6784):298.
    • Porter E.A., Wang X., Lee H.S., Weisblum B., Gellman S.H. (2000) Non-haemolytic beta-amino-acid oligomers. Nature;404:565. Erratum: 2000, 405(6784):298.
    • (2000) Nature , vol.404 , pp. 565
    • Porter, E.A.1    Wang, X.2    Lee, H.S.3    Weisblum, B.4    Gellman, S.H.5
  • 19
    • 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.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 20
    • 0033616105 scopus 로고    scopus 로고
    • De novo design of antibacterial beta-peptides
    • Hamuro Y., Schneider J.P., 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
  • 21
    • 0031539136 scopus 로고    scopus 로고
    • Helix bundles and coiled coils in alpha-spectrin and tropomyosin: a theoretical CD study
    • Bode K.A., Applequist J. (1997) Helix bundles and coiled coils in alpha-spectrin and tropomyosin: a theoretical CD study. Biopolymers;42:855-860.
    • (1997) Biopolymers , vol.42 , pp. 855-860
    • Bode, K.A.1    Applequist, J.2
  • 23
    • 0030461803 scopus 로고    scopus 로고
    • Beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers
    • Appella D.H., Christianson L.A., Karle I.L., Powell D.R., Gellman S.H. (1996) Beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers. J Am Chem Soc;118:13071-13072.
    • (1996) J Am Chem Soc , vol.118 , pp. 13071-13072
    • Appella, D.H.1    Christianson, L.A.2    Karle, I.L.3    Powell, D.R.4    Gellman, S.H.5
  • 25
    • 0033577324 scopus 로고    scopus 로고
    • Formation of short, stable helices in aqueous solution by β-amino acid hexamers
    • Appella D.H., Barchi J.J. Jr, Durell S.R., Gellman S.H. (1999) Formation of short, stable helices in aqueous solution by β-amino acid hexamers. J Am Chem Soc;121:2309-2310.
    • (1999) J Am Chem Soc , vol.121 , pp. 2309-2310
    • Appella, D.H.1    Barchi Jr, J.J.2    Durell, S.R.3    Gellman, S.H.4
  • 27
    • 52049107912 scopus 로고    scopus 로고
    • Hybrid alphagamma polypeptides: structural characterization of a C12/C10 helix with alternating hydrogen-bond polarity
    • Vasudev P.G., Chatterjee S., Ananda K., Shamala N., Balaram P. (2008) Hybrid alphagamma polypeptides: structural characterization of a C12/C10 helix with alternating hydrogen-bond polarity. Angew Chem Int Ed Engl;47:6430-6432.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 6430-6432
    • Vasudev, P.G.1    Chatterjee, S.2    Ananda, K.3    Shamala, N.4    Balaram, P.5
  • 29
    • 0031468514 scopus 로고    scopus 로고
    • Antiparallel sheet formation in beta-peptide foldamers: effects of beta-amino acid substitution on conformational preference
    • Krauthauser S., Christianson L.A., Powell D.R., Gellman S.H. (1997) Antiparallel sheet formation in beta-peptide foldamers: effects of beta-amino acid substitution on conformational preference. J Am Chem Soc;119:11719-11720.
    • (1997) J Am Chem Soc , vol.119 , pp. 11719-11720
    • Krauthauser, S.1    Christianson, L.A.2    Powell, D.R.3    Gellman, S.H.4
  • 31
    • 0002929747 scopus 로고
    • Speculations on the design of non-peptidic peptidomimetics
    • Farmer P.S., Ariens E.J. (1982) Speculations on the design of non-peptidic peptidomimetics. Trends Pharmacol Sci;3:362-365.
    • (1982) Trends Pharmacol Sci , vol.3 , pp. 362-365
    • Farmer, P.S.1    Ariens, E.J.2
  • 32
    • 0000908874 scopus 로고
    • Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis
    • Zuckermann R.N., Kerr J.M., Kent S.B.H., Moos W.H. (1992) Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis. J Am Chem Soc;114:10646-10647.
    • (1992) J Am Chem Soc , vol.114 , pp. 10646-10647
    • Zuckermann, R.N.1    Kerr, J.M.2    Kent, S.B.H.3    Moos, W.H.4
  • 34
    • 34249070808 scopus 로고    scopus 로고
    • Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action
    • Zhu W.L., Song Y.M., Park Y., Park K.H., Yang S.T., Kim J.I., Park I.S., Hahm K.S., Shin S.Y. (2007) Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action. Biochim Biophys Acta;1768:1506-1517.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1506-1517
    • Zhu, W.L.1    Song, Y.M.2    Park, Y.3    Park, K.H.4    Yang, S.T.5    Kim, J.I.6    Park, I.S.7    Hahm, K.S.8    Shin, S.Y.9
  • 35
    • 0141888597 scopus 로고    scopus 로고
    • Helical peptoid mimics of magainin-2 amide
    • Patch J.A., Barron A.E. (2003) Helical peptoid mimics of magainin-2 amide. J Am Chem Soc;125:12092-12093.
    • (2003) J Am Chem Soc , vol.125 , pp. 12092-12093
    • Patch, J.A.1    Barron, A.E.2
  • 36
    • 47749116861 scopus 로고    scopus 로고
    • Synthetic antimicrobial peptidomimetics with therapeutic potential
    • Haug B.E., Stensen W., Kalaaji M., Rekdal O., Svendsen J.S. (2008) Synthetic antimicrobial peptidomimetics with therapeutic potential. J Med Chem;51:4306-4314.
    • (2008) J Med Chem , vol.51 , pp. 4306-4314
    • Haug, B.E.1    Stensen, W.2    Kalaaji, M.3    Rekdal, O.4    Svendsen, J.S.5
  • 37
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. (1995) Peptide antibiotics and their role in innate immunity. Annu Rev Immunol;13:61-92.
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 38
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol;3:238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 39
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock R.E.W., Rozek A. (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol Lett;206:143-149.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 40
    • 33748940257 scopus 로고    scopus 로고
    • Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering
    • Salditt T., Li C.H., Spaar A. (2006) Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering. Biochim Biophys Acta;1758:1483-1498.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1483-1498
    • Salditt, T.1    Li, C.H.2    Spaar, A.3
  • 41
    • 0032752132 scopus 로고    scopus 로고
    • Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria
    • Scott M.G., Gold M.R., Hancock R.E.W. (1999) Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria. Infect Immun;67:6445-6453.
    • (1999) Infect Immun , vol.67 , pp. 6445-6453
    • Scott, M.G.1    Gold, M.R.2    Hancock, R.E.W.3
  • 42
    • 14844312173 scopus 로고    scopus 로고
    • Asymmetric synthesis of beta-amino acids and alpha-substituted beta-amino acids
    • Cardillo G., Tomasini C. (1996) Asymmetric synthesis of beta-amino acids and alpha-substituted beta-amino acids. Chem Soc Rev;25:117-128.
    • (1996) Chem Soc Rev , vol.25 , pp. 117-128
    • Cardillo, G.1    Tomasini, C.2
  • 43
    • 0036897824 scopus 로고    scopus 로고
    • Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers
    • Patch J.A., Barron A.E. (2002) Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers. Curr Opin Chem Biol;6:872-877.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 872-877
    • Patch, J.A.1    Barron, A.E.2
  • 44
    • 3042812727 scopus 로고    scopus 로고
    • Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones
    • Schmitt M.A., Weisblum B., Gellman S.H. (2004) Unexpected relationships between structure and function in alpha, beta-peptides: antimicrobial foldamers with heterogeneous backbones. J Am Chem Soc;126:6848-6849.
    • (2004) J Am Chem Soc , vol.126 , pp. 6848-6849
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 45
    • 0141670369 scopus 로고    scopus 로고
    • Side-chain control of beta-peptide secondary structures
    • Martinek T.A., Fulop F. (2003) Side-chain control of beta-peptide secondary structures. Eur J Biochem;270:3657-3666.
    • (2003) Eur J Biochem , vol.270 , pp. 3657-3666
    • Martinek, T.A.1    Fulop, F.2
  • 46
    • 0037427276 scopus 로고    scopus 로고
    • Helix macrodipole control of beta 3 peptide 14-helix stability in water
    • Hart S.A., Bahadoor A.B., Matthews E.E., Qiu X.J., Schepartz A. (2003) Helix macrodipole control of beta 3 peptide 14-helix stability in water. J Am Chem Soc;125:4022-4023.
    • (2003) J Am Chem Soc , vol.125 , pp. 4022-4023
    • Hart, S.A.1    Bahadoor, A.B.2    Matthews, E.E.3    Qiu, X.J.4    Schepartz, A.5
  • 47
    • 48149115235 scopus 로고    scopus 로고
    • Stable hairpins with beta-peptides: route to tackle protein-protein interactions
    • Baldauf C., Pisabarro M.T. (2008) Stable hairpins with beta-peptides: route to tackle protein-protein interactions. J Phys Chem B;112:7581-7591.
    • (2008) J Phys Chem B , vol.112 , pp. 7581-7591
    • Baldauf, C.1    Pisabarro, M.T.2
  • 48
    • 0037202210 scopus 로고    scopus 로고
    • Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency
    • Raguse T.L., Porter E.A., Weisblum B., 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.
    • (2002) J Am Chem Soc , vol.124 , pp. 12774-12785
    • Raguse, T.L.1    Porter, E.A.2    Weisblum, B.3    Gellman, S.H.4
  • 49
    • 33846251959 scopus 로고    scopus 로고
    • Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of alpha/beta-peptides
    • Schmitt M.A., Weisblum B., Gellman S.H. (2007) Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of alpha/beta-peptides. J Am Chem Soc;129:417-428.
    • (2007) J Am Chem Soc , vol.129 , pp. 417-428
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 51
    • 0035471135 scopus 로고    scopus 로고
    • beta-Peptides: from structure to function
    • Cheng R.P., Gellman S.H., 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
    • 0034802565 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of antimicrobial beta-peptides
    • Liu D.H., 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
  • 53
    • 0026677582 scopus 로고
    • Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices
    • Park N.G., Lee S., Oishi O., Aoyagi H., Iwanaga S., Yamashita S., Ohno M. (1992) Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices. Biochemistry;31:12241-12247.
    • (1992) Biochemistry , vol.31 , pp. 12241-12247
    • Park, N.G.1    Lee, S.2    Oishi, O.3    Aoyagi, H.4    Iwanaga, S.5    Yamashita, S.6    Ohno, M.7
  • 54
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J., Cho Y., Dinh N.N., Waring A.J., Lehrer R.I. (1998) Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother;42:2206-2214.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 55
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek A., Friedrich C.L., Hancock R.E.W. (2000) Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry;39:15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.W.3
  • 56
    • 0033603830 scopus 로고    scopus 로고
    • Synthesis and structural characterization of helix-forming beta-peptides: trans-2-aminocyclopentanecarboxylic acid oligomers
    • Appella D.H., Christianson L.A., Klein D.A., Richards M.R., Powell D.R., Gellman S.H. (1999) Synthesis and structural characterization of helix-forming beta-peptides: trans-2-aminocyclopentanecarboxylic acid oligomers. J Am Chem Soc;121:7574-7581.
    • (1999) J Am Chem Soc , vol.121 , pp. 7574-7581
    • Appella, D.H.1    Christianson, L.A.2    Klein, D.A.3    Richards, M.R.4    Powell, D.R.5    Gellman, S.H.6
  • 57
    • 0037178109 scopus 로고    scopus 로고
    • Mimicry of host-defense peptides by unnatural oligomers: antimicrobial beta-peptides
    • Porter E.A., Weisblum B., Gellman S.H. (2002) Mimicry of host-defense peptides by unnatural oligomers: antimicrobial beta-peptides. J Am Chem Soc;124:7324-7330.
    • (2002) J Am Chem Soc , vol.124 , pp. 7324-7330
    • Porter, E.A.1    Weisblum, B.2    Gellman, S.H.3
  • 58
    • 72749105356 scopus 로고    scopus 로고
    • Antimicrobial mechanism of pore-forming protegrin peptides: 100 pores to kill E. coli
    • Bolintineanu D., Hazrati E., Davis H.T., Lehrer R.I., Kaznessis Y.N. (2010) Antimicrobial mechanism of pore-forming protegrin peptides: 100 pores to kill E. coli. Peptides;31:1-8.
    • (2010) Peptides , vol.31 , pp. 1-8
    • Bolintineanu, D.1    Hazrati, E.2    Davis, H.T.3    Lehrer, R.I.4    Kaznessis, Y.N.5
  • 59
    • 0026788013 scopus 로고
    • Mechanism of magainin 2a induced permeabilization of phospholipid vesicles
    • Grant E. Jr, Beeler T.J., Taylor K.M., Gable K., Roseman M.A. (1992) Mechanism of magainin 2a induced permeabilization of phospholipid vesicles. Biochemistry;31:9912-9918.
    • (1992) Biochemistry , vol.31 , pp. 9912-9918
    • Grant Jr, E.1    Beeler, T.J.2    Taylor, K.M.3    Gable, K.4    Roseman, M.A.5
  • 61
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions
    • Schibli D.J., Epand R.F., Vogel H.J., Epand R.M. (2002) Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochem Cell Biol;80:667-677.
    • (2002) Biochem Cell Biol , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 62
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study
    • Oren Z., Shai Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry;36:1826-1835.
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 64
    • 0035068010 scopus 로고    scopus 로고
    • All-D-cecropin B: synthesis, conformation, lipopolysaccharide binding, and antibacterial activity
    • Bland J.M., De Lucca A.J., Jacks T.J., Vigo C.B. (2001) All-D-cecropin B: synthesis, conformation, lipopolysaccharide binding, and antibacterial activity. Mol Cell Biochem;218:105-111.
    • (2001) Mol Cell Biochem , vol.218 , pp. 105-111
    • Bland, J.M.1    De Lucca, A.J.2    Jacks, T.J.3    Vigo, C.B.4
  • 66
    • 0347417960 scopus 로고    scopus 로고
    • Antibiotic and hemolytic activity of a beta(2)/beta(3) peptide capable of folding into a 12/10-helical secondary structure
    • Arvidsson P.I., Ryder N.S., Weiss H.M., Gross G., Kretz O., Woessner R., 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.
    • (2003) Chembiochem , vol.4 , 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
  • 68
    • 77249095412 scopus 로고    scopus 로고
    • Antimicrobial activity of small beta-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides
    • Hansen T., Alst T., Havelkova M., Strom M.B. (2010) Antimicrobial activity of small beta-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides. J Med Chem;53:595-606.
    • (2010) J Med Chem , vol.53 , pp. 595-606
    • Hansen, T.1    Alst, T.2    Havelkova, M.3    Strom, M.B.4
  • 69
    • 34547948394 scopus 로고    scopus 로고
    • Conformational study of short peptoid models for future applications as potent antimicrobial compounds
    • Nandel F.S., Saini A. (2007) Conformational study of short peptoid models for future applications as potent antimicrobial compounds. Macromol Theory Simul;16:295-303.
    • (2007) Macromol Theory Simul , vol.16 , pp. 295-303
    • Nandel, F.S.1    Saini, A.2
  • 70
    • 64149103140 scopus 로고    scopus 로고
    • Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function
    • Fowler S.A., Blackwell H.E. (2009) Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function. Org Biomol Chem;7:1508-1524.
    • (2009) Org Biomol Chem , vol.7 , pp. 1508-1524
    • Fowler, S.A.1    Blackwell, H.E.2
  • 73
    • 0034835809 scopus 로고    scopus 로고
    • Peptoid oligomers with alpha-chiral, aromatic side chains: sequence requirements for the formation of stable peptoid helices
    • Wu C.W., Sanborn T.J., Huang K., Zuckermann R.N., Barron A.E. (2001) Peptoid oligomers with alpha-chiral, aromatic side chains: sequence requirements for the formation of stable peptoid helices. J Am Chem Soc;123:6778-6784.
    • (2001) J Am Chem Soc , vol.123 , pp. 6778-6784
    • Wu, C.W.1    Sanborn, T.J.2    Huang, K.3    Zuckermann, R.N.4    Barron, A.E.5
  • 74
    • 0036015849 scopus 로고    scopus 로고
    • Toward the synthesis of artificial proteins: the discovery of an amphiphilic helical peptoid assembly
    • Burkoth T.S., Beausoleil E., Kaur S., Tang D.Z., Cohen F.E., Zuckermann R.N. (2002) Toward the synthesis of artificial proteins: the discovery of an amphiphilic helical peptoid assembly. Chem Biol;9:647-654.
    • (2002) Chem Biol , vol.9 , pp. 647-654
    • Burkoth, T.S.1    Beausoleil, E.2    Kaur, S.3    Tang, D.Z.4    Cohen, F.E.5    Zuckermann, R.N.6
  • 75
    • 70450177277 scopus 로고    scopus 로고
    • New strategies for the design of folded peptoids revealed by a survey of noncovalent interactions in model systems
    • Gorske B.C., Stringer J.R., Bastian B.L., Fowler S.A., Blackwell H.E. (2009) New strategies for the design of folded peptoids revealed by a survey of noncovalent interactions in model systems. J Am Chem Soc;131:16555-16567.
    • (2009) J Am Chem Soc , vol.131 , pp. 16555-16567
    • Gorske, B.C.1    Stringer, J.R.2    Bastian, B.L.3    Fowler, S.A.4    Blackwell, H.E.5
  • 77
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin - a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • Asthana N., Yadav S.P., Ghosh J.K. (2004) Dissection of antibacterial and toxic activity of melittin - a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J Biol Chem;279:55042-55050.
    • (2004) J Biol Chem , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 78
    • 28044446984 scopus 로고    scopus 로고
    • Novel lysine-peptoid hybrids with antibacterial properties
    • Ryge T.S., Hansen P.R. (2005) Novel lysine-peptoid hybrids with antibacterial properties. J Pept Sci;11:727-734.
    • (2005) J Pept Sci , vol.11 , pp. 727-734
    • Ryge, T.S.1    Hansen, P.R.2
  • 82
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • Wiegand I., Hilpert K., Hancock R.E.W. (2008) Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat Protoc;3:163-175.
    • (2008) Nat Protoc , vol.3 , pp. 163-175
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.W.3
  • 86
    • 33847258359 scopus 로고    scopus 로고
    • Antibacterial surfaces on expanded polytetrafluoroethylene; penicillin attachment
    • Aumsuwan N., Heinhorst S., Urban M.W. (2007) Antibacterial surfaces on expanded polytetrafluoroethylene; penicillin attachment. Biomacromolecules;8:713-718.
    • (2007) Biomacromolecules , vol.8 , pp. 713-718
    • Aumsuwan, N.1    Heinhorst, S.2    Urban, M.W.3
  • 89
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: an overview of a promising class of therapeutics
    • Giuliani A., Pirri G., Nicoletto S.F. (2007) Antimicrobial peptides: an overview of a promising class of therapeutics. Cent Eur J Biol;2:1-33.
    • (2007) Cent Eur J Biol , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.F.3
  • 90
    • 69949191216 scopus 로고    scopus 로고
    • Antimicrobial and antifungal activities of a novel cationic antimicrobial peptide, omiganan, in experimental skin colonisation models
    • Rubinchik E., Dugourd D., Algara T., Pasetka C., Friedland H.D. (2009) Antimicrobial and antifungal activities of a novel cationic antimicrobial peptide, omiganan, in experimental skin colonisation models. Int J Antimicrob Agents;34:457-461.
    • (2009) Int J Antimicrob Agents , vol.34 , pp. 457-461
    • Rubinchik, E.1    Dugourd, D.2    Algara, T.3    Pasetka, C.4    Friedland, H.D.5
  • 92
    • 34247140867 scopus 로고    scopus 로고
    • Antimicrobial activities of ceragenins against clinical isolates of resistant Staphylococcus aureus
    • Chin J.N., Rybak M.J., Cheung C.M., Savage P.B. (2007) Antimicrobial activities of ceragenins against clinical isolates of resistant Staphylococcus aureus. Antimicrob Agents Chemother;51:1268-1273.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1268-1273
    • Chin, J.N.1    Rybak, M.J.2    Cheung, C.M.3    Savage, P.B.4
  • 93
    • 0031062621 scopus 로고    scopus 로고
    • Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • Gesell J., Zasloff M., Opella S.J. (1997) Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J Biomol NMR;9:127-135.
    • (1997) J Biomol NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 94
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., Peitsch M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 95
    • 34247362490 scopus 로고    scopus 로고
    • Foldamers as versatile frameworks for the design and evolution of function
    • Goodman C.M., Choi S., Shandler S., DeGrado W.F. (2007) Foldamers as versatile frameworks for the design and evolution of function. Nat Chem Biol;3:252-262.
    • (2007) Nat Chem Biol , vol.3 , pp. 252-262
    • Goodman, C.M.1    Choi, S.2    Shandler, S.3    DeGrado, W.F.4
  • 96
    • 57349160853 scopus 로고    scopus 로고
    • Theoretical analysis of secondary structures of beta-peptides
    • Wu Y.D., Han W., Wang D.P., Gao Y., Zhao Y.L. (2008) Theoretical analysis of secondary structures of beta-peptides. Acc Chem Res;41:1418-1427.
    • (2008) Acc Chem Res , vol.41 , pp. 1418-1427
    • Wu, Y.D.1    Han, W.2    Wang, D.P.3    Gao, Y.4    Zhao, Y.L.5


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