메뉴 건너뛰기




Volumn , Issue , 2013, Pages 305-333

Antimicrobial agents

Author keywords

Antibiotic; Antifungal; Antimicrobial peptide agents; Antiviral; DiPoPe; DMPC; DMPG; Lipid composition; LUV; Membrane curvature strain; MLV

Indexed keywords


EID: 84903406641     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1533/9781908818348.305     Document Type: Chapter
Times cited : (8)

References (38)
  • 1
    • 0033736593 scopus 로고    scopus 로고
    • Current and future antifungal therapy: new targets for antifungal therapy
    • Andriole T.V. Current and future antifungal therapy: new targets for antifungal therapy. Int. J. Antimicrob. Agents 2000, 16:317-321.
    • (2000) Int. J. Antimicrob. Agents , vol.16 , pp. 317-321
    • Andriole, T.V.1
  • 2
    • 0345276642 scopus 로고    scopus 로고
    • Interaction of synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: a biophysical study
    • Aranda F.J., Teruel J.A., Ortiz A. Interaction of synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: a biophysical study. Biochim. Biophys. Acta 2003, 1618:51-58.
    • (2003) Biochim. Biophys. Acta , vol.1618 , pp. 51-58
    • Aranda, F.J.1    Teruel, J.A.2    Ortiz, A.3
  • 3
    • 33645765417 scopus 로고    scopus 로고
    • Phospholipid vesicles as biosensors to evaluate antimicrobial agent-membrane interaction
    • Fresta M., Puglisi G. Phospholipid vesicles as biosensors to evaluate antimicrobial agent-membrane interaction. Rec. Res. Devel. Antimicrob. Agents Chemother 2000, 4:27-53.
    • (2000) Rec. Res. Devel. Antimicrob. Agents Chemother , vol.4 , pp. 27-53
    • Fresta, M.1    Puglisi, G.2
  • 4
    • 79953790729 scopus 로고    scopus 로고
    • Bacterial membrane lipids in the action of antimicrobial agents
    • Epand R.M., Epand R.F. Bacterial membrane lipids in the action of antimicrobial agents. J. Pept. Sci 2010, 17:298-305.
    • (2010) J. Pept. Sci , vol.17 , pp. 298-305
    • Epand, R.M.1    Epand, R.F.2
  • 5
    • 0029853192 scopus 로고    scopus 로고
    • Correlation of trimethoprim and brodimoprim physicochemical and lipid membrane interaction properties with their accumulation in human neutrophils
    • Fresta M., Furneri M.P., Mezzasalma E., Nicolosi V.M., Puglisi G. Correlation of trimethoprim and brodimoprim physicochemical and lipid membrane interaction properties with their accumulation in human neutrophils. Antimicrob. Agents Chemother 1996, 40:2865-2873.
    • (1996) Antimicrob. Agents Chemother , vol.40 , pp. 2865-2873
    • Fresta, M.1    Furneri, M.P.2    Mezzasalma, E.3    Nicolosi, V.M.4    Puglisi, G.5
  • 6
    • 0034660429 scopus 로고    scopus 로고
    • Antimicrobial nonapeptide leucinostatin A-dependent effects on the physical properties of phospholipid model membranes
    • Fresta M., Ricci M., Rossi C., Furneri P.M., Puglisi G. Antimicrobial nonapeptide leucinostatin A-dependent effects on the physical properties of phospholipid model membranes. J. Coll. Interface Sci 2000, 226:222-230.
    • (2000) J. Coll. Interface Sci , vol.226 , pp. 222-230
    • Fresta, M.1    Ricci, M.2    Rossi, C.3    Furneri, P.M.4    Puglisi, G.5
  • 7
    • 0036975799 scopus 로고    scopus 로고
    • Combining molecular modeling with experimental methodologies: mechanism of membrane permeation and accumulation of ofloxacin
    • Fresta M., Guccione S., Beccari A.R., Furneri P.M., Puglisi G. Combining molecular modeling with experimental methodologies: mechanism of membrane permeation and accumulation of ofloxacin. Bioorg. Med. Chem 2002, 10:3871-3889.
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 3871-3889
    • Fresta, M.1    Guccione, S.2    Beccari, A.R.3    Furneri, P.M.4    Puglisi, G.5
  • 8
    • 59149083858 scopus 로고    scopus 로고
    • Structural and calorimetrical studies of the effect of different aminoglycosides on DPPC liposomes
    • Oszlánczi A., Bota A., Czabai G., Klumpp E. Structural and calorimetrical studies of the effect of different aminoglycosides on DPPC liposomes. Coll. Surf. B Biointerfaces 2009, 69:116-121.
    • (2009) Coll. Surf. B Biointerfaces , vol.69 , pp. 116-121
    • Oszlánczi, A.1    Bota, A.2    Czabai, G.3    Klumpp, E.4
  • 9
    • 70450221516 scopus 로고    scopus 로고
    • Influence of aminoglycoside antibiotics on the thermal behavior and structural features of DPPE-DPPG model membranes
    • Oszlánczi A., Bota A., Klumpp E. Influence of aminoglycoside antibiotics on the thermal behavior and structural features of DPPE-DPPG model membranes. Coll. Surf. B Biointerfaces 2010, 75:141-148.
    • (2010) Coll. Surf. B Biointerfaces , vol.75 , pp. 141-148
    • Oszlánczi, A.1    Bota, A.2    Klumpp, E.3
  • 10
    • 33846290714 scopus 로고    scopus 로고
    • Layer formation in the bacteria membrane mimetic DPPE-DPPG/water system induced by sulfadiazine
    • Oszlánczi A., Bota A., Klumpp E. Layer formation in the bacteria membrane mimetic DPPE-DPPG/water system induced by sulfadiazine. Biophys. Chem 2007, 125:334-340.
    • (2007) Biophys. Chem , vol.125 , pp. 334-340
    • Oszlánczi, A.1    Bota, A.2    Klumpp, E.3
  • 11
    • 0034916176 scopus 로고    scopus 로고
    • Packing characteristics of model system mimicking cytoplasmic bacterial membranes
    • Lohner K., Latal A., Degovics G., Gariedel P. Packing characteristics of model system mimicking cytoplasmic bacterial membranes. Chem. Phys. Lipids 2001, 111:177-192.
    • (2001) Chem. Phys. Lipids , vol.111 , pp. 177-192
    • Lohner, K.1    Latal, A.2    Degovics, G.3    Gariedel, P.4
  • 12
    • 75949118910 scopus 로고    scopus 로고
    • Structural and morphological changes in bacteria-membrane mimetic DPPE/DPPG/water systems induced by sulfadiazine
    • Oszlánczi A., Bota A., Czabai G., Berenyi S., Klumpp E. Structural and morphological changes in bacteria-membrane mimetic DPPE/DPPG/water systems induced by sulfadiazine. Coll. Surf. B Biointerfaces 2010, 76:519-528.
    • (2010) Coll. Surf. B Biointerfaces , vol.76 , pp. 519-528
    • Oszlánczi, A.1    Bota, A.2    Czabai, G.3    Berenyi, S.4    Klumpp, E.5
  • 13
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with biomembrane-mimetic systems
    • Lohner K., Prenner E.J. Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with biomembrane-mimetic systems. Biochim. Biophys. Acta 1999, 1462:141-156.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 14
    • 71649106004 scopus 로고    scopus 로고
    • Induction of non-lamellar lipid phase by antimicrobial peptides: a potential link to mode of action
    • Haney E.F., Nathoo S., Vogel H.J., Prenner E.J. Induction of non-lamellar lipid phase by antimicrobial peptides: a potential link to mode of action. Chem. Phys. Lipids 2010, 163:82-93.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 82-93
    • Haney, E.F.1    Nathoo, S.2    Vogel, H.J.3    Prenner, E.J.4
  • 15
  • 16
    • 0032566283 scopus 로고    scopus 로고
    • Relationship of membrane curvature to the formation of pores by magainin 2
    • Matsuzaki K., Sugishita K., Ishibe N., Ueha M., Nakata S., et al. Relationship of membrane curvature to the formation of pores by magainin 2. Biochemistry 1998, 37:11856-11863.
    • (1998) Biochemistry , vol.37 , pp. 11856-11863
    • Matsuzaki, K.1    Sugishita, K.2    Ishibe, N.3    Ueha, M.4    Nakata, S.5
  • 17
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock K.J., Lee D.K., Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophy. J 2003, 84:3052-3060.
    • (2003) Biophy. J , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 18
    • 59849092098 scopus 로고    scopus 로고
    • Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain
    • Galanth C., Abbassi F., Lequin O., Ayala-Sanmartin J., Ladram A., et al. Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain. Biochemistry 2009, 48:313-327.
    • (2009) Biochemistry , vol.48 , pp. 313-327
    • Galanth, C.1    Abbassi, F.2    Lequin, O.3    Ayala-Sanmartin, J.4    Ladram, A.5
  • 19
    • 33748920525 scopus 로고    scopus 로고
    • The effect of binding of spider-derived antimicrobial peptides, oxyopinins, on lipid membranes
    • Nomura K., Corzo G. The effect of binding of spider-derived antimicrobial peptides, oxyopinins, on lipid membranes. Biochim. Biophys. Acta 2006, 1758(9):1475-1482.
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1475-1482
    • Nomura, K.1    Corzo, G.2
  • 20
    • 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., et al. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol 2002, 80:49-63.
    • (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
  • 21
    • 33745747109 scopus 로고    scopus 로고
    • Solid state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and mellitin
    • Ramamoorthy A., Thennarasu S., Lee D.K., Tan A.M., Maloy L. Solid state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and mellitin. Biophys. J 2006, 91:206-216.
    • (2006) Biophys. J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.M.4    Maloy, L.5
  • 22
    • 0034834560 scopus 로고    scopus 로고
    • Analogs of the antimicrobial peptide trichogin having opposite membrane properties
    • Epand R.F., Epand R.M., Formaggio F., Crisma M., Wu H.Y., et al. Analogs of the antimicrobial peptide trichogin having opposite membrane properties. Eur. J. Biochem 2001, 268:703-712.
    • (2001) Eur. J. Biochem , vol.268 , pp. 703-712
    • Epand, R.F.1    Epand, R.M.2    Formaggio, F.3    Crisma, M.4    Wu, H.Y.5
  • 23
    • 85031266879 scopus 로고    scopus 로고
    • The antimicrobial peptide trichogin and its interaction with phospholipid membranes
    • Epand R.F., Epand R.M., Monaco V., Stoia S., Formaggio F., et al. The antimicrobial peptide trichogin and its interaction with phospholipid membranes. Eur. J. Biochem 1999, 55:358-363.
    • (1999) Eur. J. Biochem , vol.55 , pp. 358-363
    • Epand, R.F.1    Epand, R.M.2    Monaco, V.3    Stoia, S.4    Formaggio, F.5
  • 24
    • 28244489607 scopus 로고    scopus 로고
    • Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
    • Powers J.P.S., Tan A., Ramamoorthy A., Hancock R.E.W. Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes. Biochem 2005, 44:15504-15513.
    • (2005) Biochem , vol.44 , pp. 15504-15513
    • Powers, J.P.S.1    Tan, A.2    Ramamoorthy, A.3    Hancock, R.E.W.4
  • 25
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner E.J., Lewis R.N.A.H., McElhaney R.N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta 1999, 1462:201-221.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 26
    • 0030853508 scopus 로고    scopus 로고
    • Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity
    • Prenner E.J., Lewis R.N.A.H., Neuman K.C., Gruner S.M., Kondejewski L.H., et al. Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity. Biochemistry 1997, 36:7906-7916.
    • (1997) Biochemistry , vol.36 , pp. 7906-7916
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Neuman, K.C.3    Gruner, S.M.4    Kondejewski, L.H.5
  • 28
    • 34948879131 scopus 로고    scopus 로고
    • Interactions of tryptophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry
    • Andrushchenko V.V., Vogel H.J., Prenner E.J. Interactions of tryptophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry. Biochim. Biophys. Acta 2007, 1768:2447-2458.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2447-2458
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 29
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptides
    • Lohner K., Blondelle S.E. Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptides. Comb. Chem. High Throughput Screen 2005, 8:239-255.
    • (2005) Comb. Chem. High Throughput Screen , vol.8 , pp. 239-255
    • Lohner, K.1    Blondelle, S.E.2
  • 30
    • 28044441143 scopus 로고    scopus 로고
    • Headgroup structure and fatty acid chain length of the acidic phospholipids modulate the interaction of membrane mimetic vesicles with the antimicrobial peptide protegrin-1
    • Jing W., Prenner E.J., Vogel H.J., Waring A.J., Lehrer I.R. Headgroup structure and fatty acid chain length of the acidic phospholipids modulate the interaction of membrane mimetic vesicles with the antimicrobial peptide protegrin-1. J. Peptide Sci 2005, 11:735-743.
    • (2005) J. Peptide Sci , vol.11 , pp. 735-743
    • Jing, W.1    Prenner, E.J.2    Vogel, H.J.3    Waring, A.J.4    Lehrer, I.R.5
  • 31
    • 2442492150 scopus 로고    scopus 로고
    • The cyclic antimicrobial peptide RTD-1 induces stabilized lipid-peptide domains more efficiently than its open-chain analogue
    • Abuja P.M., Zenz A., Trabi M., Craik D.J., Lohner K. The cyclic antimicrobial peptide RTD-1 induces stabilized lipid-peptide domains more efficiently than its open-chain analogue. FEBS Lett 2004, 566:301-306.
    • (2004) FEBS Lett , vol.566 , pp. 301-306
    • Abuja, P.M.1    Zenz, A.2    Trabi, M.3    Craik, D.J.4    Lohner, K.5
  • 32
    • 79952916267 scopus 로고    scopus 로고
    • C- and N-truncated antimicrobial peptides from LFampin 265-284: biophysical versus microbiology results
    • Adão R., Nazmi K., Bolscher J.G.M., Bastos M. C- and N-truncated antimicrobial peptides from LFampin 265-284: biophysical versus microbiology results. J. Pharm. Bio All. Sci 2011, 3(1):60-69.
    • (2011) J. Pharm. Bio All. Sci , vol.3 , Issue.1 , pp. 60-69
    • Adão, R.1    Nazmi, K.2    Bolscher, J.G.M.3    Bastos, M.4
  • 33
    • 42149140555 scopus 로고    scopus 로고
    • Membrane structure and interactions of a short lycotoxin I analogue
    • Adão R., Seixas R., Gomes P., Costa Pessoa J., Bastos M. Membrane structure and interactions of a short lycotoxin I analogue. J. Peptide Sci 2008, 14:528-534.
    • (2008) J. Peptide Sci , vol.14 , pp. 528-534
    • Adão, R.1    Seixas, R.2    Gomes, P.3    Costa Pessoa, J.4    Bastos, M.5
  • 34
    • 30344462076 scopus 로고    scopus 로고
    • A one-enzyme strategy to release an antimicrobial peptide from the LFampin-domain of bovine lactoferrin
    • Bolscher J.G., van der Kraan M.I., Nazmi K., Kalay H., Grün C.H., van't Hof W., et al. A one-enzyme strategy to release an antimicrobial peptide from the LFampin-domain of bovine lactoferrin. Peptides 2006, 27:1-9.
    • (2006) Peptides , vol.27 , pp. 1-9
    • Bolscher, J.G.1    van der Kraan, M.I.2    Nazmi, K.3    Kalay, H.4    Grün, C.H.5    Van't Hof, W.6
  • 35
    • 0345276642 scopus 로고    scopus 로고
    • Interaction of a synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: a biophysical study
    • Aranda F.J., Teruel J.A., Ortiz A. Interaction of a synthetic peptide corresponding to the N-terminus of canine distemper virus fusion protein with phospholipid vesicles: a biophysical study. Biochim. Biophys. Acta 2003, 1618:51-58.
    • (2003) Biochim. Biophys. Acta , vol.1618 , pp. 51-58
    • Aranda, F.J.1    Teruel, J.A.2    Ortiz, A.3
  • 36
    • 78049306063 scopus 로고    scopus 로고
    • Rigid amphipathic fusion inhibitors, small molecule antiviral compounds against enveloped viruses
    • St Vincent M.R., Colpitts C.C., Ustinov A.V., Muqadas M., Joyce M.A., et al. Rigid amphipathic fusion inhibitors, small molecule antiviral compounds against enveloped viruses. Proc. Nat. Acad. Sci 2010, 107:17339-17344.
    • (2010) Proc. Nat. Acad. Sci , vol.107 , pp. 17339-17344
    • St Vincent, M.R.1    Colpitts, C.C.2    Ustinov, A.V.3    Muqadas, M.4    Joyce, M.A.5
  • 37
    • 68949172175 scopus 로고    scopus 로고
    • Search for novel neuroaminidase inhibitors: design, synthesis and interaction of oseltamivir derivatives with model membrane using docking, NMR and DSC methods
    • D'Souza C., Kanyalkar M., Joshi M., Coutinho E., Srivastava S. Search for novel neuroaminidase inhibitors: design, synthesis and interaction of oseltamivir derivatives with model membrane using docking, NMR and DSC methods. Biochim. Biophys. Acta 2009, 1788(9):1740-1751.
    • (2009) Biochim. Biophys. Acta , vol.1788 , Issue.9 , pp. 1740-1751
    • D'Souza, C.1    Kanyalkar, M.2    Joshi, M.3    Coutinho, E.4    Srivastava, S.5
  • 38
    • 84861092298 scopus 로고    scopus 로고
    • In search of a novel antifungal agent: probing molecular interactions of fluconazole and its analogues with model membranes by NMR and DSC techniques
    • Pawar B., Joshi M., Srivastava S., Kanyalkar M. In search of a novel antifungal agent: probing molecular interactions of fluconazole and its analogues with model membranes by NMR and DSC techniques. J. Pharm. Pharmac 2012, 64(6):802-810.
    • (2012) J. Pharm. Pharmac , vol.64 , Issue.6 , pp. 802-810
    • Pawar, B.1    Joshi, M.2    Srivastava, S.3    Kanyalkar, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.