메뉴 건너뛰기




Volumn 1808, Issue 9, 2011, Pages 2197-2205

Structural basis for the enhanced activity of cyclic antimicrobial peptides: The case of BPC194

Author keywords

Antimicrobial peptide; Molecular dynamics; Peptide folding; Peptide membrane interaction; Structure function of cyclic peptide

Indexed keywords

CYCLIC(LYSYLLYSYLLEUCYLLYSYLLYSYLPHENYLALANYLLYSYLLYSYLLEUCYLGLUTAMINE); POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 79960015637     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.05.001     Document Type: Article
Times cited : (57)

References (47)
  • 2
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • DOI 10.1016/S0952-7915(99)80005-3
    • R.I. Lehrer, and T. Ganz Antimicrobial peptides in mammalian and insect host defence Curr. Opin. Immunol. 11 1999 23 27 (Pubitemid 29082332)
    • (1999) Current Opinion in Immunology , vol.11 , Issue.1 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 3
    • 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
  • 5
    • 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
  • 6
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • DOI 10.1021/bi000946l
    • H.W. Huang Action of antimicrobial peptides: two-state model Biochemistry 39 2000 8347 8352 (Pubitemid 30489931)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8347-8352
    • Huang, H.W.1
  • 9
    • 0041475925 scopus 로고    scopus 로고
    • The cyclization of peptides and depsipeptides
    • DOI 10.1002/psc.491
    • J.S. Davies The cyclization of peptides and depsipeptides J. Pept. Sci. 9 2003 471 501 (Pubitemid 37009926)
    • (2003) Journal of Peptide Science , vol.9 , Issue.8 , pp. 471-501
    • Davies, J.S.1
  • 10
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanism of action
    • R.M. Epand, and H. Vogel Diversity of antimicrobial peptides and their mechanism of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.2
  • 11
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat. Rev. Immunol. 3 2003 710 720 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 12
    • 0017382706 scopus 로고
    • Conformations of di-N-methylleucine gramicidin S and N-methylleucine gramicidin S compatible with the sidedness hypothesis
    • T. Kato, and N. Izumiya Conformations of di-N-methylleucine gramicidin S and N-methylleucine gramicidin S compatible with the sidedness hypothesis Biochim. Biophys. Acta 493 1977
    • (1977) Biochim. Biophys. Acta , vol.493
    • Kato, T.1    Izumiya, N.2
  • 13
    • 32544456244 scopus 로고    scopus 로고
    • Antimicrobial peptides: New candidates in the fight against bacterial infections
    • DOI 10.1002/bip.20286
    • O. Toke Antimicrobial peptides: new candidates in the fight against bacterial infections Biopolymers 80 2005 717 735 (Pubitemid 43266580)
    • (2005) Biopolymers - Peptide Science Section , vol.80 , Issue.6 , pp. 717-735
    • Toke, O.1
  • 14
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • M.N. Melo, R. Ferre, and M.A.R.B. Castanho Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations Nat. Rev. Microbiol. 7 2009 245 250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 15
    • 33750057421 scopus 로고    scopus 로고
    • Improvement of cyclic decapeptides against plant pathogenic bacteria using a combinatorial chemistry approach
    • DOI 10.1016/j.peptides.2006.05.001, PII S0196978106002233
    • S. Monroc, E. Badosa, E. Besalú, M. Planas, E. Bardají, E. Montesinos, and L. Feliu Improvement of cyclic decapeptides against plant pathogenic bacteria using a combinatorial chemistry approach Peptides 27 2006 2575 2584 (Pubitemid 44584387)
    • (2006) Peptides , vol.27 , Issue.11 , pp. 2575-2584
    • Monroc, S.1    Badosa, E.2    Besalu, E.3    Planas, M.4    Bardaji, E.5    Montesinos, E.6    Feliu, L.7
  • 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. Bardají 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
    • 23044503853 scopus 로고    scopus 로고
    • Chemistry: A light-actuated nanovalve derived from a channel protein
    • DOI 10.1126/science.1114760
    • A. Koçer, M. Walko, W. Meijberg, and B.L. Feringa A light-actuated nanovalve derived from a channel protein Sci. 309 2005 755 758 (Pubitemid 41077318)
    • (2005) Science , vol.309 , Issue.5735 , pp. 755-758
    • Kocer, A.1    Walko, M.2    Meijberg, W.3    Feringa, B.L.4
  • 18
    • 0141431014 scopus 로고    scopus 로고
    • The role of tryptophan residues in an integral membrane protein: Diacylglycerol kinase
    • DOI 10.1021/bi034607e
    • E. Clark, J. East, and A. Lee The role of tryptophan residues in an integral membrane protein: diacylglycerol kinase Biochemistry 42 2003 11065 11073 (Pubitemid 37174399)
    • (2003) Biochemistry , vol.42 , Issue.37 , pp. 11065-11073
    • Clark, E.H.1    East, J.M.2    Lee, A.G.3
  • 19
    • 1142298539 scopus 로고    scopus 로고
    • Interaction of Antiinflammatory Drugs with EPC Liposomes: Calorimetric Study in a Broad Concentration Range
    • C. Matos, J.L. Lima, S. Reis, A. Lopes, and M. Bastos Interaction of antiinflammatory drugs with EPC liposomes: calorimetric study in a broad concentration range Biophys. J. 86 2004 946 954 (Pubitemid 38209539)
    • (2004) Biophysical Journal , vol.86 , Issue.2 , pp. 946-954
    • Matos, C.M.1    Lima, J.L.C.2    Reis, S.3    Lopes, A.4    Bastos, M.5
  • 20
    • 34047249400 scopus 로고    scopus 로고
    • Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation
    • DOI 10.1016/j.bbamem.2007.02.005, PII S0005273607000405
    • M.N. Melo, and M.A. Castanho Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation Biochim. Biophys. Acta 1768 2007 1277 1290 (Pubitemid 46550363)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.5 , pp. 1277-1290
    • Melo, M.N.1    Castanho, M.A.R.B.2
  • 26
    • 33846846337 scopus 로고    scopus 로고
    • + counterions
    • DOI 10.1529/biophysj.106.086272
    • W. Zhao, T. Róg, A.A. Gurtovenko, I. Vattulainen, and M. Karttunen Atomic-scale structure and electrostatics of anionic palmitoyloleoylphosphatidylglycerol lipid bilayers with Na+ counterions Biophys. J. 92 2007 1114 1124 (Pubitemid 46203173)
    • (2007) Biophysical Journal , vol.92 , Issue.4 , pp. 1114-1124
    • Zhao, W.1    Rog, T.2    Gurtovenko, A.A.3    Vattulainen, I.4    Karttunen, M.5
  • 27
    • 34447342290 scopus 로고    scopus 로고
    • On the propensity of phosphatidylglycerols to form interdigitated phases
    • DOI 10.1529/biophysj.106.101592
    • G. Pabst, S. Danner, S. Karmakar, G. Deutsch, and V.A. Raghunathan On the propensity of phosphatidylglycerols to form interdigitated phases Biophys. J. 93 2007 513 525 (Pubitemid 47057817)
    • (2007) Biophysical Journal , vol.93 , Issue.2 , pp. 513-525
    • Pabst, G.1    Danner, S.2    Karmakar, S.3    Deutsch, G.4    Raghunathany, V.A.5
  • 28
    • 34247530728 scopus 로고    scopus 로고
    • Peptide insertion, positioning, and stabilization in a membrane: Insight from an all-atom molecular dynamics simulation
    • DOI 10.1002/bip.20698
    • A. Babakhani, A.A. Gorfe, J. Gullingsrud, J.E. Kim, and J.A. McCammon Peptide insertion, positioning, and stabilization in a membrane: insight from an all-atom molecular dynamics simulation Biopolymers 2007 490 497 (Pubitemid 46649829)
    • (2007) Biopolymers , vol.85 , Issue.5-6 , pp. 490-497
    • Babakhani, A.1    Gorfe, A.A.2    Gullingsrud, J.3    Kim, J.E.4    McCammon, J.A.5
  • 29
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • I.G. Tironi, R. Sperb, P.E. Smith, and W.F. van Gunsteren A generalized reaction field method for molecular dynamics simulations J. Chem. Phys. 102 1995 5451 5459
    • (1995) J. Chem. Phys. , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    Van Gunsteren, W.F.4
  • 34
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • D. Sengupta, H. Leontiadou, A.E. Mark, and S.J. Marrink Toroidal pores formed by antimicrobial peptides show significant disorder Biochim. Biophys. Acta 1778 2008 2308 2317
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.J.4
  • 35
    • 36248932202 scopus 로고    scopus 로고
    • Computer simulations of antimicrobial peptides
    • E. Mátyus, C. Kandt, and D.P. Tieleman Computer simulations of antimicrobial peptides Curr. Med. Chem. 14 2007 2789 2798
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2789-2798
    • Mátyus, E.1    Kandt, C.2    Tieleman, D.P.3
  • 36
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 37
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • DOI 10.1074/jbc.274.1.29
    • M. Wu, and R.E.W. Hancock Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmatic membrane J. Biol. Chem. 274 1999 29 35 (Pubitemid 29035025)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 29-35
    • Wu, M.1    Hancock, R.E.W.2
  • 38
    • 0024065282 scopus 로고
    • Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns
    • M.C. Manning, M. Illangasekare, and R.W. Woody Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns Biophys. Chem. 31 1988 77 86
    • (1988) Biophys. Chem. , vol.31 , pp. 77-86
    • Manning, M.C.1    Illangasekare, M.2    Woody, R.W.3
  • 39
    • 0018267874 scopus 로고
    • Circular dichroism of beta turns in peptides and proteins
    • C.A. Bush, S.K. Sarkar, and K.D. Kopple Circular dichroism of beta turns in peptides and proteins Biochemistry 17 1978 4951 4954
    • (1978) Biochemistry , vol.17 , pp. 4951-4954
    • Bush, C.A.1    Sarkar, S.K.2    Kopple, K.D.3
  • 41
    • 34249081426 scopus 로고    scopus 로고
    • Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1
    • S.T. Henriques, A. Quintas, L.A. Bagatolli, F. Homble, and M.A. Castanho Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1 Mol. Membr. Biol. 24 2007 282 293
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 282-293
    • Henriques, S.T.1    Quintas, A.2    Bagatolli, L.A.3    Homble, F.4    Castanho, M.A.5
  • 42
  • 43
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • DOI 10.1074/jbc.271.41.25261
    • L.H. Kondejewski, S.W. Farmer, D.S. Wishart, C.M. Kay, R.E.W. Hancock, and R.S. Hodges Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs J. Biol. Chem. 271 1996 25261 25268 (Pubitemid 26337892)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 44
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • DOI 10.1002/bip.10260
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248 (Pubitemid 36098316)
    • (2002) Biopolymers - Peptide Science Section , vol.66 , Issue.4 , pp. 236-248
    • Shai, Y.1
  • 45
    • 40049089464 scopus 로고    scopus 로고
    • Observation of multiple folding pathways of β-hairpin trpzip2 from independent continuous folding trajectories
    • DOI 10.1093/bioinformatics/btn029
    • C. Chen, and Y. Xiao Observation of multiple folding pathways of beta-hairpin trpzip2 from independent continuous folding trajectories Bioinformatics 24 2008 659 665 (Pubitemid 351321209)
    • (2008) Bioinformatics , vol.24 , Issue.5 , pp. 659-665
    • Chen, C.1    Xiao, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.