메뉴 건너뛰기




Volumn 105, Issue 9, 2013, Pages 2093-2103

Mechanism of membrane permeation induced by synthetic β-hairpin peptides

Author keywords

[No Author keywords available]

Indexed keywords

LIPOSOME; PEPTIDE;

EID: 84887369179     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.09.040     Document Type: Article
Times cited : (32)

References (55)
  • 1
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Y. Shai Mode of action of membrane active antimicrobial peptides Biopolymers 66 2002 236 248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 2
    • 33845373255 scopus 로고    scopus 로고
    • Host defense peptides and lipopeptides: Modes of action and potential candidates for the treatment of bacterial and fungal infections
    • Y. Shai, A. Makovitzky, and D. Avrahami Host defense peptides and lipopeptides: modes of action and potential candidates for the treatment of bacterial and fungal infections Curr. Protein Pept. Sci. 7 2006 479 486
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 479-486
    • Shai, Y.1    Makovitzky, A.2    Avrahami, D.3
  • 3
    • 84884356283 scopus 로고    scopus 로고
    • Properties and mechanisms of action of naturally occurring antifungal peptides
    • 10.1007/s00018-00013-01260-00011
    • N.L. van der Weerden, M.R. Bleackley, and M.A. Anderson Properties and mechanisms of action of naturally occurring antifungal peptides Cell. Mol. Life Sci. 70 2013 3545 3570 10.1007/s00018-00013-01260-00011
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 3545-3570
    • Van Der Weerden, N.L.1    Bleackley, M.R.2    Anderson, M.A.3
  • 4
    • 33746842648 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment
    • J.S. Mader, and D.W. Hoskin Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment Expert Opin. Investig. Drugs 15 2006 933 946
    • (2006) Expert Opin. Investig. Drugs , vol.15 , pp. 933-946
    • Mader, J.S.1    Hoskin, D.W.2
  • 5
    • 84859562228 scopus 로고    scopus 로고
    • Anticancer β-hairpin peptides: Membrane-induced folding triggers activity
    • C. Sinthuvanich, and A.S. Veiga J.P. Schneider Anticancer β-hairpin peptides: membrane-induced folding triggers activity J. Am. Chem. Soc. 134 2012 6210 6217
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6210-6217
    • Sinthuvanich, C.1    Veiga, A.S.2    Schneider, J.P.3
  • 6
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • D.W. Hoskin, and A. Ramamoorthy Studies on anticancer activities of antimicrobial peptides Biochim. Biophys. Acta 1778 2008 357 375
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 7
    • 36749074939 scopus 로고    scopus 로고
    • Inherent antibacterial activity of a peptide-based beta-hairpin hydrogel
    • D.A. Salick, and J.K. Kretsinger J.P. Schneider Inherent antibacterial activity of a peptide-based beta-hairpin hydrogel J. Am. Chem. Soc. 129 2007 14793 14799
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14793-14799
    • Salick, D.A.1    Kretsinger, J.K.2    Schneider, J.P.3
  • 8
    • 4744350913 scopus 로고    scopus 로고
    • Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus
    • B. Ozbas, and J. Kretsinger D.J. Pochan Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus Macromolecules 37 2004 7331 7337
    • (2004) Macromolecules , vol.37 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Pochan, D.J.3
  • 9
    • 70349173315 scopus 로고    scopus 로고
    • Tuning the pH responsiveness of beta-hairpin peptide folding, self-assembly, and hydrogel material formation
    • K. Rajagopal, and M.S. Lamm J.P. Schneider Tuning the pH responsiveness of beta-hairpin peptide folding, self-assembly, and hydrogel material formation Biomacromolecules 10 2009 2619 2625
    • (2009) Biomacromolecules , vol.10 , pp. 2619-2625
    • Rajagopal, K.1    Lamm, M.S.2    Schneider, J.P.3
  • 10
    • 0037132592 scopus 로고    scopus 로고
    • Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide
    • J.P. Schneider, and D.J. Pochan J. Kretsinger Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide J. Am. Chem. Soc. 124 2002 15030 15037
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Kretsinger, J.3
  • 11
    • 0019331570 scopus 로고
    • Studies on the mechanism of membrane fusion: Kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle contents
    • J. Wilschut, and N. Düzgüneş D. Papahadjopoulos Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle contents Biochemistry 19 1980 6011 6021
    • (1980) Biochemistry , vol.19 , pp. 6011-6021
    • Wilschut, J.1    Düzgüneş, N.2    Papahadjopoulos, D.3
  • 12
    • 78049324771 scopus 로고    scopus 로고
    • Cell-penetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid
    • S.T. Yang, and E. Zaitseva K. Melikov Cell-penetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid Biophys. J. 99 2010 2525 2533
    • (2010) Biophys. J. , vol.99 , pp. 2525-2533
    • Yang, S.T.1    Zaitseva, E.2    Melikov, K.3
  • 13
    • 84877737915 scopus 로고    scopus 로고
    • Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)
    • D.K. Lee, and J.R. Brender A. Ramamoorthy Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78) Biochemistry 52 2013 3254 3263
    • (2013) Biochemistry , vol.52 , pp. 3254-3263
    • Lee, D.K.1    Brender, J.R.2    Ramamoorthy, A.3
  • 14
    • 0019871607 scopus 로고
    • Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins
    • J.N. Weinstein, and R.D. Klausner R. Blumenthal Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins Biochim. Biophys. Acta 647 1981 270 284
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 270-284
    • Weinstein, J.N.1    Klausner, R.D.2    Blumenthal, R.3
  • 15
    • 84986512474 scopus 로고
    • Charmm - A program for macromolecular energy, minimization, and dynamics calculations
    • B.R. Brooks, and R.E. Bruccoleri M. Karplus Charmm - a program for macromolecular energy, minimization, and dynamics calculations J. Comput. Chem. 4 1983 187 217
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Karplus, M.3
  • 16
    • 78649529340 scopus 로고    scopus 로고
    • β-Barrel topology of Alzheimer's β-amyloid ion channels
    • H. Jang, and F.T. Arce R. Nussinov β-Barrel topology of Alzheimer's β-amyloid ion channels J. Mol. Biol. 404 2010 917 934
    • (2010) J. Mol. Biol. , vol.404 , pp. 917-934
    • Jang, H.1    Arce, F.T.2    Nussinov, R.3
  • 17
    • 58149311146 scopus 로고    scopus 로고
    • Models of toxic β-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer β-amyloid ion channels
    • H. Jang, and B. Ma R. Nussinov Models of toxic β-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer β-amyloid ion channels Biophys. J. 95 2008 4631 4642
    • (2008) Biophys. J. , vol.95 , pp. 4631-4642
    • Jang, H.1    Ma, B.2    Nussinov, R.3
  • 18
    • 77952960621 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms ion channels: Molecular dynamic simulation, atomic force microscopy, and electrical conductance studies
    • R. Capone, and M. Mustata R. Lal Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies Biophys. J. 98 2010 2644 2652
    • (2010) Biophys. J. , vol.98 , pp. 2644-2652
    • Capone, R.1    Mustata, M.2    Lal, R.3
  • 19
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • G.E. Schulz The structure of bacterial outer membrane proteins Biochim. Biophys. Acta 1565 2002 308 317
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 20
    • 0029124070 scopus 로고
    • Transbilayer pores formed by beta-barrels: Molecular modeling of pore structures and properties
    • M.S. Sansom, and I.D. Kerr Transbilayer pores formed by beta-barrels: molecular modeling of pore structures and properties Biophys. J. 69 1995 1334 1343
    • (1995) Biophys. J. , vol.69 , pp. 1334-1343
    • Sansom, M.S.1    Kerr, I.D.2
  • 21
    • 34548788549 scopus 로고    scopus 로고
    • Models of β-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • H. Jang, J. Zheng, and R. Nussinov Models of β-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process Biophys. J. 93 2007 1938 1949
    • (2007) Biophys. J. , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 22
    • 38949167084 scopus 로고    scopus 로고
    • New structures help the modeling of toxic amyloidbeta ion channels
    • H. Jang, and J. Zheng R. Nussinov New structures help the modeling of toxic amyloidbeta ion channels Trends Biochem. Sci. 33 2008 91 100
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 91-100
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 23
    • 72549099399 scopus 로고    scopus 로고
    • Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels
    • H. Jang, and F.T. Arce R. Nussinov Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels Biophys. J. 97 2009 3029 3037
    • (2009) Biophys. J. , vol.97 , pp. 3029-3037
    • Jang, H.1    Arce, F.T.2    Nussinov, R.3
  • 24
    • 77954949785 scopus 로고    scopus 로고
    • Structural convergence among diverse, toxic β-sheet ion channels
    • H. Jang, and F. Teran Arce R. Nussinov Structural convergence among diverse, toxic β-sheet ion channels J. Phys. Chem. B 114 2010 9445 9451
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9445-9451
    • Jang, H.1    Teran Arce, F.2    Nussinov, R.3
  • 25
    • 77950890953 scopus 로고    scopus 로고
    • Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome
    • H. Jang, and F.T. Arce R. Lal Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome Proc. Natl. Acad. Sci. USA 107 2010 6538 6543
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6538-6543
    • Jang, H.1    Arce, F.T.2    Lal, R.3
  • 26
    • 70350043396 scopus 로고    scopus 로고
    • K3 fragment of amyloidogenic β(2)-microglobulin forms ion channels: Implication for dialysis related amyloidosis
    • M. Mustata, and R. Capone R. Nussinov K3 fragment of amyloidogenic β(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis J. Am. Chem. Soc. 131 2009 14938 14945
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14938-14945
    • Mustata, M.1    Capone, R.2    Nussinov, R.3
  • 27
    • 34247625467 scopus 로고    scopus 로고
    • Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect
    • H. Jang, B. Ma, and R. Nussinov Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect BMC Struct. Biol. 7 2007 21
    • (2007) BMC Struct. Biol. , vol.7 , pp. 21
    • Jang, H.1    Ma, B.2    Nussinov, R.3
  • 28
    • 16244391442 scopus 로고    scopus 로고
    • Determination of peptide oligomerization in lipid bilayers using 19F spin diffusion NMR
    • J.J. Buffy, A.J. Waring, and M. Hong Determination of peptide oligomerization in lipid bilayers using 19F spin diffusion NMR J. Am. Chem. Soc. 127 2005 4477 4483
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4477-4483
    • Buffy, J.J.1    Waring, A.J.2    Hong, M.3
  • 29
    • 33745855891 scopus 로고    scopus 로고
    • Membrane-bound dimer structure of a β-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR
    • R. Mani, and M. Tang M. Hong Membrane-bound dimer structure of a β-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR Biochemistry 45 2006 8341 8349
    • (2006) Biochemistry , vol.45 , pp. 8341-8349
    • Mani, R.1    Tang, M.2    Hong, M.3
  • 30
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • M. Tang, A.J. Waring, and M. Hong Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR J. Am. Chem. Soc. 129 2007 11438 11446
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 32
    • 70350151198 scopus 로고    scopus 로고
    • Targeting phosphatidylserine in anti-cancer therapy
    • H. Kenis, and C. Reutelingsperger Targeting phosphatidylserine in anti-cancer therapy Curr. Pharm. Des. 15 2009 2719 2723
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 2719-2723
    • Kenis, H.1    Reutelingsperger, C.2
  • 33
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • M.T. Lee, and W.C. Hung H.W. Huang Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides Proc. Natl. Acad. Sci. USA 105 2008 5087 5092
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5087-5092
    • Lee, M.T.1    Hung, W.C.2    Huang, H.W.3
  • 34
    • 77956761543 scopus 로고    scopus 로고
    • Kinetic pathway of antimicrobial peptide magainin 2-induced pore formation in lipid membranes
    • Y. Tamba, and H. Ariyama M. Yamazaki Kinetic pathway of antimicrobial peptide magainin 2-induced pore formation in lipid membranes J. Phys. Chem. B 114 2010 12018 12026
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12018-12026
    • Tamba, Y.1    Ariyama, H.2    Yamazaki, M.3
  • 35
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • R. Mani, and S.D. Cady M. Hong Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR Proc. Natl. Acad. Sci. USA 103 2006 16242 16247
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Hong, M.3
  • 36
    • 84883409216 scopus 로고    scopus 로고
    • Process of inducing pores in membranes by melittin
    • M.T. Lee, and T.L. Sun H.W. Huang Process of inducing pores in membranes by melittin Proc. Natl. Acad. Sci. USA 110 2013 14243 14248
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 14243-14248
    • Lee, M.T.1    Sun, T.L.2    Huang, H.W.3
  • 37
    • 33749535555 scopus 로고    scopus 로고
    • Interaction of protegrin-1 with lipid bilayers: Membrane thinning effect
    • H. Jang, and B. Ma R. Nussinov Interaction of protegrin-1 with lipid bilayers: membrane thinning effect Biophys. J. 91 2006 2848 2859
    • (2006) Biophys. J. , vol.91 , pp. 2848-2859
    • Jang, H.1    Ma, B.2    Nussinov, R.3
  • 38
    • 79959651424 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link
    • H. Jang, and F.T. Arce R. Lal Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link Biophys. J. 100 2011 1775 1783
    • (2011) Biophys. J. , vol.100 , pp. 1775-1783
    • Jang, H.1    Arce, F.T.2    Lal, R.3
  • 39
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • R.L. Fahrner, and T. Dieckmann J. Feigon Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes Chem. Biol. 3 1996 543 550
    • (1996) Chem. Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Feigon, J.3
  • 40
    • 0031925507 scopus 로고    scopus 로고
    • β-sheet antibiotic peptides as potential dental therapeutics
    • K.T. Miyasaki, and R.I. Lehrer β-sheet antibiotic peptides as potential dental therapeutics Int. J. Antimicrob. Agents 9 1998 269 280
    • (1998) Int. J. Antimicrob. Agents , vol.9 , pp. 269-280
    • Miyasaki, K.T.1    Lehrer, R.I.2
  • 41
  • 42
    • 50849120027 scopus 로고    scopus 로고
    • Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1
    • L.M. Gottler, and R. de la Salud Bea E.N. Marsh Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1 Biochemistry 47 2008 9243 9250
    • (2008) Biochemistry , vol.47 , pp. 9243-9250
    • Gottler, L.M.1    De La Salud Bea, R.2    Marsh, E.N.3
  • 43
    • 0018881828 scopus 로고
    • Comparative properties and methods of preparation of lipid vesicles (liposomes)
    • F. Szoka Jr., and D. Papahadjopoulos Comparative properties and methods of preparation of lipid vesicles (liposomes) Annu. Rev. Biophys. Bioeng. 9 1980 467 508
    • (1980) Annu. Rev. Biophys. Bioeng. , vol.9 , pp. 467-508
    • Szoka, Jr.F.1    Papahadjopoulos, D.2
  • 44
    • 0021102360 scopus 로고
    • Physicochemical characterization of large unilamellar phospholipid vesicles prepared by reverse-phase evaporation
    • N. Düzgüneş, and J. Wilschut D. Papahadjopoulos Physicochemical characterization of large unilamellar phospholipid vesicles prepared by reverse-phase evaporation Biochim. Biophys. Acta 732 1983 289 299
    • (1983) Biochim. Biophys. Acta , vol.732 , pp. 289-299
    • Düzgüneş, N.1    Wilschut, J.2    Papahadjopoulos, D.3
  • 45
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • B.N. Ames, and D.T. Dubin The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid J. Biol. Chem. 235 1960 769 775
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 46
    • 59049093067 scopus 로고    scopus 로고
    • Nanoparticles of cationic chimeric peptide and sodium polyacrylate exhibit striking antinociception activity at lower dose
    • K. Gupta, and V.P. Singh S. Maiti Nanoparticles of cationic chimeric peptide and sodium polyacrylate exhibit striking antinociception activity at lower dose J. Control. Release 134 2009 47 54
    • (2009) J. Control. Release , vol.134 , pp. 47-54
    • Gupta, K.1    Singh, V.P.2    Maiti, S.3
  • 47
    • 77649218400 scopus 로고    scopus 로고
    • Methods to monitor liposome fusion, permeability, and interaction with cells
    • N. Düzgüneş, H. Faneca, and M.C. Lima Methods to monitor liposome fusion, permeability, and interaction with cells Methods Mol. Biol. 606 2010 209 232
    • (2010) Methods Mol. Biol. , vol.606 , pp. 209-232
    • Düzgüneş, N.1    Faneca, H.2    Lima, M.C.3
  • 48
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • N. Kucerka, S. Tristram-Nagle, and J.F. Nagle Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains J. Membr. Biol. 208 2005 193 202
    • (2005) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 49
    • 1542285301 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl
    • P. Mukhopadhyay, L. Monticelli, and D.P. Tieleman Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl Biophys. J. 86 2004 1601 1609
    • (2004) Biophys. J. , vol.86 , pp. 1601-1609
    • Mukhopadhyay, P.1    Monticelli, L.2    Tieleman, D.P.3
  • 50
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • J.B. Klauda, and R.M. Venable R.W. Pastor Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types J. Phys. Chem. B 114 2010 7830 7843
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1    Venable, R.M.2    Pastor, R.W.3
  • 51
    • 33751157933 scopus 로고
    • Solvent-induced forces between two hydrophilic groups
    • S.R. Durell, B.R. Brooks, and A. Bennaim Solvent-induced forces between two hydrophilic groups J. Phys. Chem. 98 1994 2198 2202
    • (1994) J. Phys. Chem. , vol.98 , pp. 2198-2202
    • Durell, S.R.1    Brooks, B.R.2    Bennaim, A.3
  • 52
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • A.D. Mackerell Jr., M. Feig, and C.L. Brooks III Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25 2004 1400 1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, Jr.A.D.1    Feig, M.2    Brooks III, C.L.3
  • 53
    • 84856298593 scopus 로고    scopus 로고
    • Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: Relevance to the ion channel mechanism of AD pathology
    • L. Connelly, and H. Jang R. Lal Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology J. Phys. Chem. B 116 2012 1728 1735
    • (2012) J. Phys. Chem. B , vol.116 , pp. 1728-1735
    • Connelly, L.1    Jang, H.2    Lal, R.3
  • 54
    • 84858308911 scopus 로고    scopus 로고
    • All-d-enantiomer of β-amyloid peptide forms ion channels in lipid bilayers
    • R. Capone, and H. Jang R. Lal All-d-enantiomer of β-amyloid peptide forms ion channels in lipid bilayers J. Chem. Theory Comput. 8 2012 1143 1152
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1143-1152
    • Capone, R.1    Jang, H.2    Lal, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.