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Volumn 35, Issue 10-11, 2009, Pages 986-997

Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles

Author keywords

Antimicrobial peptides; Binding free energy calculations; IsCT; Molecular dynamics simulations

Indexed keywords

ANIONIC LIPIDS; ANIONIC MICELLES; ANTI-MICROBIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; BACTERIAL MEMBRANES; BI-LAYER; BINDING FREE ENERGY; BINDING STRENGTH; CYTOPLASMIC MEMBRANE; ELECTROSTATIC PROPERTIES; ENTROPIC CONTRIBUTIONS; EQUILIBRIUM STRUCTURES; MAMMALIAN CELLS; MEMBRANE BINDING; MICELLE SYSTEMS; MOLECULAR DYNAMICS SIMULATIONS; RELATIVE BINDING; RELATIVE FREE ENERGY; SDS MICELLES; SODIUM DODECYL SULPHATE; THERMODYNAMIC CYCLE;

EID: 73149118069     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020902902742     Document Type: Conference Paper
Times cited : (11)

References (77)
  • 1
    • 0036312540 scopus 로고    scopus 로고
    • Antimicrobial resistance and aging: Beginning of the end of the antibiotic era?
    • T.T. Yoshikawa, Antimicrobial resistance and aging: beginning of the end of the antibiotic era? J. Am. Geriatr. Soc. 50 (2002), pp. 226-229.
    • (2002) J. Am. Geriatr. Soc. , vol.50 , pp. 226-229
    • Yoshikawa, T.T.1
  • 2
    • 0030841073 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility
    • K. Hiramatsu, H. Hanaki, T. Ino, K. Yabuta, T. Oguri, and F.C. Tenover, Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility, J. Antimicrob. Chemother. 40 (1997), pp. 135-136.
    • (1997) J. Antimicrob. Chemother. , vol.40 , pp. 135-136
    • Hiramatsu, K.1    Hanaki, H.2    Ino, T.3    Yabuta, K.4    Oguri, T.5    Tenover, F.C.6
  • 3
    • 0028787685 scopus 로고
    • Emergence of multiple-antibiotic-resistant Streptococcus pneumoniae in Hong Kong Antimicrob
    • K.M. Kam, K.Y. Luey, S.M. Fung, P.P. Yiu, T.J. Harden, and M.M. Cheung, Emergence of multiple-antibiotic-resistant Streptococcus pneumoniae in Hong Kong, Antimicrob. Agents Chemother. 39 (1995), pp. 2667-2670.
    • (1995) Agents Chemother. , vol.39 , pp. 2667-2670
    • Kam, K.M.1    Luey, K.Y.2    Fung, S.M.3    Yiu, P.P.4    Harden, T.J.5    Cheung, M.M.6
  • 5
    • 0031813081 scopus 로고    scopus 로고
    • Genetics of MRSA
    • W. Grubb, Genetics of MRSA, Rev. Med. Microbiol. 9 (1998), pp. 153-162.
    • (1998) Rev. Med. Microbiol. , vol.9 , pp. 153-162
    • Grubb, W.1
  • 6
    • 32544456244 scopus 로고    scopus 로고
    • Antimicrobial peptides: New candidates in the fight against bacterial infections
    • T. Orsolya, Antimicrobial peptides: new candidates in the fight against bacterial infections, Peptide Sci. 80 (2005), pp. 717-735.
    • (2005) Peptide Sci , vol.80 , pp. 717-735
    • Orsolya, T.1
  • 7
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff, Antimicrobial peptides of multicellular organisms, Nature 415 (2002), pp. 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 8
    • 44649155678 scopus 로고    scopus 로고
    • Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: Predicting experimental toxicity
    • A.A. Langham, H. Khandelia, B. Schuster, A.J. Waring, R.I. Lehrer, and Y.N. Kaznessis, Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: predicting experimental toxicity, Peptides 29 (2008), pp. 1085-1093.
    • (2008) Peptides , vol.29 , pp. 1085-1093
    • Langham, A.A.1    Khandelia, H.2    Schuster, B.3    Waring, A.J.4    Lehrer, R.I.5    Kaznessis, Y.N.6
  • 10
    • 0037228233 scopus 로고    scopus 로고
    • Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A
    • R.W. Hong, M. Shchepetov, J.N. Weiser, P.H. Axelsen, Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A, Antimicrob. Agents Chemother. 47 (2003), pp. 1-6.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1-6
    • Hong, R.W.1    Shchepetov, M.2    Weiser, J.N.3    Axelsen, P.H.4
  • 12
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • S. Yechiel, Mode of action of membrane active antimicrobial peptides, Peptide Sci. 66 (2002), pp. 236-248.
    • (2002) Peptide Sci , vol.66 , pp. 236-248
    • Yechiel, S.1
  • 13
    • 33746592900 scopus 로고    scopus 로고
    • Effects of mutations on the C-terminus of protegrin-1: A molecular dynamics simulation study
    • A.A. Langham and Y.N. Kaznessis, Effects of mutations on the C-terminus of protegrin-1: a molecular dynamics simulation study, Mol. Simulation 32 (2006), pp. 193-201.
    • (2006) Mol. Simulation , vol.32 , pp. 193-201
    • Langham, A.A.1    Kaznessis, Y.N.2
  • 14
    • 33645751940 scopus 로고    scopus 로고
    • How can a Betasheet peptide be both a potent antimicrobial and harmfully toxic: Molecular dynamics simulations of protegrin-1 in micelles
    • A.A. Langham, H. Khandelia, and Y.N. Kaznessis, How can a Betasheet peptide be both a potent antimicrobial and harmfully toxic: molecular dynamics simulations of protegrin-1 in micelles, J. Peptide Sci. 84 (2006), pp. 219-231.
    • (2006) J. Peptide Sci. , vol.84 , pp. 219-231
    • Langham, A.A.1    Khandelia, H.2    Kaznessis, Y.N.3
  • 15
    • 33746651219 scopus 로고    scopus 로고
    • Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions
    • H. Khandelia, A.A. Langham, Y.N. Kaznessis, Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions, Biochim. Biophys. Acta (BBA) Biomembranes 1758 (2006), pp. 1224-1234.
    • (2006) Biochim. Biophys. Acta (BBA) Biomembranes , vol.1758 , pp. 1224-1234
    • Khandelia, H.1    Langham, A.A.2    Kaznessis, Y.N.3
  • 16
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • A. Peschel, How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10 (2002), pp. 179-186.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 17
    • 0033042432 scopus 로고    scopus 로고
    • Peptide antibiotics Antimicrob
    • R.E.W. Hancock and D.S. Chapple, Peptide antibiotics, Antimicrob. Agents Chemother. 43 (1999), pp. 1317-1323.
    • (1999) Agents Chemother. , vol.43 , pp. 1317-1323
    • Hancock, R.E.W.1    Chapple, D.S.2
  • 19
    • 34548316598 scopus 로고    scopus 로고
    • Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data
    • A. Langham, A. Waring, and Y. Kaznessis, Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data, BMC Biochem. 8 (2007), 11.
    • (2007) BMC Biochem , vol.8 , pp. 11
    • Langham, A.1    Waring, A.2    Kaznessis, Y.3
  • 20
    • 41549125949 scopus 로고    scopus 로고
    • On the nature of antimicrobial activity: A model for protegrin-1 pores
    • A.A. Langham, A.S. Ahmad, and Y.N. Kaznessis, On the nature of antimicrobial activity: a model for protegrin-1 pores, J. Am. Chem. Soc. 130 (2008), pp. 4338-4346.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4338-4346
    • Langham, A.A.1    Ahmad, A.S.2    Kaznessis, Y.N.3
  • 21
    • 62849091215 scopus 로고    scopus 로고
    • Determining the orientation of protegrin-1 in DLPC bilayers using an implicit solventmembrane model in PLoS one
    • A. Sayyed-Ahmad and Y.N. Kaznessis, Determining the orientation of protegrin-1 in DLPC bilayers using an implicit solventmembrane model in PLoS one, Public Libr. Sci. 4 (2009), e4799.
    • (2009) Public Libr. Sci. , vol.4
    • Sayyed-Ahmad, A.1    Kaznessis, Y.N.2
  • 22
    • 59149103015 scopus 로고    scopus 로고
    • Poisson-Nernst-Planck models of nonequilibrium ion electrodiffusion through a protegrin transmembrane pore PLoS
    • D.S. Bolintineanu, A. Sayyed-Ahmad, H.T. Davis, and Y.N. Kaznessis, Poisson-Nernst-Planck models of nonequilibrium ion electrodiffusion through a protegrin transmembrane pore, PLoS Comput. Biol. 5 (2009), e1000277.
    • (2009) Comput. Biol. , vol.5
    • Bolintineanu, D.S.1    Sayyed-Ahmad, A.2    Davis, H.T.3    Kaznessis, Y.N.4
  • 25
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • M.R. Yeaman and N.Y. Yount, Mechanisms of antimicrobial peptide action and resistance, Pharmacol. Rev. 55 (2003), pp. 27-55.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 27
    • 4544349379 scopus 로고    scopus 로고
    • Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs
    • K. Lee, S.Y. Shin, K. Kim, S.S. Lim, and K.-S. Hahm, Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs, Biochem. Biophys. Res. Commun. 323 (2004), pp. 712-719.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 712-719
    • Lee, K.1    Shin, S.Y.2    Kim, K.3    Lim, S.S.4    Hahm, K.-S.5
  • 28
    • 0033405041 scopus 로고    scopus 로고
    • Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7
    • L.T. Chong, Y. Duan, L. Wang, I. Massova, and P.A. Kollman, Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7, PNAS 96 (1999), pp. 14330-14335.
    • (1999) PNAS , vol.96 , pp. 14330-14335
    • Chong, L.T.1    Duan, Y.2    Wang, L.3    Massova, I.4    Kollman, P.A.5
  • 29
    • 0033543147 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution
    • T. Wymore, X.F. Gao, and T.C. Wong, Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution, J. Mol. Struct. 195 (1999), pp. 195-210.
    • (1999) J. Mol. Struct. , vol.195 , pp. 195-210
    • Wymore, T.1    Gao, X.F.2    Wong, T.C.3
  • 30
    • 0036675379 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Adrenocorticotropin (1-24) peptide in a solvated dodecylphosphocholine (DPC) micelle and in a Dimyistoylphosphatidylcholine (DMPC) bilayer
    • T. Wong and S. Kamath, Molecular dynamics simulations of Adrenocorticotropin (1-24) peptide in a solvated dodecylphosphocholine (DPC) micelle and in a Dimyistoylphosphatidylcholine (DMPC) bilayer, J. Biomol. Struct. Dyn. 20 (2002), pp. 39-57.
    • (2002) J. Biomol. Struct. Dyn. , vol.20 , pp. 39-57
    • Wong, T.1    Kamath, S.2
  • 31
    • 0347963579 scopus 로고
    • Molecular Dynamics Simulation Analysis of a sodium dodecyl sulfate micelle in aqueous solution: Decreased fluidity of the micelle hydrocarbon interior
    • A. MacKerell, Molecular Dynamics Simulation Analysis of a sodium dodecyl sulfate micelle in aqueous solution: decreased fluidity of the micelle hydrocarbon interior, J. Phys. Chem. 99 (1995), pp. 1846-1855.
    • (1995) J. Phys. Chem. , vol.99 , pp. 1846-1855
    • MacKerell, A.1
  • 34
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • S.E. Feller and J.A.D. MacKerell, An improved empirical potential energy function for molecular simulations of phospholipids, J. Phys. Chem. B 104 (2000), pp. 7510-7515.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, J.A.D.2
  • 36
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • H. Andersen, Molecular dynamics simulations at constant pressure and/or temperature, J. Chem. Phys. 72 (1980), pp. 2384-2393.
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.1
  • 37
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W. Hoover, Canonical dynamics:equilibrium phase-space distributions, Phys. Rev. A 31 (1985), pp. 1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.1
  • 38
    • 33846823909 scopus 로고
    • Particle mesh Ewald:an N log(N) methods for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen, Particle mesh Ewald:an N log(N) methods for Ewald sums in large systems, J. Chem. Phys. 98 (1993), pp. 100089-110092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 100089-110092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 40
    • 0000871204 scopus 로고
    • Multiconfiguration thermodynamic integration
    • T. Straatsma and J. McCammon, Multiconfiguration thermodynamic integration, J. Chem. Phys. 95 (1991), pp. 1175-1188.
    • (1991) J. Chem. Phys. , vol.95 , pp. 1175-1188
    • Straatsma, T.1    McCammon, J.2
  • 41
    • 0034900495 scopus 로고    scopus 로고
    • Free energy decomposition of proteinprotein interactions
    • S.Y. Noskov and C. Lim, Free energy decomposition of proteinprotein interactions, Biophys. J. 81 (2001), pp. 737-750.
    • (2001) Biophys. J. , vol.81 , pp. 737-750
    • Noskov, S.Y.1    Lim, C.2
  • 42
    • 0028360307 scopus 로고
    • The contribution of vibrational entropy to molecular association: The dimerization of insulin
    • B. Tidor and M. Karplus, The contribution of vibrational entropy to molecular association: the dimerization of insulin, J. Mol. Biol. 238 (1994), pp. 405-414.
    • (1994) J. Mol. Biol. , vol.238 , pp. 405-414
    • Tidor, B.1    Karplus, M.2
  • 44
    • 0027166270 scopus 로고
    • Empirical scale of side-chain conformational entropy in protein folding
    • S.D. Pickett and M.J.E. Sternberg, Empirical scale of side-chain conformational entropy in protein folding, J. Mol. Biol. 231 (1993), pp. 825-839.
    • (1993) J. Mol. Biol. , vol.231 , pp. 825-839
    • Pickett, S.D.1    Sternberg, M.J.E.2
  • 45
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • B. Honig and A. Nicholls, Classical electrostatics in biology and chemistry, Science 268 (1995), pp. 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 46
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • D. Chandler, Interfaces and the driving force of hydrophobic assembly, Nature 437 (2005), pp. 640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 47
    • 0033972258 scopus 로고    scopus 로고
    • Relative energies of binding for antibody-carbohydrate-antigen complexes computed from freeenergy simulations
    • A. Pathiaseril and R.J. Woods, Relative energies of binding for antibody-carbohydrate-antigen complexes computed from freeenergy simulations, J. Am. Chem. Soc. 122 (2000), pp. 331-338.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 331-338
    • Pathiaseril, A.1    Woods, R.J.2
  • 48
    • 0003241140 scopus 로고    scopus 로고
    • Free energies of hydration from thermodynamic integration: Comparison of molecular mechanics force fields and evaluation of calculation accuracy
    • R.C.W. Volkhard Helms, Free energies of hydration from thermodynamic integration: comparison of molecular mechanics force fields and evaluation of calculation accuracy, J. Comput. Chem. 18 (1997), pp. 449-462.
    • (1997) J. Comput. Chem. , vol.18 , pp. 449-462
    • Helms Volkhard, W.R.C.1
  • 49
    • 0346971105 scopus 로고    scopus 로고
    • Performance comparison of generalized Born and Poisson methods in the calculation of electrostatic solvation energies for protein structures
    • M. Feig, A. Onufriev, M.S. Lee, W. Im, D.A. Case, and C.L. Brooks III, Performance comparison of generalized Born and Poisson methods in the calculation of electrostatic solvation energies for protein structures, J. Comput. Chem. 25 (2004), pp. 265-284.
    • (2004) J. Comput. Chem. , vol.25 , pp. 265-284
    • Feig, M.1    Onufriev, A.2    Lee, M.S.3    Im, W.4    Case, D.A.5    Brooks III, C.L.6
  • 50
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: Computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • W. Im, D. Beglov, and B. Roux, Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation, Comput. Phys. Commun. 111 (1998), pp. 59-75.
    • (1998) Comput. Phys. Commun. , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 51
    • 2542429164 scopus 로고    scopus 로고
    • Efficient solution technique for solving the Poisson-Boltzmann equation
    • A. Sayyed-Ahmad, K. Tuncay, and P.J. Ortoleva, Efficient solution technique for solving the Poisson-Boltzmann equation, J. Comput. Chem. 25 (2004), pp. 1068-1074.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1068-1074
    • Sayyed-Ahmad, A.1    Tuncay, K.2    Ortoleva, P.J.3
  • 52
    • 33644844890 scopus 로고    scopus 로고
    • Energetics of the native and non-native states of the glycophorin transmembrane helix dimer
    • M. Mottamal, J. Zhang, and T. Lazaridis, Energetics of the native and non-native states of the glycophorin transmembrane helix dimer, Proteins 62 (2006), pp. 996-1009.
    • (2006) Proteins , vol.62 , pp. 996-1009
    • Mottamal, M.1    Zhang, J.2    Lazaridis, T.3
  • 53
    • 1442300070 scopus 로고    scopus 로고
    • Free energy simulations and MM-PBSA analyses on the affinity and specificity of steroid binding to antiestradiol antibody
    • T. Laitinen, J.A. Kankare, and M. Peräkylä, Free energy simulations and MM-PBSA analyses on the affinity and specificity of steroid binding to antiestradiol antibody, Proteins 55 (2004), pp. 34-43.
    • (2004) Proteins , vol.55 , pp. 34-43
    • Laitinen, T.1    Kankare, J.A.2    Peräkylä, M.3
  • 54
    • 33749447306 scopus 로고    scopus 로고
    • A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides
    • A. Ganoth, R. Friedman, E. Nachliel, and M. Gutman, A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides, Biophys. J. 91 (2006), pp. 2436-2450.
    • (2006) Biophys. J. , vol.91 , pp. 2436-2450
    • Ganoth, A.1    Friedman, R.2    Nachliel, E.3    Gutman, M.4
  • 55
    • 0031277394 scopus 로고    scopus 로고
    • Molecular docking of superantigens with class II major histocompatibility complex proteins
    • L.C. Mark and A. Olson, Molecular docking of superantigens with class II major histocompatibility complex proteins, J. Mol. Recognit. 10 (1997), pp. 277-289.
    • (1997) J. Mol. Recognit. , vol.10 , pp. 277-289
    • Mark, L.C.1    Olson, A.2
  • 57
    • 0347602124 scopus 로고    scopus 로고
    • Converging free energy estimates: MMPB( GB)SA studies on the protein-protein complex Ras-Raf
    • D.A.C. Holger Gohlke, Converging free energy estimates: MMPB( GB)SA studies on the protein-protein complex Ras-Raf, J. Comput. Chem. 25 (2004), pp. 238-250.
    • (2004) J. Comput. Chem. , vol.25 , pp. 238-250
    • Gohlke Holger, C.D.A.1
  • 58
    • 17044372385 scopus 로고    scopus 로고
    • Absolute and relative entropies from computer simulation with applications to ligand binding
    • J. Carlsson and J. Aqvist, Absolute and relative entropies from computer simulation with applications to ligand binding, J. Phys. Chem. B 109 (2005), pp. 6448-6456.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 6448-6456
    • Carlsson, J.1    Aqvist, J.2
  • 59
    • 33646178918 scopus 로고    scopus 로고
    • Calculation of absolute protein-ligand binding affinity using path and endpoint approaches
    • M.S. Lee and M.A. Olson, Calculation of absolute protein-ligand binding affinity using path and endpoint approaches, Biophys. J. 90 (2006), pp. 864-877.
    • (2006) Biophys. J. , vol.90 , pp. 864-877
    • Lee, M.S.1    Olson, M.A.2
  • 60
    • 24344456625 scopus 로고    scopus 로고
    • Study of the insulin dimerization: Binding free energy calculations and per-residue free energy decomposition
    • V. Zoete, M. Meuwly, and M. Karplus, Study of the insulin dimerization: binding free energy calculations and per-residue free energy decomposition, Proteins: Struct. Function Bioinf. 61 (2005), pp. 79-93.
    • (2005) Proteins: Struct. Function Bioinf. , vol.61 , pp. 79-93
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 61
    • 27744467398 scopus 로고    scopus 로고
    • Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: What do point mutations achieve?
    • H. Khandelia and Y.N. Kaznessis, Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: what do point mutations achieve? Peptides 26 (2005), pp. 2037-2049.
    • (2005) Peptides , vol.26 , pp. 2037-2049
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 62
    • 22344445910 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the helical antimicrobial peptide ovispirin-1 in a zwitterionic dodecylphosphocholine micelle: Insights into host-cell toxicity
    • H. Khandelia and Y.N. Kaznessis, Molecular dynamics simulations of the helical antimicrobial peptide ovispirin-1 in a zwitterionic dodecylphosphocholine micelle: insights into host-cell toxicity, J. Phys. Chem. B 109 (2005), pp. 12990-12996.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 12990-12996
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 63
    • 28144436374 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: Conformational analysis of peptide and lipids
    • P. Lague, B. Roux, and R.W. Pastor, Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: conformational analysis of peptide and lipids, J. Mol. Biol. 354 (2005), pp. 1129-1141.
    • (2005) J. Mol. Biol. , vol.354 , pp. 1129-1141
    • Lague, P.1    Roux, B.2    Pastor, R.W.3
  • 64
    • 0035017426 scopus 로고    scopus 로고
    • Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle
    • T.C.W. Xinfeng Gao, Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle, Biopolymers 58 (2001), pp. 643-659.
    • (2001) Biopolymers , vol.58 , pp. 643-659
    • GaoXinfeng, W.T.C.1
  • 65
    • 0033047067 scopus 로고    scopus 로고
    • Molecular dynamics study of substance P peptides partitioned in a sodium dodecylsulfate micelle
    • T. Wymore and T.C. Wong, Molecular dynamics study of substance P peptides partitioned in a sodium dodecylsulfate micelle, Biophys. J. 76 (1999), pp. 1213-1227. (Pubitemid 29262604)
    • (1999) Biophysical Journal , vol.76 , Issue.3 , pp. 1213-1227
    • Wymore, T.1    Wong, T.C.2
  • 66
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics versus environment: Simulations of OmpA in a micelle and in a bilayer
    • P.J. Bond and M.S.P. Sansom, Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer, J. Mol. Biol. 329 (2003), pp. 1035-1053.
    • (2003) J. Mol. Biol. , vol.329 , pp. 1035-1053
    • Bond, P.J.1    Sansom, M.S.P.2
  • 67
    • 84973857317 scopus 로고
    • Self organization of stable category recognition codes for analog input patterns
    • G.A. Carpenter and S. Grossberg, Self organization of stable category recognition codes for analog input patterns, Appl. Opt. 26 (1987), pp. 4919-4930.
    • (1987) Appl. Opt. , vol.26 , pp. 4919-4930
    • Carpenter, G.A.1    Grossberg, S.2
  • 68
    • 0027393187 scopus 로고
    • Statistical clustering techniques for the analysis of long molecular dynamics trajectories: Analysis of 2.2-ns trajectories of YPGDV
    • M.E. Karpen, D.J. Tobias, and C.L. Brooks III, Statistical clustering techniques for the analysis of long molecular dynamics trajectories: analysis of 2.2-ns trajectories of YPGDV, Biochemistry 32 (1993), pp. 412-420.
    • (1993) Biochemistry , vol.32 , pp. 412-420
    • Karpen, M.E.1    Tobias, D.J.2    Brooks III, C.L.3
  • 70
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritrpticin bound to micelles: A distinct membrane-bound peptide fold
    • D.J. Schibli, P.M. Hwang, and H.J. Vogel, Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold, Biochemistry 38 (1999), pp. 16749-16755.
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 71
    • 0038702321 scopus 로고    scopus 로고
    • The structure of the antimicrobial peptide Ac-RRWWRF-NH2 bound to micelles and its interactions with phospholipid bilayers
    • W. Jing, H.N. Hunter, J. Hagel, H.J. Vogel, The structure of the antimicrobial peptide Ac-RRWWRF-NH2 bound to micelles and its interactions with phospholipid bilayers, J. Pept. Res. 61 (2003), pp. 219-229.
    • (2003) J. Pept. Res. , vol.61 , pp. 219-229
    • Jing, W.1    Hunter, H.N.2    Hagel, J.3    Vogel, H.J.4
  • 73
    • 0038375258 scopus 로고    scopus 로고
    • Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR
    • M. Lindberg, H. Biverstahl, A. Graslund, and L. Maler, Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR, Eur. J. Biochem. 270 (2003), pp. 3055-3063.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3055-3063
    • Lindberg, M.1    Biverstahl, H.2    Graslund, A.3    Maler, L.4
  • 75
    • 0347963579 scopus 로고
    • Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: Decreased fluidity of the micelle hydrocarbon interior
    • A. MacKerrell, Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: decreased fluidity of the micelle hydrocarbon interior, J. Phys. Chem. 99 (1995), pp. 327-341.
    • (1995) J. Phys. Chem. , vol.99 , pp. 327-341
    • MacKerrell, A.1
  • 76
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • A. Rozek, C.L. Friedrich, and R.E.W. Hancock, Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles, Biochemistry 39 (2000), pp. 15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.W.3
  • 77
    • 0035895423 scopus 로고    scopus 로고
    • Binding free energies and free energy components from molecular dynamics and Poisson- Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase
    • G. Archontis, T. Simonson, and M. Karplus, Binding free energies and free energy components from molecular dynamics and Poisson- Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase, J. Mol. Biol. 306 (2001), pp. 307-327.
    • (2001) J. Mol. Biol. , vol.306 , pp. 307-327
    • Archontis, G.1    Simonson, T.2    Karplus, M.3


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