메뉴 건너뛰기




Volumn 14, Issue 3, 2013, Pages 6241-6258

Adsorption and orientation of human islet amyloid polypeptide (hIAPP) Monomer at anionic lipid bilayers: Implications for membrane-mediated aggregation

Author keywords

Adsorption dynamics; Anionic palmitoyl oleolyohosphatidyl glycerol (POPG) bilayer; Binding orientation; Human islet amyloid polypeptide; Molecular dynamics simulations; Peptide lipid interaction; Type 2 diabetes

Indexed keywords

AMYLIN; PALMITOYLOLEOYLPHOSPHATIDYLGLYCEROL; PHOSPHATIDYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 84875495915     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14036241     Document Type: Article
Times cited : (32)

References (61)
  • 1
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D.J. Folding proteins in fatal ways. Nature 2003, 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The connections between equilibrium and kinetic behavior
    • Ferrone, F.A. Nucleation: The connections between equilibrium and kinetic behavior. Methods Enzymol. 2006, 412, 285-299.
    • (2006) Methods Enzymol. , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 4
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • Westermark, P.; Andersson, A.; Westermark, G.T. Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiol. Rev. 2011, 91, 795-826.
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 5
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A.; Mina, E.; Kayed, R.; Milton, S.C.; Parker, I.; Glabe, C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 2005, 280, 17294-17300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 7
    • 34547152267 scopus 로고    scopus 로고
    • Membrane interaction of islet amyloid polypeptide
    • Jayasinghe, S.A.; Langen, R. Membrane interaction of islet amyloid polypeptide. Biochim. Biophys. Acta 2007, 1768, 2002-2009.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2002-2009
    • Jayasinghe, S.A.1    Langen, R.2
  • 8
    • 67349142581 scopus 로고    scopus 로고
    • Membrane permeabilization by islet amyloid polypeptide
    • Engel, M.F.M. Membrane permeabilization by islet amyloid polypeptide. Chem. Phys. Lipids 2009, 160, 1-10.
    • (2009) Chem. Phys. Lipids , vol.160 , pp. 1-10
    • Engel, M.F.M.1
  • 9
    • 76149102617 scopus 로고    scopus 로고
    • Evidence for proteotoxicity in beta cells in Type 2 diabetes toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway
    • Gurlo, T.; Ryazantsev, S.; Huang, C.J.; Yeh, M.W.; Reber, H.A.; Hines, O.J.; O'Brien, T.D.; Glabe, C.G.; Butler, P.C. Evidence for proteotoxicity in beta cells in Type 2 diabetes toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. Am. J. Pathol. 2010, 176, 861-869.
    • (2010) Am. J. Pathol. , vol.176 , pp. 861-869
    • Gurlo, T.1    Ryazantsev, S.2    Huang, C.J.3    Yeh, M.W.4    Reber, H.A.5    Hines, O.J.6    O'Brien, T.D.7    Glabe, C.G.8    Butler, P.C.9
  • 10
    • 84858632761 scopus 로고    scopus 로고
    • Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
    • Brender, J.R.; Salamekh, S.; Ramamoorthy, A. Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective. Acc. Chem. Res. 2012, 45, 454-462.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 454-462
    • Brender, J.R.1    Salamekh, S.2    Ramamoorthy, A.3
  • 12
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • Butterfield, S.M.; Lashuel, H.A. Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems. Angew. Chem. Int. Edit. 2010, 49, 5628-5654.
    • (2010) Angew. Chem. Int. Edit. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 13
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda, J.A.; Miranker, A.D. The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes. Annu. Rev. Biophys2009, 38, 125-152.
    • (2009) Annu. Rev. Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 14
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type-2 diabetic-patients
    • Cooper, G.J.S.; Willis, A.C.; Clark, A.; Turner, R.C.; Sim, R.B.; Reid, K.B.M. Purification and characterization of a peptide from amyloid-rich pancreases of type-2 diabetic-patients. Proc. Natl. Acad. Sci. USA 1987, 84, 8628-8632.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8628-8632
    • Cooper, G.J.S.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.M.6
  • 15
    • 33845960266 scopus 로고    scopus 로고
    • Direct detection of transient alpha-helical states in islet amyloid polypeptide
    • Miranker, A.D.; Williamson, J.A. Direct detection of transient alpha-helical states in islet amyloid polypeptide. Protein Sci. 2007, 16, 110-117.
    • (2007) Protein Sci. , vol.16 , pp. 110-117
    • Miranker, A.D.1    Williamson, J.A.2
  • 16
    • 51849084313 scopus 로고    scopus 로고
    • Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state
    • Yonemoto, I.T.; Kroon, G.J.A.; Dyson, H.J.; Balch, W.E.; Kelly, J.W. Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state. Biochemistry 2008, 47, 9900-9910.
    • (2008) Biochemistry , vol.47 , pp. 9900-9910
    • Yonemoto, I.T.1    Kroon, G.J.A.2    Dyson, H.J.3    Balch, W.E.4    Kelly, J.W.5
  • 17
    • 72549109010 scopus 로고    scopus 로고
    • Evidence for a partially structured state of the amylin monomer
    • Vaiana, S.M.; Best, R.B.; Yau, W.M.; Eaton, W.A.; Hofrichter, J. Evidence for a partially structured state of the amylin monomer. Biophys. J. 2009, 97, 2948-2957.
    • (2009) Biophys. J. , vol.97 , pp. 2948-2957
    • Vaiana, S.M.1    Best, R.B.2    Yau, W.M.3    Eaton, W.A.4    Hofrichter, J.5
  • 18
    • 24644502612 scopus 로고    scopus 로고
    • Lipid membranes modulate the structure of islet amyloid polypeptide
    • Jayasinghe, S.A.; Langen, R. Lipid membranes modulate the structure of islet amyloid polypeptide. Biochemistry 2005, 44, 12113-12119.
    • (2005) Biochemistry , vol.44 , pp. 12113-12119
    • Jayasinghe, S.A.1    Langen, R.2
  • 19
    • 43949107500 scopus 로고    scopus 로고
    • Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide
    • Brender, J.R.; Lee, E.L.; Cavitt, M.A.; Gafni, A.; Steel, D.G.; Ramamoorthy, A. Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. J. Am. Chem. Soc. 2008, 130, 6424-6429.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6424-6429
    • Brender, J.R.1    Lee, E.L.2    Cavitt, M.A.3    Gafni, A.4    Steel, D.G.5    Ramamoorthy, A.6
  • 20
    • 70349428302 scopus 로고    scopus 로고
    • Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide
    • Williamson, J.A.; Loria, J.P.; Miranker, A.D. Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide. J. Mol. Biol. 2009, 393, 383-396.
    • (2009) J. Mol. Biol. , vol.393 , pp. 383-396
    • Williamson, J.A.1    Loria, J.P.2    Miranker, A.D.3
  • 21
    • 47749117154 scopus 로고    scopus 로고
    • Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding
    • Apostolidou, M.; Jayasinghe, S.A.; Langen, R. Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. J. Biol. Chem. 2008, 283, 17205-17210.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17205-17210
    • Apostolidou, M.1    Jayasinghe, S.A.2    Langen, R.3
  • 22
    • 66449087200 scopus 로고    scopus 로고
    • Dynamic alpha-helix structure of micelle-bound human amylin
    • Patil, S.M.; Xu, S.; Sheftic, S.R.; Alexandrescu, A.T. Dynamic alpha-helix structure of micelle-bound human amylin. J. Biol. Chem. 2009, 284, 11982-11991.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11982-11991
    • Patil, S.M.1    Xu, S.2    Sheftic, S.R.3    Alexandrescu, A.T.4
  • 23
    • 79960449390 scopus 로고    scopus 로고
    • Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment
    • Nanga, R.P.R.; Brender, J.R.; Vivekanandan, S.; Ramamoorthy, A. Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment. Biochim. Biophys. Acta 2011, 1808, 2337-2342.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2337-2342
    • Nanga, R.P.R.1    Brender, J.R.2    Vivekanandan, S.3    Ramamoorthy, A.4
  • 24
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide
    • Knight, J.D.; Hebda, J.A.; Miranker, A.D. Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide. Biochemistry 2006, 45, 9496-9508.
    • (2006) Biochemistry , vol.45 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 25
    • 77952682789 scopus 로고    scopus 로고
    • Effect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics simulations
    • Laghaei, R.; Mousseau, N.; Wei, G. Effect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics simulations. J. Phys. Chem. B 2010, 114, 7071-7077.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7071-7077
    • Laghaei, R.1    Mousseau, N.2    Wei, G.3
  • 26
    • 79955954237 scopus 로고    scopus 로고
    • Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations
    • Andrews, M.N.; Winter, R. Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations. Biophys. Chem. 2011, 156, 43-50.
    • (2011) Biophys. Chem. , vol.156 , pp. 43-50
    • Andrews, M.N.1    Winter, R.2
  • 27
    • 79955896407 scopus 로고    scopus 로고
    • The amyloid formation mechanism in human IAPP: Dimers have beta-strand monomer-monomer interfaces
    • Dupuis, N.F.; Wu, C.; Shea, J.E.; Bowers, M.T. The amyloid formation mechanism in human IAPP: Dimers have beta-strand monomer-monomer interfaces. J. Am. Chem. Soc. 2011, 133, 7240-7243.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7240-7243
    • Dupuis, N.F.1    Wu, C.2    Shea, J.E.3    Bowers, M.T.4
  • 28
    • 79953049279 scopus 로고    scopus 로고
    • Structure and thermodynamics of amylin dimer studied by hamiltonian-temperature replica exchange molecular dynamics simulations
    • Laghaei, R.; Mousseau, N.; Wei, G.H. Structure and thermodynamics of amylin dimer studied by hamiltonian-temperature replica exchange molecular dynamics simulations. J. Phys. Chem. B 2011, 115, 3146-3154.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 3146-3154
    • Laghaei, R.1    Mousseau, N.2    Wei, G.H.3
  • 29
    • 66249130413 scopus 로고    scopus 로고
    • Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding
    • Jiang, P.; Xu, W.; Mu, Y. Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding. PLoS Comput. Biol. 2009, 5, e1000357.
    • (2009) PLoS Comput. Biol. , vol.5
    • Jiang, P.1    Xu, W.2    Mu, Y.3
  • 30
    • 65149095089 scopus 로고    scopus 로고
    • Assembly dynamics of two-beta sheets revealed by molecular dynamics simulations
    • Xu, W.; Ping, J.; Li, W.; Mu, Y. Assembly dynamics of two-beta sheets revealed by molecular dynamics simulations. J. Chem. Phys. 2009, 130, 164709.
    • (2009) J. Chem. Phys. , vol.130 , pp. 164709
    • Xu, W.1    Ping, J.2    Li, W.3    Mu, Y.4
  • 31
    • 63649103441 scopus 로고    scopus 로고
    • Structural diversity of the soluble trimers of the human amylin(20-29) peptide revealed by molecular dynamics simulations
    • Mo, Y.; Lu, Y.; Wei, G.; Derreumaux, P. Structural diversity of the soluble trimers of the human amylin(20-29) peptide revealed by molecular dynamics simulations. J. Chem. Phys. 2009, 130, 125101-125106.
    • (2009) J. Chem. Phys. , vol.130 , pp. 125101-125106
    • Mo, Y.1    Lu, Y.2    Wei, G.3    Derreumaux, P.4
  • 32
    • 76149109093 scopus 로고    scopus 로고
    • Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides
    • Sciacca, M.F.M.; Pappalardo, M.; Attanasio, F.; Milardi, D.; La Rosa, C.; Grasso, D.M. Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides. New J. Chem. 2010, 34, 200-207.
    • (2010) New J. Chem. , vol.34 , pp. 200-207
    • Sciacca, M.F.M.1    Pappalardo, M.2    Attanasio, F.3    Milardi, D.4    la Rosa, C.5    Grasso, D.M.6
  • 33
    • 84868316813 scopus 로고    scopus 로고
    • Conformations of islet amyloid polypeptide monomers in a membrane environment: Implications for fibril formation
    • Duan, M.; Fan, J.; Huo, S. Conformations of islet amyloid polypeptide monomers in a membrane environment: Implications for fibril formation. PLoS One 2012, 7, e47150.
    • (2012) PLoS One , vol.7
    • Duan, M.1    Fan, J.2    Huo, S.3
  • 34
    • 84865652060 scopus 로고    scopus 로고
    • Probing ion channel activity of human islet amyloid polypeptide (amylin)
    • Zhao, J.; Luo, Y.; Jang, H.; Yu, X.; Wei, G.; Nussinov, R.; Zheng, J. Probing ion channel activity of human islet amyloid polypeptide (amylin). Biochim. Biophys. Acta 2012, 1818, 3121-3130.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 3121-3130
    • Zhao, J.1    Luo, Y.2    Jang, H.3    Yu, X.4    Wei, G.5    Nussinov, R.6    Zheng, J.7
  • 35
    • 84861707850 scopus 로고    scopus 로고
    • Lipid Interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations
    • Zhang, Y.; Luo, Y.; Deng, Y.; Mu, Y.; Wei, G. Lipid Interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations. PLoS One 2012, 7, e38191.
    • (2012) PLoS One , vol.7
    • Zhang, Y.1    Luo, Y.2    Deng, Y.3    Mu, Y.4    Wei, G.5
  • 37
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • Knight, J.D.; Miranker, A.D. Phospholipid catalysis of diabetic amyloid assembly. J. Mol. Biol. 2004, 341, 1175-1187.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 38
    • 36049013172 scopus 로고    scopus 로고
    • Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy
    • Lopes, D.H.J.; Meister, A.; Gohlke, A.; Hauser, A.; Blume, A.; Winter, R. Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. Biophys. J. 2007, 93, 3132-3141.
    • (2007) Biophys. J. , vol.93 , pp. 3132-3141
    • Lopes, D.H.J.1    Meister, A.2    Gohlke, A.3    Hauser, A.4    Blume, A.5    Winter, R.6
  • 39
    • 84864281394 scopus 로고    scopus 로고
    • Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer
    • Yu, X.; Zheng, J. Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer. J. Mol. Biol. 2012, 421, 561-571.
    • (2012) J. Mol. Biol. , vol.421 , pp. 561-571
    • Yu, X.1    Zheng, J.2
  • 40
    • 84862889934 scopus 로고    scopus 로고
    • Molecular interactions of alzheimer's Aβ protofilaments with lipid membranes
    • Tofoleanu, F.; Buchete, N.-V. Molecular interactions of alzheimer's Aβ protofilaments with lipid membranes. J. Mol. Biol. 2012, 421, 572-586.
    • (2012) J. Mol. Biol. , vol.421 , pp. 572-586
    • Tofoleanu, F.1    Buchete, N.-V.2
  • 41
    • 35748967575 scopus 로고    scopus 로고
    • Acyl chain order parameter profiles in phospholipid bilayers: Computation from molecular dynamics simulations and comparison with H-2 NMR experiments
    • Vermeer, L.S.; de Groot, B.L.; Reat, V.; Milon, A.; Czaplicki, J. Acyl chain order parameter profiles in phospholipid bilayers: Computation from molecular dynamics simulations and comparison with H-2 NMR experiments. Eur. Biophys. J. Biophy. 2007, 36, 919-931.
    • (2007) Eur. Biophys. J. Biophy. , vol.36 , pp. 919-931
    • Vermeer, L.S.1    de Groot, B.L.2    Reat, V.3    Milon, A.4    Czaplicki, J.5
  • 42
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • Janson, J.; Ashley, R.H.; Harrison, D.; McIntyre, S.; Butler, P.C. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 1999, 48, 491-498.
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 43
    • 67349227494 scopus 로고    scopus 로고
    • Amyloidogenic propensities and conformational properties of ProIAPP and IAPP in the presence of lipid bilayer membranes
    • Jha, S.; Sellin, D.; Seidel, R.; Winter, R. Amyloidogenic propensities and conformational properties of ProIAPP and IAPP in the presence of lipid bilayer membranes. J. Mol. Biol. 2009, 389, 907-920.
    • (2009) J. Mol. Biol. , vol.389 , pp. 907-920
    • Jha, S.1    Sellin, D.2    Seidel, R.3    Winter, R.4
  • 44
    • 62449226332 scopus 로고    scopus 로고
    • A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
    • doi:10.1088/1478-3975/6/1/015005
    • Abedini, A.; Raleigh, D.P. A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Phys. Biol. 2009, 6, doi:10.1088/1478-3975/6/1/015005.
    • (2009) Phys. Biol. , vol.6
    • Abedini, A.1    Raleigh, D.P.2
  • 45
    • 79953236597 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the interactions of kinin peptides with an anionic POPG bilayer
    • Manna, M.; Mukhopadhyay, C. Molecular dynamics simulations of the interactions of kinin peptides with an anionic POPG bilayer. Langmuir 2011, 27, 3713-3722.
    • (2011) Langmuir , vol.27 , pp. 3713-3722
    • Manna, M.1    Mukhopadhyay, C.2
  • 46
    • 79952849765 scopus 로고    scopus 로고
    • Interactions of A beta 25-35 beta-Barrel-like oligomers with anionic lipid bilayer and resulting membrane leakage: An all-atom molecular dynamics study
    • Chang, Z.W.; Luo, Y.; Zhang, Y.; Wei, G.H. Interactions of A beta 25-35 beta-Barrel-like oligomers with anionic lipid bilayer and resulting membrane leakage: An all-atom molecular dynamics study. J. Phys. Chem. B 2011, 115, 1165-1174.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1165-1174
    • Chang, Z.W.1    Luo, Y.2    Zhang, Y.3    Wei, G.H.4
  • 47
    • 29344464343 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a phosphatidylglycerol membrane
    • Elmore, D.E. Molecular dynamics simulation of a phosphatidylglycerol membrane. Febs. Lett. 2006, 580, 144-148.
    • (2006) Febs. Lett. , vol.580 , pp. 144-148
    • Elmore, D.E.1
  • 48
    • 66749128465 scopus 로고    scopus 로고
    • Interaction of an antimicrobial peptide with a model lipid bilayer using molecular dynamics simulation
    • Soliman, W.; Bhattacharjee, S.; Kaur, K. Interaction of an antimicrobial peptide with a model lipid bilayer using molecular dynamics simulation. Langmuir 2009, 25, 6591-6595.
    • (2009) Langmuir , vol.25 , pp. 6591-6595
    • Soliman, W.1    Bhattacharjee, S.2    Kaur, K.3
  • 49
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E.; Hess, B.; van der Spoel, D. GROMACS 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 2001, 7, 306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 50
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger, O.; Edholm, O.; Jahnig, F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 1997, 72, 2002-2013.
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 54
    • 84986440341 scopus 로고
    • Settle-An analytical version of the shake and rattle algorithm for rigid water models
    • Miyamoto, S.; Kollman, P.A. Settle-An analytical version of the shake and rattle algorithm for rigid water models. J. Comput. Chem. 1992, 13, 952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 55
    • 33846823909 scopus 로고
    • Particle mesh ewald-An N. Log(N) method for ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle mesh ewald-An N. Log(N) method for ewald sums in large systems. J. Chem. Phys. 1993, 98, 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 56
    • 0038440700 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid bilayers: Major artifacts due to truncating electrostatic interactions
    • Patra, M.; Karttunen, M.; Hyvonen, M.T.; Falck, E.; Lindqvist, P.; Vattulainen, I. Molecular dynamics simulations of lipid bilayers: Major artifacts due to truncating electrostatic interactions. Biophys. J. 2003, 84, 3636-3645.
    • (2003) Biophys. J. , vol.84 , pp. 3636-3645
    • Patra, M.1    Karttunen, M.2    Hyvonen, M.T.3    Falck, E.4    Lindqvist, P.5    Vattulainen, I.6
  • 57
    • 0027410408 scopus 로고
    • Phase-behavior of mixtures of dppc and popg
    • Wiedmann, T.; Salmon, A.; Wong, V. Phase-behavior of mixtures of dppc and popg. Biochim. Biophys. Acta 1993, 1167, 114-120.
    • (1993) Biochim. Biophys. Acta , vol.1167 , pp. 114-120
    • Wiedmann, T.1    Salmon, A.2    Wong, V.3
  • 58
    • 70349944668 scopus 로고    scopus 로고
    • Binding free energy and counterion release for adsorption of the antimicrobial peptide lactoferricin B on a POPG membrane
    • Tolokh, I.S.; Vivcharuk, V.; Tomberli, B.; Gray, C.G. Binding free energy and counterion release for adsorption of the antimicrobial peptide lactoferricin B on a POPG membrane. Phys. Rev. E 2009, 80, 031911.
    • (2009) Phys. Rev. E , vol.80 , pp. 031911
    • Tolokh, I.S.1    Vivcharuk, V.2    Tomberli, B.3    Gray, C.G.4
  • 60
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.