메뉴 건너뛰기




Volumn 13, Issue 5, 2006, Pages 531-538

Mimicking Helical Antibacterial Peptides with Nonpeptidic Folding Oligomers

Author keywords

CHEMBIO; MICROBIO

Indexed keywords

BACTERIA (MICROORGANISMS); MAMMALIA; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; NEGIBACTERIA; POSIBACTERIA;

EID: 33746888689     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.03.009     Document Type: Article
Times cited : (126)

References (39)
  • 1
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann E. Bee and wasp venoms. Science 177 (1972) 314-322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 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 84 (1987) 5449-5453
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 3
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 8
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 9
    • 0031059377 scopus 로고    scopus 로고
    • Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial activity of amphipathic helical peptides
    • McDonald D.L., Beyermann M., and Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial activity of amphipathic helical peptides. FEBS Lett. 403 (1997) 208-212
    • (1997) FEBS Lett. , vol.403 , pp. 208-212
    • McDonald, D.L.1    Beyermann, M.2    Bienert, M.3
  • 10
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 11
    • 13944277208 scopus 로고    scopus 로고
    • β-Peptides, γ-peptides and isosteric backbones: new scaffolds with controlled shapes for mimicking protein secondary structure elements
    • Nielsen P.E. (Ed), Wiley-VCH Verlag, Weinheim, Germany
    • Guichard G. β-Peptides, γ-peptides and isosteric backbones: new scaffolds with controlled shapes for mimicking protein secondary structure elements. In: Nielsen P.E. (Ed). Pseudopeptides in Drug Development (2004), Wiley-VCH Verlag, Weinheim, Germany 33-120
    • (2004) Pseudopeptides in Drug Development , pp. 33-120
    • Guichard, G.1
  • 12
    • 9444226868 scopus 로고    scopus 로고
    • The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components
    • Seebach D., Beck A.K., and Bierbaum D.J. The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components. Chem. Biodiv. 1 (2004) 1111-1239
    • (2004) Chem. Biodiv. , vol.1 , pp. 1111-1239
    • Seebach, D.1    Beck, A.K.2    Bierbaum, D.J.3
  • 13
    • 0035471135 scopus 로고    scopus 로고
    • β-Peptides: from structure to function
    • Cheng R.P., Gellman S.H., and DeGrado W.F. β-Peptides: from structure to function. Chem. Rev. 101 (2001) 3219-3232
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    DeGrado, W.F.3
  • 14
    • 17344384874 scopus 로고    scopus 로고
    • Non-haemolytic beta-amino-acid oligomers
    • Erratum: Nature 405(6784), 298
    • Porter E.A., Wang X., Lee H.S., Weisblum B., and Gellman S.H. Non-haemolytic beta-amino-acid oligomers. Nature 404 (2000) 565 Erratum: Nature 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
  • 15
    • 0037178109 scopus 로고    scopus 로고
    • Mimicry of host-defense peptides by unnatural oligomers: antimicrobial beta-peptides
    • Porter E.A., Weisblum B., and Gellman S.H. Mimicry of host-defense peptides by unnatural oligomers: antimicrobial beta-peptides. J. Am. Chem. Soc. 124 (2002) 7324-7330
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7324-7330
    • Porter, E.A.1    Weisblum, B.2    Gellman, S.H.3
  • 16
    • 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., and Gellman S.H. Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency. J. Am. Chem. Soc. 124 (2002) 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
  • 17
    • 0034802565 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of antimicrobial β-peptides
    • Liu D., and DeGrado W.F. De novo design, synthesis, and characterization of antimicrobial β-peptides. J. Am. Chem. Soc. 123 (2001) 7553-7559
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7553-7559
    • Liu, D.1    DeGrado, W.F.2
  • 18
    • 0347417960 scopus 로고    scopus 로고
    • Antibiotic and hemolytic activity of a β2/β3 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., and Seebach D. Antibiotic and hemolytic activity of a β2/β3 peptide capable of folding into a 12/10-helical secondary structure. ChemBioChem 4 (2003) 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
  • 19
    • 0141888597 scopus 로고    scopus 로고
    • Helical peptoid mimics of magainin-2 amide
    • Patch J.A., and Barron A.E. Helical peptoid mimics of magainin-2 amide. J. Am. Chem. Soc. 125 (2003) 12092-12093
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12092-12093
    • Patch, J.A.1    Barron, A.E.2
  • 21
    • 0036944713 scopus 로고    scopus 로고
    • Helix forming oligoureas: temperature-dependent NMR, structure determination and circular dichroism of a nonomer with functionalised side chain
    • Hemmerlin C., Marraud M., Rognan D., Graff R., Semetey V., Briand J.-P., and Guichard G. Helix forming oligoureas: temperature-dependent NMR, structure determination and circular dichroism of a nonomer with functionalised side chain. Helv. Chim. Acta 85 (2002) 3692-3711
    • (2002) Helv. Chim. Acta , vol.85 , pp. 3692-3711
    • Hemmerlin, C.1    Marraud, M.2    Rognan, D.3    Graff, R.4    Semetey, V.5    Briand, J.-P.6    Guichard, G.7
  • 22
    • 13944267446 scopus 로고    scopus 로고
    • N,N′-linked oligoureas as foldamers: chain length requirements for helix formation in protic solvent investigated by circular dichroism, NMR spectroscopy and molecular dynamics
    • Violette A., Averlant-Petit M.C., Semetey V., Hemmerlin C., Casimir R., Graff R., Marraud M., Briand J.-P., Rognan D., and Guichard G. N,N′-linked oligoureas as foldamers: chain length requirements for helix formation in protic solvent investigated by circular dichroism, NMR spectroscopy and molecular dynamics. J. Am. Chem. Soc. 127 (2005) 2156-2164
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2156-2164
    • Violette, A.1    Averlant-Petit, M.C.2    Semetey, V.3    Hemmerlin, C.4    Casimir, R.5    Graff, R.6    Marraud, M.7    Briand, J.-P.8    Rognan, D.9    Guichard, G.10
  • 23
    • 0034603443 scopus 로고    scopus 로고
    • Solid phase synthesis of oligoureas using O-succinimidyl-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl carbamate derivatives
    • Guichard G., Semetey V., Rodriguez M., and Briand J.-P. Solid phase synthesis of oligoureas using O-succinimidyl-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl carbamate derivatives. Tetrahedron Lett. 41 (2000) 1553-1557
    • (2000) Tetrahedron Lett. , vol.41 , pp. 1553-1557
    • Guichard, G.1    Semetey, V.2    Rodriguez, M.3    Briand, J.-P.4
  • 24
    • 0033550306 scopus 로고    scopus 로고
    • An effective preparation of O-succinimidyl-2-(tert-butoxycarbonylamino)-ethylcarbamate derivatives from β-amino-acids. Application to the synthesis of urea-containing pseudopeptides and oligoureas
    • Guichard G., Semetey V., Didierjean C., Aubry A., Briand J.-P., and Rodriguez M. An effective preparation of O-succinimidyl-2-(tert-butoxycarbonylamino)-ethylcarbamate derivatives from β-amino-acids. Application to the synthesis of urea-containing pseudopeptides and oligoureas. J. Org. Chem. 64 (1999) 8702-8705
    • (1999) J. Org. Chem. , vol.64 , pp. 8702-8705
    • Guichard, G.1    Semetey, V.2    Didierjean, C.3    Aubry, A.4    Briand, J.-P.5    Rodriguez, M.6
  • 25
    • 0346665667 scopus 로고    scopus 로고
    • 3-residues with side-chain branching adjacent to the β-carbon atom
    • 3-residues with side-chain branching adjacent to the β-carbon atom. Helv. Chim. Acta 85 (2002) 4154-4164
    • (2002) Helv. Chim. Acta , vol.85 , pp. 4154-4164
    • Raguse, T.L.1    Lai, J.R.2    Gellman, S.H.3
  • 27
    • 0141670369 scopus 로고    scopus 로고
    • Side-chain control of β-peptide secondary structures
    • Martinek T.A., and Fülöp F. Side-chain control of β-peptide secondary structures. Eur. J. Biochem. (Tokyo) 270 (2003) 3657-3666
    • (2003) Eur. J. Biochem. (Tokyo) , vol.270 , pp. 3657-3666
    • Martinek, T.A.1    Fülöp, F.2
  • 28
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau W.-M., Wimley W.C., Gawrisch K., and White S.H. The preference of tryptophan for membrane interfaces. Biochemistry 37 (1998) 14713-14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 30
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • Vogel H.J., Schibli D.J., Jing W., Lohmeier-Vogel E.M., Epand R.F., and Epand R.M. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol. 80 (2002) 49-63
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Jing, W.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 32
    • 0033863173 scopus 로고    scopus 로고
    • Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies
    • Blondelle S.E., and Lohner K. Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55 (2000) 74-87
    • (2000) Biopolymers , vol.55 , pp. 74-87
    • Blondelle, S.E.1    Lohner, K.2
  • 34
    • 0242286228 scopus 로고    scopus 로고
    • Liposomes as models for antimicrobial peptides
    • Epand R.M., and Epand R.F. Liposomes as models for antimicrobial peptides. Methods Enzymol. 372 (2003) 124-133
    • (2003) Methods Enzymol. , vol.372 , pp. 124-133
    • Epand, R.M.1    Epand, R.F.2
  • 38
    • 17444429937 scopus 로고    scopus 로고
    • Synthesis of urea oligomers and their antibacterial activity
    • Tang H., Doerksen R.J., and Tew G.N. Synthesis of urea oligomers and their antibacterial activity. Chem. Commun. (2005) 1537-1539
    • (2005) Chem. Commun. , pp. 1537-1539
    • Tang, H.1    Doerksen, R.J.2    Tew, G.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.