메뉴 건너뛰기




Volumn 32, Issue 5, 2011, Pages 875-880

Improved proteolytic stability of chicken cathelicidin-2 derived peptides by d-amino acid substitutions and cyclization

Author keywords

Chicken cathelicidin 2; Cyclization; d Amino acid substitution; Host defense peptide; Stability

Indexed keywords

BACTERIAL PROTEIN; BACTERIUM LIPOPOLYSACCHARIDE; CATHELICIDIN; CATHELICIDIN 2; PHENYLALANINE; PROTEINASE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 79955470808     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2011.02.017     Document Type: Article
Times cited : (75)

References (33)
  • 1
    • 41649084341 scopus 로고    scopus 로고
    • Design and synthesis of cyclic disulfide-bonded antibacterial peptides on the basis of the α helical domain of Tenecin 1, an insect defensin
    • DOI 10.1016/j.bmc.2008.01.019, PII S0968089608000369
    • H.S. Ahn, W. Cho, J.M. Kim, B.P. Joshi, J.W. Park, and C.R. Lohani Design and synthesis of cyclic disulfide-bonded antibacterial peptides on the basis of the alpha helical domain of Tenecin 1, an insect defensin Bioorg Med Chem 16 2008 4127 4137 (Pubitemid 351484010)
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.7 , pp. 4127-4137
    • Ahn, H.-s.1    Cho, W.2    Kim, J.-m.3    Joshi, B.P.4    Park, J.-w.5    Lohani, C.R.6    Cho, H.7    Lee, K.-H.8
  • 2
    • 13844315653 scopus 로고    scopus 로고
    • A re-evaluation of the role of host defence peptides in mammalian immunity
    • DOI 10.2174/1389203053027494
    • D.M. Bowdish, D.J. Davidson, and R.E. Hancock A re-evaluation of the role of host defence peptides in mammalian immunity Curr Protein Pept Sci 6 2005 35 51 (Pubitemid 40259800)
    • (2005) Current Protein and Peptide Science , vol.6 , Issue.1 , pp. 35-51
    • Bowdish, D.M.E.1    Davidson, D.J.2    Hancock, R.E.W.3
  • 3
    • 3342965837 scopus 로고    scopus 로고
    • In vitro activity and potency of an intravenously injected antimicrobial peptide and its DL amino acid analog in mice infected with bacteria
    • DOI 10.1128/AAC.48.8.3127-3129.2004
    • A. Braunstein, N. Papo, and Y. Shai In vitro activity and potency of an intravenously injected antimicrobial peptide and its dl amino acid analog in mice infected with bacteria Antimicrob Agents Chemother 48 2004 3127 3129 (Pubitemid 38989185)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.8 , pp. 3127-3129
    • Braunstein, A.1    Papo, N.2    Shai, Y.3
  • 4
    • 3142691160 scopus 로고    scopus 로고
    • Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides
    • DOI 10.1021/bi035948v
    • M. Dathe, H. Nikolenko, J. Klose, and M. Bienert Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan- containing hexapeptides Biochemistry 43 2004 9140 9150 (Pubitemid 38924447)
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9140-9150
    • Dathe, M.1    Nikolenko, H.2    Klose, J.3    Bienert, M.4
  • 6
    • 0036445391 scopus 로고    scopus 로고
    • Antimicrobial activity and stability to proteolysis of small linear cationic peptides with D-amino acid substitutions
    • K. Hamamoto, Y. Kida, Y. Zhang, T. Shimizu, and K. Kuwano Antimicrobial activity and stability to proteolysis of small linear cationic peptides with d-amino acid substitutions Microbiol Immunol 46 2002 741 749 (Pubitemid 35428950)
    • (2002) Microbiology and Immunology , vol.46 , Issue.11 , pp. 741-749
    • Hamamoto, K.1    Kida, Y.2    Zhang, Y.3    Shimizu, T.4    Kuwano, K.5
  • 7
    • 0344418718 scopus 로고    scopus 로고
    • Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide
    • DOI 10.1016/S0006-2952(99)00259-2, PII S0006295299002592
    • S.Y. Hong, J.E. Oh, and K.H. Lee Effect of d-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide Biochem Pharmacol 58 1999 1775 1780 (Pubitemid 29505418)
    • (1999) Biochemical Pharmacology , vol.58 , Issue.11 , pp. 1775-1780
    • Hong, S.Y.1    Oh, J.E.2    Lee, K.-H.3
  • 8
  • 9
    • 51949114856 scopus 로고    scopus 로고
    • Structure-antimicrobial activity relationship between pleurocidin and its enantiomer
    • J. Lee, and D.G. Lee Structure-antimicrobial activity relationship between pleurocidin and its enantiomer Exp Mol Med 40 2008 370 376
    • (2008) Exp Mol Med , vol.40 , pp. 370-376
    • Lee, J.1    Lee, D.G.2
  • 12
    • 37249076371 scopus 로고    scopus 로고
    • Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3
    • DOI 10.1016/j.peptides.2007.10.013, PII S0196978107004251
    • G. Maisetta, M. Di Luca, S. Esin, W. Florio, F.L. Brancatisano, and D. Bottai Evaluation of the inhibitory effects of human serum components on bactericidal activity of human beta defensin 3 Peptides 29 2008 1 6 (Pubitemid 350266113)
    • (2008) Peptides , vol.29 , Issue.1 , pp. 1-6
    • Maisetta, G.1    Di Luca, M.2    Esin, S.3    Florio, W.4    Brancatisano, F.L.5    Bottai, D.6    Campa, M.7    Batoni, G.8
  • 13
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: obstacles and realistic outlook
    • DOI 10.1016/j.coph.2006.04.006, PII S1471489206001299, Anti-infectives/New Technologies
    • A.K. Marr, W.J. Gooderham, and R.E. Hancock Antibacterial peptides for therapeutic use: obstacles and realistic outlook Curr Opin Pharmacol 6 2006 468 472 (Pubitemid 44340665)
    • (2006) Current Opinion in Pharmacology , vol.6 , Issue.5 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3
  • 14
    • 67649256037 scopus 로고    scopus 로고
    • Control of cell selectivity of antimicrobial peptides
    • K. Matsuzaki Control of cell selectivity of antimicrobial peptides Biochim Biophys Acta 1788 2009 1687 1692
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1687-1692
    • Matsuzaki, K.1
  • 16
    • 33750080503 scopus 로고    scopus 로고
    • De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria
    • DOI 10.1016/j.peptides.2006.04.019, PII S0196978106002208
    • S. Monroc, E. Badosa, L. Feliu, M. Planas, E. Montesinos, and E. Bardaji De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria Peptides 27 2006 2567 2574 (Pubitemid 44584384)
    • (2006) Peptides , vol.27 , Issue.11 , pp. 2567-2574
    • Monroc, S.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5    Bardaji, E.6
  • 17
    • 0034705132 scopus 로고    scopus 로고
    • Cyclization of a cytolytic amphipathic α-helical peptide and its diastereomer: Effect on structure, interaction with model membranes, and biological function
    • DOI 10.1021/bi992408i
    • Z. Oren, and Y. Shai Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function Biochemistry 39 2000 6103 6114 (Pubitemid 30327085)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6103-6114
    • Oren, Z.1    Shai, Y.2
  • 18
    • 1242352887 scopus 로고    scopus 로고
    • In vitro activity and mode of action of diastereomeric antimicrobial peptides against bacterial clinical isolates
    • DOI 10.1093/jac/dkh083
    • U. Pag, M. Oedenkoven, N. Papo, Z. Oren, Y. Shai, and H.G. Sahl In vitro activity and mode of action of diastereomeric antimicrobial peptides against bacterial clinical isolates J Antimicrob Chemother 53 2004 230 239 (Pubitemid 38239955)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.53 , Issue.2 , pp. 230-239
    • Pag, U.1    Oedenkoven, M.2    Papo, N.3    Oren, Z.4    Shai, Y.5    Sahl, H.-G.6
  • 19
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • DOI 10.1038/nrmicro1441, PII N1441
    • A. Peschel, and H.G. Sahl The co-evolution of host cationic antimicrobial peptides and microbial resistance Nat Rev Microbiol 4 2006 529 536 (Pubitemid 43905612)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.7 , pp. 529-536
    • Peschel, A.1    Sahl, H.-G.2
  • 20
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • J. Potempa, and R.N. Pike Corruption of innate immunity by bacterial proteases J Innate Immun 1 2009 70 87
    • (2009) J Innate Immun , vol.1 , pp. 70-87
    • Potempa, J.1    Pike, R.N.2
  • 21
    • 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
    • A. Schmidtchen, I.M. Frick, E. Andersson, H. Tapper, and L. Bjorck Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37 Mol Microbiol 46 2002 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
  • 23
    • 34447544341 scopus 로고    scopus 로고
    • Albumin binding of short cationic antimicrobial micropeptides and its influence on the in vitro bactericidal effect
    • DOI 10.1021/jm0703542
    • J. Svenson, B.O. Brandsdal, W. Stensen, and J.S. Svendsen Albumin binding of short cationic antimicrobial micropeptides and its influence on the in vitro bactericidal effect J Med Chem 50 2007 3334 3339 (Pubitemid 47065982)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.14 , pp. 3334-3339
    • Svenson, J.1    Brandsdal, B.-O.2    Stensen, W.3    Svendsen, J.S.4
  • 24
    • 0035967534 scopus 로고    scopus 로고
    • The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: Implication to their mode of action
    • DOI 10.1021/bi0026066
    • T. Unger, Z. Oren, and Y. Shai The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: implication to their mode of action Biochemistry 40 2001 6388 6397 (Pubitemid 32472728)
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6388-6397
    • Unger, T.1    Oren, Z.2    Shai, Y.3
  • 26
    • 62549131140 scopus 로고    scopus 로고
    • Chicken heterophils are recruited to the site of Salmonella infection and release antibacterial mature Cathelicidin-2 upon stimulation with LPS
    • A. van Dijk, M.H. Tersteeg-Zijderveld, J.L. Tjeerdsma-van Bokhoven, A.J. Jansman, E.J. Veldhuizen, and H.P. Haagsman Chicken heterophils are recruited to the site of Salmonella infection and release antibacterial mature Cathelicidin-2 upon stimulation with LPS Mol Immunol 46 2009 1517 1526
    • (2009) Mol Immunol , vol.46 , pp. 1517-1526
    • Van Dijk, A.1    Tersteeg-Zijderveld, M.H.2    Tjeerdsma-Van Bokhoven, J.L.3    Jansman, A.J.4    Veldhuizen, E.J.5    Haagsman, H.P.6
  • 31
    • 19544381182 scopus 로고    scopus 로고
    • Human salivary mucin MUC7 12-mer-L and 12-mer-D peptides: Antifungal activity in saliva, enhancement of activity with protease inhibitor cocktail or EDTA, and cytotoxicity to human cells
    • DOI 10.1128/AAC.49.6.2336-2342.2005
    • G.X. Wei, and L.A. Bobek Human salivary mucin MUC7 12-mer-L and 12-mer-D peptides: antifungal activity in saliva, enhancement of activity with protease inhibitor cocktail or EDTA, and cytotoxicity to human cells Antimicrob Agents Chemother 49 2005 2336 2342 (Pubitemid 40734463)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.6 , pp. 2336-2342
    • Wei, G.-X.1    Bobek, L.A.2
  • 32
    • 33646367203 scopus 로고    scopus 로고
    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity
    • DOI 10.1074/jbc.M507180200
    • Y. Xiao, Y. Cai, Y.R. Bommineni, S.C. Fernando, O. Prakash, and S.E. Gilliland Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity J Biol Chem 281 2006 2858 2867 (Pubitemid 43845751)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2858-2867
    • Xiao, Y.1    Cai, Y.2    Bommineni, Y.R.3    Fernando, S.C.4    Prakash, O.5    Gilliland, S.E.6    Zhang, G.7
  • 33
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.