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Volumn 119, Issue 48, 2015, Pages 14971-14985

A Comprehensive Computational Study of the Interaction between Human Serum Albumin and Fullerenes

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BINS; BODY FLUIDS; CHARGE TRANSFER; FATTY ACIDS; FREE ENERGY; FULLERENES; HYDROGEN BONDS; MOLECULAR ORBITALS; PHOTODYNAMIC THERAPY; QUANTUM THEORY; VAN DER WAALS FORCES;

EID: 84948784170     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b05998     Document Type: Article
Times cited : (21)

References (97)
  • 1
    • 84906242121 scopus 로고    scopus 로고
    • Chemical basis of interactions between engineered nanoparticles and biological systems
    • Mu, Q.; Jiang, G.; Chen, L.; Zhou, H.; Fourches, D.; Tropsha, A.; Yan, B. Chemical basis of interactions between engineered nanoparticles and biological systems Chem. Rev. 2014, 114, 7740-7781 10.1021/cr400295a
    • (2014) Chem. Rev. , vol.114 , pp. 7740-7781
    • Mu, Q.1    Jiang, G.2    Chen, L.3    Zhou, H.4    Fourches, D.5    Tropsha, A.6    Yan, B.7
  • 2
    • 79951898882 scopus 로고    scopus 로고
    • Interactions of nanoparticles with plasma proteins: Implication on clearance and toxicity of drug delivery systems
    • Karmali, P. P.; Simberg, D. Interactions of nanoparticles with plasma proteins: implication on clearance and toxicity of drug delivery systems Expert Opin. Drug Delivery 2011, 8, 343-357 10.1517/17425247.2011.554818
    • (2011) Expert Opin. Drug Delivery , vol.8 , pp. 343-357
    • Karmali, P.P.1    Simberg, D.2
  • 3
    • 38849111818 scopus 로고    scopus 로고
    • Cytotoxicity of nanoparticles
    • Lewinski, N.; Colvin, V.; Drezek, R. Cytotoxicity of nanoparticles Small 2008, 4, 26-49 10.1002/smll.200700595
    • (2008) Small , vol.4 , pp. 26-49
    • Lewinski, N.1    Colvin, V.2    Drezek, R.3
  • 4
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall, T.; Lynch, I.; Lindman, S.; Berggard, T.; Thulin, E.; Nilsson, H.; Dawson, K. A.; Linse, S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 2050-2055 10.1073/pnas.0608582104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggard, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 6
    • 84872034254 scopus 로고    scopus 로고
    • Studying the protein corona on nanoparticles by FCS
    • Nienhaus, G. U.; Maffre, P.; Nienhaus, K. Studying the protein corona on nanoparticles by FCS Methods Enzymol. 2013, 519, 115-137 10.1016/B978-0-12-405539-1.00004-X
    • (2013) Methods Enzymol. , vol.519 , pp. 115-137
    • Nienhaus, G.U.1    Maffre, P.2    Nienhaus, K.3
  • 7
    • 84868124431 scopus 로고    scopus 로고
    • Nanotechnology in therapeutics: A focus on nanoparticles as a drug delivery system
    • Bamrungsap, S.; Zhao, Z. L.; Chen, T.; Wang, L.; Li, C. M.; Fu, T.; Tan, W. H. Nanotechnology in therapeutics: a focus on nanoparticles as a drug delivery system Nanomedicine 2012, 7, 1253-1271 10.2217/nnm.12.87
    • (2012) Nanomedicine , vol.7 , pp. 1253-1271
    • Bamrungsap, S.1    Zhao, Z.L.2    Chen, T.3    Wang, L.4    Li, C.M.5    Fu, T.6    Tan, W.H.7
  • 8
    • 79960199378 scopus 로고    scopus 로고
    • Fullerene sorting proteins
    • Calvaresi, M.; Zerbetto, F. Fullerene sorting proteins Nanoscale 2011, 3, 2873-2881 10.1039/c1nr10082c
    • (2011) Nanoscale , vol.3 , pp. 2873-2881
    • Calvaresi, M.1    Zerbetto, F.2
  • 9
    • 77951740343 scopus 로고    scopus 로고
    • Baiting proteins with C-60
    • Calvaresi, M.; Zerbetto, F. Baiting proteins with C-60 ACS Nano 2010, 4, 2283-2299 10.1021/nn901809b
    • (2010) ACS Nano , vol.4 , pp. 2283-2299
    • Calvaresi, M.1    Zerbetto, F.2
  • 10
    • 77950516142 scopus 로고    scopus 로고
    • Nanoscale enzyme inhibitors: Fullerenes inhibit carbonic anhydrase by occluding the active site entrance
    • Innocenti, A.; Durdagi, S.; Doostdar, N.; Strom, T. A.; Barron, A. R.; Supuran, C. T. Nanoscale enzyme inhibitors: fullerenes inhibit carbonic anhydrase by occluding the active site entrance Bioorg. Med. Chem. 2010, 18, 2822-2828 10.1016/j.bmc.2010.03.026
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2822-2828
    • Innocenti, A.1    Durdagi, S.2    Doostdar, N.3    Strom, T.A.4    Barron, A.R.5    Supuran, C.T.6
  • 11
    • 66249124254 scopus 로고    scopus 로고
    • In silico drug screening approach for the design of magic bullets: A successful example with anti-HIV fullerene derivatized amino acids
    • Durdagi, S.; Supuran, C. T.; Strom, T. A.; Doostdar, N.; Kumar, M. K.; Barron, A. R.; Mavromoustakos, T.; Papadopoulos, M. G. In silico drug screening approach for the design of magic bullets: a successful example with anti-HIV fullerene derivatized amino acids J. Chem. Inf. Model. 2009, 49, 1139-1143 10.1021/ci900047s
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 1139-1143
    • Durdagi, S.1    Supuran, C.T.2    Strom, T.A.3    Doostdar, N.4    Kumar, M.K.5    Barron, A.R.6    Mavromoustakos, T.7    Papadopoulos, M.G.8
  • 12
    • 84887205137 scopus 로고    scopus 로고
    • Potential Medical Applications of Fullerenes: An Overview
    • Wiley-Blackwell: Chichester, U.K
    • Thakral, S.; Thakral, N. K. Potential Medical Applications of Fullerenes: An Overview. In Bio-Nanotechnology; Wiley-Blackwell: Chichester, U.K., 2013; pp 424-441.
    • (2013) Bio-Nanotechnology , pp. 424-441
    • Thakral, S.1    Thakral, N.K.2
  • 13
    • 84890862428 scopus 로고    scopus 로고
    • Fullerene-biomolecule conjugates and their biomedicinal applications
    • Cui, Q.; Yang, X.; Ebrahimi, A.; Li, J. Fullerene-biomolecule conjugates and their biomedicinal applications Int. J. Nanomed. 2013, 9, 77-92 10.2147/IJN.S52829
    • (2013) Int. J. Nanomed. , vol.9 , pp. 77-92
    • Cui, Q.1    Yang, X.2    Ebrahimi, A.3    Li, J.4
  • 14
    • 84875206491 scopus 로고    scopus 로고
    • Functionalizing nanoparticles with biological molecules: Developing chemistries that facilitate nanotechnology
    • Sapsford, K. E.; Algar, W. R.; Berti, L.; Gemmill, K. B.; Casey, B. J.; Oh, E.; Stewart, M. H.; Medintz, I. L. Functionalizing nanoparticles with biological molecules: Developing chemistries that facilitate nanotechnology Chem. Rev. 2013, 113, 1904-2074 10.1021/cr300143v
    • (2013) Chem. Rev. , vol.113 , pp. 1904-2074
    • Sapsford, K.E.1    Algar, W.R.2    Berti, L.3    Gemmill, K.B.4    Casey, B.J.5    Oh, E.6    Stewart, M.H.7    Medintz, I.L.8
  • 16
    • 0344495996 scopus 로고    scopus 로고
    • Synthesis and anti-HIV properties of new water-soluble bis-functionalized[60]fullerene derivatives
    • Bosi, S.; Da Ros, T.; Spalluto, G.; Balzarini, J.; Prato, M. Synthesis and anti-HIV properties of new water-soluble bis-functionalized[60]fullerene derivatives Bioorg. Med. Chem. Lett. 2003, 13, 4437-4440 10.1016/j.bmcl.2003.09.016
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4437-4440
    • Bosi, S.1    Da Ros, T.2    Spalluto, G.3    Balzarini, J.4    Prato, M.5
  • 17
    • 84907042785 scopus 로고    scopus 로고
    • Binding of fullerenes to amyloid beta fibrils: Size matters
    • Huy, P. D. Q.; Li, M. S. Binding of fullerenes to amyloid beta fibrils: size matters Phys. Chem. Chem. Phys. 2014, 16, 20030-20040 10.1039/C4CP02348J
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 20030-20040
    • Huy, P.D.Q.1    Li, M.S.2
  • 18
    • 0033797981 scopus 로고    scopus 로고
    • The role of albumin in critical illness
    • Nicholson, J. P.; Wolmarans, M. R.; Park, G. R. The role of albumin in critical illness Brit J. Anaesth 2000, 85, 599-610 10.1093/bja/85.4.599
    • (2000) Brit J. Anaesth , vol.85 , pp. 599-610
    • Nicholson, J.P.1    Wolmarans, M.R.2    Park, G.R.3
  • 19
    • 84906783332 scopus 로고    scopus 로고
    • A clinical update of using albumin as a drug vehicle - A commentary
    • Kratz, F. A clinical update of using albumin as a drug vehicle-A commentary J. Controlled Release 2014, 190, 331-336 10.1016/j.jconrel.2014.03.013
    • (2014) J. Controlled Release , vol.190 , pp. 331-336
    • Kratz, F.1
  • 20
    • 84895488695 scopus 로고    scopus 로고
    • Interactive association of drugs binding to human serum albumin
    • Yang, F.; Zhang, Y.; Liang, H. Interactive association of drugs binding to human serum albumin Int. J. Mol. Sci. 2014, 15, 3580-3595 10.3390/ijms15033580
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 3580-3595
    • Yang, F.1    Zhang, Y.2    Liang, H.3
  • 22
    • 35348930538 scopus 로고    scopus 로고
    • Protein conformation changes induced by a novel organophosphate-containing water-soluble derivative of a C60 fullerene nanoparticle
    • Zhang, X.-f.; Shu, C.-y.; Xie, L.; Wang, C.-r.; Zhang, Y.-z.; Xiang, J.-f.; Li, L.; Tang, Y.-l. Protein conformation changes induced by a novel organophosphate-containing water-soluble derivative of a C60 fullerene nanoparticle J. Phys. Chem. C 2007, 111, 14327-14333 10.1021/jp073267u
    • (2007) J. Phys. Chem. C , vol.111 , pp. 14327-14333
    • Zhang, X.-F.1    Shu, C.-Y.2    Xie, L.3    Wang, C.-R.4    Zhang, Y.-Z.5    Xiang, J.-F.6    Li, L.7    Tang, Y.-L.8
  • 23
    • 0026664548 scopus 로고
    • Atomic-structure and chemistry of human serum-albumin
    • He, X. M.; Carter, D. C. Atomic-structure and chemistry of human serum-albumin Nature 1992, 358, 209-215 10.1038/358209a0
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 24
    • 21744445084 scopus 로고    scopus 로고
    • A molecular dynamics study of human serum albumin binding sites
    • Artali, R.; Bombieri, G.; Calabi, L.; Del Pra, A. A molecular dynamics study of human serum albumin binding sites Farmaco 2005, 60, 485-495 10.1016/j.farmac.2005.04.010
    • (2005) Farmaco , vol.60 , pp. 485-495
    • Artali, R.1    Bombieri, G.2    Calabi, L.3    Del Pra, A.4
  • 25
    • 50249122634 scopus 로고    scopus 로고
    • Structure, photophysical property, and cytotoxicity of human serum albumin complexed with tris(dicarboxymethylene)[60]fullerene
    • Qu, X.; Komatsu, T.; Sato, T.; Glatter, O.; Horinouchi, H.; Kobayashi, K.; Tsuchida, E. Structure, photophysical property, and cytotoxicity of human serum albumin complexed with tris(dicarboxymethylene)[60]fullerene Bioconjugate Chem. 2008, 19, 1556-1560 10.1021/bc800207j
    • (2008) Bioconjugate Chem. , vol.19 , pp. 1556-1560
    • Qu, X.1    Komatsu, T.2    Sato, T.3    Glatter, O.4    Horinouchi, H.5    Kobayashi, K.6    Tsuchida, E.7
  • 26
    • 84862809856 scopus 로고    scopus 로고
    • Binding of fullerol to human serum albumin: Spectroscopic and electrochemical approach
    • Zhang, M. F.; Xu, Z. Q.; Ge, Y. S.; Jiang, F. L.; Liu, Y. Binding of fullerol to human serum albumin: spectroscopic and electrochemical approach J. Photochem. Photobiol., B 2012, 108, 34-43 10.1016/j.jphotobiol.2011.12.006
    • (2012) J. Photochem. Photobiol., B , vol.108 , pp. 34-43
    • Zhang, M.F.1    Xu, Z.Q.2    Ge, Y.S.3    Jiang, F.L.4    Liu, Y.5
  • 27
    • 84864234552 scopus 로고    scopus 로고
    • Maximizing the relaxivity of Gd-complex by synergistic effect of HSA and carboxylfullerene
    • Zhen, M.; Zheng, J.; Ye, L.; Li, S.; Jin, C.; Li, K.; Qiu, D.; Han, H.; Shu, C.; Yang, Y. et al. Maximizing the relaxivity of Gd-complex by synergistic effect of HSA and carboxylfullerene ACS Appl. Mater. Interfaces 2012, 4, 3724-3729 10.1021/am300817z
    • (2012) ACS Appl. Mater. Interfaces , vol.4 , pp. 3724-3729
    • Zhen, M.1    Zheng, J.2    Ye, L.3    Li, S.4    Jin, C.5    Li, K.6    Qiu, D.7    Han, H.8    Shu, C.9    Yang, Y.10
  • 28
    • 84881312332 scopus 로고    scopus 로고
    • Preparation of soluble stable C60/human serum albumin nanoparticles via cyclodextrin complexation and their reactive oxygen production characteristics
    • Abdulmalik, A.; Hibah, A.; Zainy, B. M.; Makoto, A.; Daisuke, I.; Masaki, O.; Kaneto, U.; Fumitoshi, H. Preparation of soluble stable C60/human serum albumin nanoparticles via cyclodextrin complexation and their reactive oxygen production characteristics Life Sci. 2013, 93, 277-282 10.1016/j.lfs.2013.06.021
    • (2013) Life Sci. , vol.93 , pp. 277-282
    • Abdulmalik, A.1    Hibah, A.2    Zainy, B.M.3    Makoto, A.4    Daisuke, I.5    Masaki, O.6    Kaneto, U.7    Fumitoshi, H.8
  • 29
    • 80052153093 scopus 로고    scopus 로고
    • Interaction of human serum album and C(60) aggregates in solution
    • Song, M.; Liu, S.; Yin, J.; Wang, H. Interaction of human serum album and C(60) aggregates in solution Int. J. Mol. Sci. 2011, 12, 4964-4974 10.3390/ijms12084964
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 4964-4974
    • Song, M.1    Liu, S.2    Yin, J.3    Wang, H.4
  • 30
    • 84879035450 scopus 로고    scopus 로고
    • Human serum albumin interactions with C-60 fullerene studied by spectroscopy, small-angle neutron scattering, and molecular dynamics simulations
    • Li, S.; Zhao, X. C.; Mo, Y. M.; Cummings, P. T.; Heller, W. T. Human serum albumin interactions with C-60 fullerene studied by spectroscopy, small-angle neutron scattering, and molecular dynamics simulations J. Nanopart. Res. 2013, 15, 1769 10.1007/s11051-013-1769-0
    • (2013) J. Nanopart. Res. , vol.15 , pp. 1769
    • Li, S.1    Zhao, X.C.2    Mo, Y.M.3    Cummings, P.T.4    Heller, W.T.5
  • 33
    • 33645462298 scopus 로고    scopus 로고
    • Interaction of C-60-fullerene and carboxyfullerene with proteins: Docking and binding site alignment
    • Benyamini, H.; Shulman-Peleg, A.; Wolfson, H. J.; Belgorodsky, B.; Fadeev, L.; Gozin, M. Interaction of C-60-fullerene and carboxyfullerene with proteins: Docking and binding site alignment Bioconjugate Chem. 2006, 17, 378-386 10.1021/bc050299g
    • (2006) Bioconjugate Chem. , vol.17 , pp. 378-386
    • Benyamini, H.1    Shulman-Peleg, A.2    Wolfson, H.J.3    Belgorodsky, B.4    Fadeev, L.5    Gozin, M.6
  • 34
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow, G.; Birkett, D. J.; Wade, D. N. The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 1975, 11, 824-832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 35
    • 33846614094 scopus 로고    scopus 로고
    • A new analytical material-enhanced laser desorption ionization (MELDI) based approach for the determination of low-mass serum constituents using fullerene derivatives for selective enrichment
    • Vallant, R. M.; Szabo, Z.; Trojer, L.; Najam-ul-Haq, M.; Rainer, M.; Huck, C. W.; Bakry, R.; Bonn, G. K. A new analytical material-enhanced laser desorption ionization (MELDI) based approach for the determination of low-mass serum constituents using fullerene derivatives for selective enrichment J. Proteome Res. 2007, 6, 44-53 10.1021/pr060347m
    • (2007) J. Proteome Res. , vol.6 , pp. 44-53
    • Vallant, R.M.1    Szabo, Z.2    Trojer, L.3    Najam-Ul-Haq, M.4    Rainer, M.5    Huck, C.W.6    Bakry, R.7    Bonn, G.K.8
  • 36
    • 78751703392 scopus 로고    scopus 로고
    • Pulmonary toxicity of carbon nanotubes: A systematic report
    • Kayat, J.; Gajbhiye, V.; Tekade, R. K.; Jain, N. K. Pulmonary toxicity of carbon nanotubes: a systematic report Nanomedicine 2011, 7, 40-49 10.1016/j.nano.2010.06.008
    • (2011) Nanomedicine , vol.7 , pp. 40-49
    • Kayat, J.1    Gajbhiye, V.2    Tekade, R.K.3    Jain, N.K.4
  • 38
    • 0025068367 scopus 로고
    • Mutagenic and genotoxic properties of singlet oxygen
    • Piette, J. Mutagenic and genotoxic properties of singlet oxygen J. Photochem. Photobiol., B 1990, 4, 335-339 10.1016/1011-1344(90)85039-Y
    • (1990) J. Photochem. Photobiol., B , vol.4 , pp. 335-339
    • Piette, J.1
  • 39
    • 70350455504 scopus 로고    scopus 로고
    • Structural and mutagenic approach to create human serum albumin-based oxygen carrier and photosensitizer
    • Komatsu, T.; Nakagawa, A.; Qu, X. Structural and mutagenic approach to create human serum albumin-based oxygen carrier and photosensitizer Drug Metab. Pharmacokinet. 2009, 24, 287-299 10.2133/dmpk.24.287
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 287-299
    • Komatsu, T.1    Nakagawa, A.2    Qu, X.3
  • 40
    • 40649101151 scopus 로고    scopus 로고
    • Rescoring docking hit lists for model cavity sites: Predictions and experimental testing
    • Graves, A. P.; Shivakumar, D. M.; Boyce, S. E.; Jacobson, M. P.; Case, D. A.; Shoichet, B. K. Rescoring docking hit lists for model cavity sites: predictions and experimental testing J. Mol. Biol. 2008, 377, 914-934 10.1016/j.jmb.2008.01.049
    • (2008) J. Mol. Biol. , vol.377 , pp. 914-934
    • Graves, A.P.1    Shivakumar, D.M.2    Boyce, S.E.3    Jacobson, M.P.4    Case, D.A.5    Shoichet, B.K.6
  • 41
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • Wang, J.; Wang, W.; Kollman, P. A.; Case, D. A. Automatic atom type and bond type perception in molecular mechanical calculations J. Mol. Graphics Modell. 2006, 25, 247-260 10.1016/j.jmgm.2005.12.005
    • (2006) J. Mol. Graphics Modell. , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 48
    • 84884192184 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald
    • Salomon-Ferrer, R.; Götz, A. W.; Poole, D.; Le Grand, S.; Walker, R. C. Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald J. Chem. Theory Comput. 2013, 9, 3878-3888 10.1021/ct400314y
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 3878-3888
    • Salomon-Ferrer, R.1    Götz, A.W.2    Poole, D.3    Le Grand, S.4    Walker, R.C.5
  • 49
    • 84860767348 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 1. Generalized Born
    • Götz, A. W.; Williamson, M. J.; Xu, D.; Poole, D.; Le Grand, S.; Walker, R. C. Routine microsecond molecular dynamics simulations with AMBER on GPUs. 1. Generalized Born J. Chem. Theory Comput. 2012, 8, 1542-1555 10.1021/ct200909j
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1542-1555
    • Götz, A.W.1    Williamson, M.J.2    Xu, D.3    Poole, D.4    Le Grand, S.5    Walker, R.C.6
  • 50
    • 84868214675 scopus 로고    scopus 로고
    • SPFP: Speed without compromise¯A mixed precision model for GPU accelerated molecular dynamics simulations
    • Le Grand, S.; Götz, A. W.; Walker, R. C. SPFP: Speed without compromise¯A mixed precision model for GPU accelerated molecular dynamics simulations Comput. Phys. Commun. 2013, 184, 374-380 10.1016/j.cpc.2012.09.022
    • (2013) Comput. Phys. Commun. , vol.184 , pp. 374-380
    • Le Grand, S.1    Götz, A.W.2    Walker, R.C.3
  • 51
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes J. Comput. Phys. 1977, 23, 327-341 10.1016/0021-9991(77)90098-5
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 53
    • 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 10.1021/ct700301q
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 54
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S.; Berendsen, H. J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme Proteins: Struct., Funct., Genet. 1998, 30, 144-154 10.1002/(SICI)1097-0134(19980201)30:2<144::AID-PROT4>3.0.CO;2-N
    • (1998) Proteins: Struct., Funct., Genet. , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 55
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models
    • Kollman, P. A.; Massova, I.; Reyes, C.; Kuhn, B.; Huo, S.; Chong, L.; Lee, M.; Lee, T.; Duan, Y.; Wang, W. et al. Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models Acc. Chem. Res. 2000, 33, 889-897 10.1021/ar000033j
    • (2000) Acc. Chem. Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6    Lee, M.7    Lee, T.8    Duan, Y.9    Wang, W.10
  • 56
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke, H.; Kiel, C.; Case, D. A. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes J. Mol. Biol. 2003, 330, 891-913 10.1016/S0022-2836(03)00610-7
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 57
    • 84883231678 scopus 로고    scopus 로고
    • A contribution to the drug resistance mechanism of darunavir, amprenavir, indinavir, and saquinavir complexes with HIV-1 protease due to flap mutation I50V: A systematic MM-PBSA and thermodynamic integration study
    • Leonis, G.; Steinbrecher, T.; Papadopoulos, M. G. A contribution to the drug resistance mechanism of darunavir, amprenavir, indinavir, and saquinavir complexes with HIV-1 protease due to flap mutation I50V: a systematic MM-PBSA and thermodynamic integration study J. Chem. Inf. Model. 2013, 53, 2141-2153 10.1021/ci4002102
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2141-2153
    • Leonis, G.1    Steinbrecher, T.2    Papadopoulos, M.G.3
  • 58
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • Hou, T.; Wang, J.; Li, Y.; Wang, W. Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations J. Chem. Inf. Model. 2011, 51, 69-82 10.1021/ci100275a
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 69-82
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 59
    • 84904966105 scopus 로고    scopus 로고
    • Evaluation and application of MD-PB/SA in structure-based hierarchical virtual screening
    • Cao, R.; Huang, N.; Wang, Y. Evaluation and application of MD-PB/SA in structure-based hierarchical virtual screening J. Chem. Inf. Model. 2014, 54, 1987-1996 10.1021/ci5003203
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 1987-1996
    • Cao, R.1    Huang, N.2    Wang, Y.3
  • 61
    • 84876531626 scopus 로고    scopus 로고
    • Identification of sumoylation activating enzyme 1 inhibitors by structure-based virtual screening
    • Kumar, A.; Ito, A.; Hirohama, M.; Yoshida, M.; Zhang, K. Y. Identification of sumoylation activating enzyme 1 inhibitors by structure-based virtual screening J. Chem. Inf. Model. 2013, 53, 809-820 10.1021/ci300618e
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 809-820
    • Kumar, A.1    Ito, A.2    Hirohama, M.3    Yoshida, M.4    Zhang, K.Y.5
  • 62
    • 84859856495 scopus 로고    scopus 로고
    • Discovery of a novel acetylcholinesterase inhibitor by structure-based virtual screening techniques
    • Chen, Y.; Fang, L.; Peng, S.; Liao, H.; Lehmann, J.; Zhang, Y. Discovery of a novel acetylcholinesterase inhibitor by structure-based virtual screening techniques Bioorg. Med. Chem. Lett. 2012, 22, 3181-3187 10.1016/j.bmcl.2012.03.046
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 3181-3187
    • Chen, Y.1    Fang, L.2    Peng, S.3    Liao, H.4    Lehmann, J.5    Zhang, Y.6
  • 64
    • 35348864558 scopus 로고    scopus 로고
    • Validation of an automated procedure for the prediction of relative free energies of binding on a set of aldose reductase inhibitors
    • Ferrari, A. M.; Degliesposti, G.; Sgobba, M.; Rastelli, G. Validation of an automated procedure for the prediction of relative free energies of binding on a set of aldose reductase inhibitors Bioorg. Med. Chem. 2007, 15, 7865-7877 10.1016/j.bmc.2007.08.019
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 7865-7877
    • Ferrari, A.M.1    Degliesposti, G.2    Sgobba, M.3    Rastelli, G.4
  • 66
    • 84987133653 scopus 로고
    • New energy decomposition scheme for molecular-interactions within Hartree-Fock approximation
    • Kitaura, K.; Morokuma, K. New energy decomposition scheme for molecular-interactions within Hartree-Fock approximation Int. J. Quantum Chem. 1976, 10, 325-340 10.1002/qua.560100211
    • (1976) Int. J. Quantum Chem. , vol.10 , pp. 325-340
    • Kitaura, K.1    Morokuma, K.2
  • 67
    • 36849107181 scopus 로고
    • Molecular Orbital Studies of Hydrogen Bonds. III. C⋯-O···H-O hydrogen bond in H2CO···H2O and H2CO···2H2O
    • Morokuma, K. Molecular Orbital Studies of Hydrogen Bonds. III. C⋯-O···H-O hydrogen bond in H2CO···H2O and H2CO···2H2O J. Chem. Phys. 1971, 55, 1236-1244 10.1063/1.1676210
    • (1971) J. Chem. Phys. , vol.55 , pp. 1236-1244
    • Morokuma, K.1
  • 69
    • 33846595219 scopus 로고    scopus 로고
    • Pair interaction energy decomposition analysis
    • Fedorov, D. G.; Kitaura, K. Pair interaction energy decomposition analysis J. Comput. Chem. 2007, 28, 222-237 10.1002/jcc.20496
    • (2007) J. Comput. Chem. , vol.28 , pp. 222-237
    • Fedorov, D.G.1    Kitaura, K.2
  • 71
    • 67650463388 scopus 로고    scopus 로고
    • Energy decomposition analysis of covalent bonds and intermolecular interactions
    • Su, P.; Li, H. Energy decomposition analysis of covalent bonds and intermolecular interactions J. Chem. Phys. 2009, 131, 014102 10.1063/1.3159673
    • (2009) J. Chem. Phys. , vol.131 , pp. 014102
    • Su, P.1    Li, H.2
  • 72
    • 84890021933 scopus 로고
    • Calculation of small molecular interactions by differences of separate total energies - Some procedures with reduced errors
    • Boys, S. F.; Bernardi, F. Calculation of small molecular interactions by differences of separate total energies-Some procedures with reduced errors Mol. Phys. 1970, 19, 553-566 10.1080/00268977000101561
    • (1970) Mol. Phys. , vol.19 , pp. 553-566
    • Boys, S.F.1    Bernardi, F.2
  • 74
    • 0032549195 scopus 로고    scopus 로고
    • Hydrogen bond strengths revealed by topological analyses of experimentally observed electron densities
    • Espinosa, E.; Molins, E.; Lecomte, C. Hydrogen bond strengths revealed by topological analyses of experimentally observed electron densities Chem. Phys. Lett. 1998, 285, 170-173 10.1016/S0009-2614(98)00036-0
    • (1998) Chem. Phys. Lett. , vol.285 , pp. 170-173
    • Espinosa, E.1    Molins, E.2    Lecomte, C.3
  • 76
    • 0037202606 scopus 로고    scopus 로고
    • Update of the AIM2000-program for atoms in molecules
    • Biegler-Konig, F.; Schonbohm, J. Update of the AIM2000-program for atoms in molecules J. Comput. Chem. 2002, 23, 1489-1494 10.1002/jcc.10085
    • (2002) J. Comput. Chem. , vol.23 , pp. 1489-1494
    • Biegler-Konig, F.1    Schonbohm, J.2
  • 77
    • 84906551636 scopus 로고    scopus 로고
    • Elucidation of conformational states, dynamics, and mechanism of binding in human kappa-opioid receptor complexes
    • Leonis, G.; Avramopoulos, A.; Salmas, R. E.; Durdagi, S.; Yurtsever, M.; Papadopoulos, M. G. Elucidation of conformational states, dynamics, and mechanism of binding in human kappa-opioid receptor complexes J. Chem. Inf. Model. 2014, 54, 2294-2308 10.1021/ci5002873
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 2294-2308
    • Leonis, G.1    Avramopoulos, A.2    Salmas, R.E.3    Durdagi, S.4    Yurtsever, M.5    Papadopoulos, M.G.6
  • 79
    • 77953607291 scopus 로고    scopus 로고
    • Binding of anti-Parkinson¯s disease drugs to human serum albumin is allosterically modulated
    • Fanali, G.; Rampoldi, V.; Masi, A. d.; Bolli, A.; Lopiano, L.; Ascenzi, P.; Fasano, M. Binding of anti-Parkinson¯s disease drugs to human serum albumin is allosterically modulated IUBMB Life 2010, 62, 371-376 10.1002/iub.317
    • (2010) IUBMB Life , vol.62 , pp. 371-376
    • Fanali, G.1    Rampoldi, V.2    Masi, A.D.3    Bolli, A.4    Lopiano, L.5    Ascenzi, P.6    Fasano, M.7
  • 80
    • 84919808019 scopus 로고    scopus 로고
    • Analysis of the structure and dynamics of human serum albumin
    • Guizado, T. R. Analysis of the structure and dynamics of human serum albumin J. Mol. Model. 2014, 20, 2450 10.1007/s00894-014-2450-y
    • (2014) J. Mol. Model. , vol.20 , pp. 2450
    • Guizado, T.R.1
  • 81
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S.; Mandelkow, H.; Brick, P.; Franks, N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites Nat. Struct. Biol. 1998, 5, 827-835 10.1038/1869
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 83
    • 0035861982 scopus 로고    scopus 로고
    • Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids
    • Petitpas, I.; Grune, T.; Bhattacharya, A. A.; Curry, S. Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids J. Mol. Biol. 2001, 314, 955-960 10.1006/jmbi.2000.5208
    • (2001) J. Mol. Biol. , vol.314 , pp. 955-960
    • Petitpas, I.1    Grune, T.2    Bhattacharya, A.A.3    Curry, S.4
  • 84
    • 0037404491 scopus 로고    scopus 로고
    • In silico prediction of drug-binding strengths to human serum albumin
    • Colmenarejo, G. In silico prediction of drug-binding strengths to human serum albumin Med. Res. Rev. 2003, 23, 275-301 10.1002/med.10039
    • (2003) Med. Res. Rev. , vol.23 , pp. 275-301
    • Colmenarejo, G.1
  • 85
    • 33746218831 scopus 로고    scopus 로고
    • Molecular dynamics study of conformational changes in human serum albumin by binding of fatty acids
    • Fujiwara, S.-i.; Amisaki, T. Molecular dynamics study of conformational changes in human serum albumin by binding of fatty acids Proteins: Struct., Funct., Genet. 2006, 64, 730-739 10.1002/prot.21053
    • (2006) Proteins: Struct., Funct., Genet. , vol.64 , pp. 730-739
    • Fujiwara, S.-I.1    Amisaki, T.2
  • 86
    • 84896738757 scopus 로고    scopus 로고
    • A principal component analysis of the dynamics of subdomains and binding sites in human serum albumin
    • Paris, G.; Ramseyer, C.; Enescu, M. A principal component analysis of the dynamics of subdomains and binding sites in human serum albumin Biopolymers 2014, 101, 561-572 10.1002/bip.22418
    • (2014) Biopolymers , vol.101 , pp. 561-572
    • Paris, G.1    Ramseyer, C.2    Enescu, M.3
  • 87
    • 84862833913 scopus 로고    scopus 로고
    • Computational studies of darunavir into HIV-1 protease and DMPC bilayer: Necessary conditions for effective binding and the role of the flaps
    • Leonis, G.; Czyznikowska, Z.; Megariotis, G.; Reis, H.; Papadopoulos, M. G. Computational studies of darunavir into HIV-1 protease and DMPC bilayer: necessary conditions for effective binding and the role of the flaps J. Chem. Inf. Model. 2012, 52, 1542-58 10.1021/ci300014z
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 1542-1558
    • Leonis, G.1    Czyznikowska, Z.2    Megariotis, G.3    Reis, H.4    Papadopoulos, M.G.5
  • 88
    • 84855196452 scopus 로고    scopus 로고
    • Binding of novel fullerene inhibitors to HIV-1 protease: Insight through molecular dynamics and molecular mechanics Poisson-Boltzmann surface area calculations
    • Tzoupis, H.; Leonis, G.; Durdagi, S.; Mouchlis, V.; Mavromoustakos, T.; Papadopoulos, M. G. Binding of novel fullerene inhibitors to HIV-1 protease: insight through molecular dynamics and molecular mechanics Poisson-Boltzmann surface area calculations J. Comput.-Aided Mol. Des. 2011, 25, 959-976 10.1007/s10822-011-9475-4
    • (2011) J. Comput.-Aided Mol. Des. , vol.25 , pp. 959-976
    • Tzoupis, H.1    Leonis, G.2    Durdagi, S.3    Mouchlis, V.4    Mavromoustakos, T.5    Papadopoulos, M.G.6
  • 89
    • 84863107521 scopus 로고    scopus 로고
    • Dual inhibitors for aspartic proteases HIV-1 PR and renin: Advancements in AIDS-hypertension-diabetes linkage via molecular dynamics, inhibition assays, and binding free energy calculations
    • Tzoupis, H.; Leonis, G.; Megariotis, G.; Supuran, C. T.; Mavromoustakos, T.; Papadopoulos, M. G. Dual inhibitors for aspartic proteases HIV-1 PR and renin: advancements in AIDS-hypertension-diabetes linkage via molecular dynamics, inhibition assays, and binding free energy calculations J. Med. Chem. 2012, 55, 5784-5796 10.1021/jm300180r
    • (2012) J. Med. Chem. , vol.55 , pp. 5784-5796
    • Tzoupis, H.1    Leonis, G.2    Megariotis, G.3    Supuran, C.T.4    Mavromoustakos, T.5    Papadopoulos, M.G.6
  • 91
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin: Anatomy of drug site I
    • Petitpas, I.; Bhattacharya, A. A.; Twine, S.; East, M.; Curry, S. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I J. Biol. Chem. 2001, 276, 22804-22809 10.1074/jbc.M100575200
    • (2001) J. Biol. Chem. , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 93
    • 77951977240 scopus 로고    scopus 로고
    • Allostery in a monomeric protein: The case of human serum albumin
    • Ascenzi, P.; Fasano, M. Allostery in a monomeric protein: The case of human serum albumin Biophys. Chem. 2010, 148, 16-22 10.1016/j.bpc.2010.03.001
    • (2010) Biophys. Chem. , vol.148 , pp. 16-22
    • Ascenzi, P.1    Fasano, M.2
  • 94
    • 77953607291 scopus 로고    scopus 로고
    • Binding of anti-Parkinson¯s disease drugs to human serum albumin is allosterically modulated
    • Fanali, G.; Rampoldi, V.; di Masi, A.; Bolli, A.; Lopiano, L.; Ascenzi, P.; Fasano, M. Binding of anti-Parkinson¯s disease drugs to human serum albumin is allosterically modulated IUBMB Life 2010, 62, 371-376 10.1002/iub.317
    • (2010) IUBMB Life , vol.62 , pp. 371-376
    • Fanali, G.1    Rampoldi, V.2    Di Masi, A.3    Bolli, A.4    Lopiano, L.5    Ascenzi, P.6    Fasano, M.7
  • 95
    • 0002647038 scopus 로고
    • 3 - Ligand Binding by Albumin
    • Academic Press: San Diego
    • Peters, T., Jr. 3-Ligand Binding by Albumin. In All about Albumin; Peters, T., Ed.; Academic Press: San Diego, 1995; pp 76-132.
    • (1995) All about Albumin , pp. 76-132
    • Peters, T.1
  • 96
    • 0021030158 scopus 로고
    • Structural requirements for drug binding to site II on human serum albumin
    • Wanwimolruk, S.; Birkett, D. J.; Brooks, P. M. Structural requirements for drug binding to site II on human serum albumin Mol. Pharmacol. 1983, 24, 458-463
    • (1983) Mol. Pharmacol. , vol.24 , pp. 458-463
    • Wanwimolruk, S.1    Birkett, D.J.2    Brooks, P.M.3
  • 97
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • Kragh-Hansen, U. Molecular aspects of ligand binding to serum albumin Pharmacol. Rev. 1981, 33, 17-53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1


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