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Volumn 118, Issue 1, 2014, Pages 189-194

Difference of carboxybetaine and oligo(ethylene glycol) moieties in altering hydrophobic interactions: A molecular simulation study

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; MOLECULES; POLYETHYLENE GLYCOLS; POLYOLS; UREA;

EID: 84892562048     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp410224w     Document Type: Article
Times cited : (36)

References (41)
  • 1
    • 0035892450 scopus 로고    scopus 로고
    • Bacterial adhesion to surface hydrophilic and hydrophobic contact lenses
    • Bruinsma, G. M.; van der Mei, H. C.; Busscher, H. J. Bacterial adhesion to surface hydrophilic and hydrophobic contact lenses Biomaterials 2001, 22, 3217-3224
    • (2001) Biomaterials , vol.22 , pp. 3217-3224
    • Bruinsma, G.M.1    Van Der Mei, H.C.2    Busscher, H.J.3
  • 3
    • 78650601505 scopus 로고    scopus 로고
    • Zwitterionic poly(carboxybetaine) hydrogels for glucose biosensors in complex media
    • Yang, W.; Xue, H.; Carr, L. R.; Wang, J.; Jiang, S. Zwitterionic poly(carboxybetaine) hydrogels for glucose biosensors in complex media Biosens. Bioelectron. 2011, 26, 2454-2459
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 2454-2459
    • Yang, W.1    Xue, H.2    Carr, L.R.3    Wang, J.4    Jiang, S.5
  • 4
    • 78650089175 scopus 로고    scopus 로고
    • Difference in Hydration between Carboxybetaine and Sulfobetaine
    • Shao, Q.; He, Y.; White, A. D.; Jiang, S. Difference in Hydration between Carboxybetaine and Sulfobetaine J. Phys. Chem. B 2010, 114, 16625-16631
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16625-16631
    • Shao, Q.1    He, Y.2    White, A.D.3    Jiang, S.4
  • 5
    • 84871272254 scopus 로고    scopus 로고
    • Surface chemistry to minimize fouling from blood-based fluids
    • Blaszykowski, C.; Sheikh, S.; Thompson, M. Surface chemistry to minimize fouling from blood-based fluids Chem. Soc. Rev. 2012, 41, 5599-5612
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 5599-5612
    • Blaszykowski, C.1    Sheikh, S.2    Thompson, M.3
  • 6
    • 5444268689 scopus 로고    scopus 로고
    • Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers
    • Zheng, J.; Li, L. Y.; Chen, S. F.; Jiang, S. Y. Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers Langmuir 2004, 20, 8931-8938
    • (2004) Langmuir , vol.20 , pp. 8931-8938
    • Zheng, J.1    Li, L.Y.2    Chen, S.F.3    Jiang, S.Y.4
  • 7
    • 78650089175 scopus 로고    scopus 로고
    • Difference in Hydration between Carboxybetaine and Sulfobetaine
    • Shao, Q.; He, Y.; White, A. D.; Jiang, S. Y. Difference in Hydration between Carboxybetaine and Sulfobetaine J. Phys. Chem. B 2010, 114, 16625-16631
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16625-16631
    • Shao, Q.1    He, Y.2    White, A.D.3    Jiang, S.Y.4
  • 8
    • 79952082628 scopus 로고    scopus 로고
    • Local and Bulk Hydration of Zwitterionic Glycine and its Analogues through Molecular Simulations
    • White, A.; Jiang, S. Y. Local and Bulk Hydration of Zwitterionic Glycine and its Analogues through Molecular Simulations J. Phys. Chem. B 2011, 115, 660-667
    • (2011) J. Phys. Chem. B , vol.115 , pp. 660-667
    • White, A.1    Jiang, S.Y.2
  • 9
    • 83655197598 scopus 로고    scopus 로고
    • Poly(zwitterionic)protein conjugates offer increased stability without sacrificing binding affinity or bioactivity
    • Keefe, A. J.; Jiang, S. Y. Poly(zwitterionic)protein conjugates offer increased stability without sacrificing binding affinity or bioactivity Nat. Chem. 2012, 4, 59-63
    • (2012) Nat. Chem. , vol.4 , pp. 59-63
    • Keefe, A.J.1    Jiang, S.Y.2
  • 10
    • 84866893168 scopus 로고    scopus 로고
    • Different effects of zwitterion and ethylene glycol on proteins
    • Shao, Q.; He, Y.; White, A. D.; Jiang, S. Y. Different effects of zwitterion and ethylene glycol on proteins J. Chem. Phys. 2012, 136, 225101
    • (2012) J. Chem. Phys. , vol.136 , pp. 225101
    • Shao, Q.1    He, Y.2    White, A.D.3    Jiang, S.Y.4
  • 12
    • 67449084506 scopus 로고    scopus 로고
    • Dewetting and Hydrophobic Interaction in Physical and Biological Systems
    • Berne, B. J.; Weeks, J. D.; Zhou, R. H. Dewetting and Hydrophobic Interaction in Physical and Biological Systems Annu. Rev. Phys. Chem. 2009, 60, 85-103
    • (2009) Annu. Rev. Phys. Chem. , vol.60 , pp. 85-103
    • Berne, B.J.1    Weeks, J.D.2    Zhou, R.H.3
  • 13
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. Interfaces and the driving force of hydrophobic assembly Nature 2005, 437, 640-647
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 14
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson, H. J.; Wright, P. E.; Scheraga, H. A. The role of hydrophobic interactions in initiation and propagation of protein folding Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 13057-13061
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3
  • 17
    • 4143121554 scopus 로고    scopus 로고
    • Free energy of ligand binding to protein: Evaluation of the contribution of water molecules by computational methods
    • Cozzini, P.; Fornabaio, M.; Marabotti, A.; Abraham, D. J.; Kellogg, G. E.; Mozzarelli, A. Free energy of ligand binding to protein: Evaluation of the contribution of water molecules by computational methods Curr. Med. Chem. 2004, 11, 3093-3118
    • (2004) Curr. Med. Chem. , vol.11 , pp. 3093-3118
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogg, G.E.5    Mozzarelli, A.6
  • 18
    • 0037187108 scopus 로고    scopus 로고
    • The hydrophobic effect and the influence of solute-solvent attractions
    • Huang, D. M.; Chandler, D. The hydrophobic effect and the influence of solute-solvent attractions J. Phys. Chem. B 2002, 106, 2047-2053
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2047-2053
    • Huang, D.M.1    Chandler, D.2
  • 19
    • 34247500338 scopus 로고    scopus 로고
    • Effect of ions on the hydrophobic interaction between two plates
    • Zangi, R.; Hagen, M.; Berne, B. J. Effect of ions on the hydrophobic interaction between two plates J. Am. Chem. Soc. 2007, 129, 4678-4686
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4678-4686
    • Zangi, R.1    Hagen, M.2    Berne, B.J.3
  • 20
    • 23244459863 scopus 로고    scopus 로고
    • Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: Origin of osmolyte compatibility
    • Athawale, M. V.; Dordick, J. S.; Garde, S. Osmolyte trimethylamine-N- oxide does not affect the strength of hydrophobic interactions: Origin of osmolyte compatibility Biophys. J. 2005, 89, 858-866
    • (2005) Biophys. J. , vol.89 , pp. 858-866
    • Athawale, M.V.1    Dordick, J.S.2    Garde, S.3
  • 21
    • 63149153986 scopus 로고    scopus 로고
    • Urea's Action on Hydrophobic Interactions
    • Zangi, R.; Zhou, R. H.; Berne, B. J. Urea's Action on Hydrophobic Interactions J. Am. Chem. Soc. 2009, 131, 1535-1541
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.H.2    Berne, B.J.3
  • 23
    • 0038717923 scopus 로고    scopus 로고
    • Binary phases of aliphatic N-oxides and water: Force field development and molecular dynamics simulation
    • Kast, K. M.; Brickmann, J.; Kast, S. M.; Berry, R. S. Binary phases of aliphatic N-oxides and water: Force field development and molecular dynamics simulation J. Phys. Chem. A 2003, 107, 5342-5351
    • (2003) J. Phys. Chem. A , vol.107 , pp. 5342-5351
    • Kast, K.M.1    Brickmann, J.2    Kast, S.M.3    Berry, R.S.4
  • 24
    • 84962467448 scopus 로고    scopus 로고
    • Effect of Carbon Spacer Length on Zwitterionic Carboxybetaines
    • Shao, Q.; Jiang, S. Y. Effect of Carbon Spacer Length on Zwitterionic Carboxybetaines J. Phys. Chem. B 2013, 117, 1357-1366
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1357-1366
    • Shao, Q.1    Jiang, S.Y.2
  • 25
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L.; Maxwell, D. S.; TiradoRives, J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids J. Am. Chem. Soc. 1996, 118, 11225-11236
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 28
    • 34547809547 scopus 로고
    • Unified formulation of the constant temperature molecular-dynamics methods
    • Nose, S. A Unified formulation of the constant temperature molecular-dynamics methods J. Chem. Phys. 1984, 81, 511-519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nose, S.A.1
  • 29
    • 0001538909 scopus 로고
    • Canonical dynamics - Equilibrium phase-space distributions
    • Hoover, W. G. Canonical dynamics-equilibrium phase-space distributions Phys. Rev. A 1985, 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 30
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess, B. P-LINCS: A parallel linear constraint solver for molecular simulation J. Chem. Theory Comput. 2008, 4, 116-122
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 31
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 32
    • 38349091489 scopus 로고    scopus 로고
    • Well-tempered metadynamics: A smoothly converging and tunable free-energy method
    • Barducci, A.; Bussi, G.; Parrinello, M. Well-tempered metadynamics: A smoothly converging and tunable free-energy method Phys. Rev. Lett. 2008, 100, 020603(1-4)
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 0206031-0206034
    • Barducci, A.1    Bussi, G.2    Parrinello, M.3
  • 36
    • 33646163934 scopus 로고    scopus 로고
    • Does urea denature hydrophobic interactions?
    • Lee, M. E.; van der Vegt, N. F. A. Does urea denature hydrophobic interactions? J. Am. Chem. Soc. 2006, 128, 4948-4949
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4948-4949
    • Lee, M.E.1    Van Der Vegt, N.F.A.2
  • 37
    • 79953759344 scopus 로고    scopus 로고
    • Role of Solvation Effects in Protein Denaturation: From Thermodynamics to Single Molecules and Back
    • England, J. L.; Haran, G. Role of Solvation Effects in Protein Denaturation: From Thermodynamics to Single Molecules and Back Annu. Rev. Phys. Chem. 2011, 62, 257-277
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 257-277
    • England, J.L.1    Haran, G.2
  • 38
    • 0030844580 scopus 로고    scopus 로고
    • The different faces of poly(ethylene glycol)
    • Israelachvili, J. The different faces of poly(ethylene glycol) Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 8378-8379
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8378-8379
    • Israelachvili, J.1
  • 39
    • 67749106309 scopus 로고    scopus 로고
    • Theory for Protein Folding Cooperativity: Helix Bundles
    • Ghosh, K.; Dill, K. A. Theory for Protein Folding Cooperativity: Helix Bundles J. Am. Chem. Soc. 2009, 131, 2306-2312
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2306-2312
    • Ghosh, K.1    Dill, K.A.2
  • 40
    • 38449098568 scopus 로고    scopus 로고
    • Effect of polyethylene glycols on the function and structure of thiol proteases
    • Fatima, S.; Khan, R. H. Effect of polyethylene glycols on the function and structure of thiol proteases J. Biochem. 2007, 142, 65-72
    • (2007) J. Biochem. , vol.142 , pp. 65-72
    • Fatima, S.1    Khan, R.H.2
  • 41
    • 27544496736 scopus 로고    scopus 로고
    • Protein PEGylation decreases observed target association rates via a dual blocking mechanism
    • Kubetzko, S.; Sarkar, C. A.; Pluckthun, A. Protein PEGylation decreases observed target association rates via a dual blocking mechanism Mol. Pharmacol. 2005, 68, 1439-1454
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1439-1454
    • Kubetzko, S.1    Sarkar, C.A.2    Pluckthun, A.3


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