메뉴 건너뛰기




Volumn 9, Issue 9, 2014, Pages 2003-2007

How many antimicrobial peptide molecules kill a bacterium? The case of PMAP-23

Author keywords

[No Author keywords available]

Indexed keywords

LIPOSOME; PMAP 23; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; LIPID; PORCINE MYELOID ANTIBACTERIAL PEPTIDE 23;

EID: 84912532312     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500426r     Document Type: Article
Times cited : (103)

References (35)
  • 1
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. W., and Sahl, H. G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 12, 1551-1557.
    • (2006) Nat. Biotechnol. , vol.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 2
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: Primeval molecules or future drugs?
    • Peters, B. M., Shirtliff, M. E., and Jabra-Rizk, M. A. (2010) Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog. 6, e1001067.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001067
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 3
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel, A., and Sahl, H. G. (2006) The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4, 529-536.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 4
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a comeback
    • Fox, J. C. (2013) Antimicrobial peptides stage a comeback. Nat. Biotechnol. 31, 379-382.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 379-382
    • Fox, J.C.1
  • 5
    • 59449088862 scopus 로고    scopus 로고
    • Antibiotic-resistant bugs in 21st century-A clinical super-challenge
    • Arias, C. A., and Murray, B. E. (2009) Antibiotic-resistant bugs in 21st century-A clinical super-challenge. N. Engl. J. Med. 360, 439-443.
    • (2009) N. Engl. J. Med. , vol.360 , pp. 439-443
    • Arias, C.A.1    Murray, B.E.2
  • 6
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley, W. C. (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem. Biol. 5, 905-917.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 7
    • 70349634702 scopus 로고    scopus 로고
    • Different mechanism of action of antimicrobial peptides: Insights from fluorescence spectoscopy experiments and molecular dynamic simulations
    • Bocchinfuso, G., Palleschi, A., Orioni, B., Grande, G., Formaggio, F., Toniolo, C., Park, Y., Hahm, K. S., and Stella, L. (2009) Different mechanism of action of antimicrobial peptides: insights from fluorescence spectoscopy experiments and molecular dynamic simulations. J. Pept. Sci. 15, 550-558.
    • (2009) J. Pept. Sci. , vol.15 , pp. 550-558
    • Bocchinfuso, G.1    Palleschi, A.2    Orioni, B.3    Grande, G.4    Formaggio, F.5    Toniolo, C.6    Park, Y.7    Hahm, K.S.8    Stella, L.9
  • 8
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger, B., and Lohner, K. (2006) Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta 1758, 1529-1539.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 9
    • 79955669580 scopus 로고    scopus 로고
    • Antimicrobial peptides: Successes, challenges and unanswered questions
    • Wimley, W. C., and Hristova, K. (2011) Antimicrobial peptides: successes, challenges and unanswered questions. J. Membr. Biol. 239, 27-34.
    • (2011) J. Membr. Biol. , vol.239 , pp. 27-34
    • Wimley, W.C.1    Hristova, K.2
  • 10
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, N. M., Ferre, R., and Castanho, M. A. R. B. (2009) Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7, 245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, N.M.1    Ferre, R.2    Castanho, M.A.R.B.3
  • 11
    • 83355168944 scopus 로고    scopus 로고
    • Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides
    • Melo, N. M., Ferre, R., Feliu, L., Bardaji, E., Planas, M., and Castanho, M. A. R. B. (2011) Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides. PLoS One 6, e28549.
    • (2011) PLoS One , vol.6 , pp. e28549
    • Melo, N.M.1    Ferre, R.2    Feliu, L.3    Bardaji, E.4    Planas, M.5    Castanho, M.A.R.B.6
  • 12
    • 84907858203 scopus 로고    scopus 로고
    • Toward the de novo design of antimicrobial peptides: Lack of correlation between peptide permeabilization of lipid vesicles and antimicrobial, cytolytic, or cytotoxic activity in living cells
    • He, J., Krauson, A. J., and Wimley, W. C. (2014) Toward the de novo design of antimicrobial peptides: lack of correlation between peptide permeabilization of lipid vesicles and antimicrobial, cytolytic, or cytotoxic activity in living cells. Biopolymers 102, 1-6.
    • (2014) Biopolymers , vol.102 , pp. 1-6
    • He, J.1    Krauson, A.J.2    Wimley, W.C.3
  • 14
    • 84880320843 scopus 로고    scopus 로고
    • Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa
    • Luca, V., Stringaro, A., Colone, M., Pini, A., and Mangoni, M. L. (2013) Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa. Cell. Mol. Life Sci. 70, 2773-2786.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2773-2786
    • Luca, V.1    Stringaro, A.2    Colone, M.3    Pini, A.4    Mangoni, M.L.5
  • 17
    • 79960953216 scopus 로고    scopus 로고
    • Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides
    • Bocchinfuso, G., Bobone, S., Palleschi, A., and Stella, L. (2011) Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides. Cell. Mol. Life Sci. 68, 2281-2301.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2281-2301
    • Bocchinfuso, G.1    Bobone, S.2    Palleschi, A.3    Stella, L.4
  • 19
    • 0033864862 scopus 로고    scopus 로고
    • Amphpathic, α-helical antimicrobial peptides
    • Tossi, A., Sandri, L., and Giangaspero, A. (2000) Amphpathic, α-helical antimicrobial peptides. Biopolymers 55, 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 20
    • 0025050516 scopus 로고
    • Mueller-Hinton broth undergoes visible oxidative color changes in the presence of peroxidase and hydrogen peroxide
    • Galeazzi, L., Groppa, G., and Giunta, S. (1990) Mueller-Hinton broth undergoes visible oxidative color changes in the presence of peroxidase and hydrogen peroxide. J. Clin. Microbiol. 28, 2145-2147.
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 2145-2147
    • Galeazzi, L.1    Groppa, G.2    Giunta, S.3
  • 21
    • 0034667871 scopus 로고    scopus 로고
    • How to measure tryptophan fluorescence in membrane properly, and why bother?
    • Ladokhin, A. S., Jayasinghe, S., and White, S. H. (2000) How to measure tryptophan fluorescence in membrane properly, and why bother? Anal. Biochem. 285, 235-245.
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 22
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • Gazit, E., Miller, I. R., Biggin, P. C., Sansom, M. S., and Shai, Y. (1996) Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258, 860-870.
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.4    Shai, Y.5
  • 24
    • 0031849123 scopus 로고    scopus 로고
    • Bacterial concentrations in pus and infected peritoneal fluid-implications for bactericidal activity of antibiotics
    • König, C., Simmen, H. P., and Blaser, J. (1998) Bacterial concentrations in pus and infected peritoneal fluid-implications for bactericidal activity of antibiotics. J. Antimicrob. Chemother. 42, 227-232.
    • (1998) J. Antimicrob. Chemother. , vol.42 , pp. 227-232
    • König, C.1    Simmen, H.P.2    Blaser, J.3
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu, M., Maier, E., Benz, R., and Hancock, R. E. W. (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38, 7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 30
    • 0019304939 scopus 로고
    • Colorimetric determination of phospholipids with ammonium ferrothiocyanate
    • Stewart, J. (1980) Colorimetric determination of phospholipids with ammonium ferrothiocyanate. Anal. Biochem. 104, 10-14.
    • (1980) Anal. Biochem. , vol.104 , pp. 10-14
    • Stewart, J.1
  • 31
    • 78751575968 scopus 로고    scopus 로고
    • C-terminal amidation of PMAP-23: Translocation to the inner membrane of Gram-negative bacteria
    • Kim, J. Y., Park, S. C., Yoon, M. Y., Hahm, K. S., and Park, Y. (2011) C-terminal amidation of PMAP-23: translocation to the inner membrane of Gram-negative bacteria. Amino Acids 40, 183-195.
    • (2011) Amino Acids , vol.40 , pp. 183-195
    • Kim, J.Y.1    Park, S.C.2    Yoon, M.Y.3    Hahm, K.S.4    Park, Y.5
  • 32
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • Lehrer, R., Barton, A., and Ganz, T. (1988) Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. J. Immunol. Methods 108, 153-158.
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.1    Barton, A.2    Ganz, T.3
  • 33
    • 0344222215 scopus 로고    scopus 로고
    • Determination of bacterial cell dry mass by transmission electron microscopy and densitometric image analysis
    • Loferer-Krößbacher, M., Klima, J., and Psenner, R. (1998) Determination of bacterial cell dry mass by transmission electron microscopy and densitometric image analysis. Appl. Environ. Microbiol. 64, 688-694.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 688-694
    • Loferer-Krößbacher, M.1    Klima, J.2    Psenner, R.3
  • 34
    • 0042136041 scopus 로고
    • Phospholipids of Azotobacter agilis, Agrobacterium tumefaciens, and Escherichia coli
    • Kaneshiro, T., and Marr, A. G. (1962) Phospholipids of Azotobacter agilis, Agrobacterium tumefaciens, and Escherichia coli. J. Lipid Res. 3, 184-189.
    • (1962) J. Lipid Res. , vol.3 , pp. 184-189
    • Kaneshiro, T.1    Marr, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.