메뉴 건너뛰기




Volumn 8, Issue 4, 2015, Pages 1293-1308

Probing enzyme-nanoparticle interactions using combinatorial gold nanoparticle libraries

Author keywords

acetylcholinesterase; enzyme inhibition; gold nanoparticles; modeling; neural network; protein binding; quantitative structure property relationship (QSPR); surface modification

Indexed keywords


EID: 84939990170     PISSN: 19980124     EISSN: 19980000     Source Type: Journal    
DOI: 10.1007/s12274-014-0618-5     Document Type: Article
Times cited : (26)

References (41)
  • 2
    • 67650457089 scopus 로고    scopus 로고
    • Too small to overlook
    • Maynard, A.; Rejeski, D. Too small to overlook. Nature2009, 460, 174–174.
    • (2009) Nature , vol.460 , pp. 174
    • Maynard, A.1    Rejeski, D.2
  • 3
    • 31944451232 scopus 로고    scopus 로고
    • Toxic potential of materials at the nanolevel
    • Nel, A.; Xia, T.; Madler, L.; Li, N. Toxic potential of materials at the nanolevel. Science2006, 311, 622–627.
    • (2006) Science , vol.311 , pp. 622-627
    • Nel, A.1    Xia, T.2    Madler, L.3    Li, N.4
  • 4
    • 72949094881 scopus 로고    scopus 로고
    • In vivo labelling of hippocampal beta-amyloid in triple-transgenic mice with a fluorescent acetylcholinesterase inhibitor released from nanoparticles
    • Hartig, W.; Kacza, J.; Paulke, B. R.; Grosche, J.; Bauer, U.; Hoffmann, A.; Elsinghorst, P. W.; Gutschow, M. In vivo labelling of hippocampal beta-amyloid in triple-transgenic mice with a fluorescent acetylcholinesterase inhibitor released from nanoparticles. Euro. J. Neurosci.2010, 31, 99–109.
    • (2010) Euro. J. Neurosci. , vol.31 , pp. 99-109
    • Hartig, W.1    Kacza, J.2    Paulke, B.R.3    Grosche, J.4    Bauer, U.5    Hoffmann, A.6    Elsinghorst, P.W.7    Gutschow, M.8
  • 5
    • 84885757504 scopus 로고    scopus 로고
    • Applying quantitative structure-activity relationship approaches to nanotoxicology: Current status and future potential
    • Winkler, D. A.; Mombelli, E.; Pietroiusti, A.; Tran, L.; Worth, A.; Fadeel, B.; McCall, M. J. Applying quantitative structure-activity relationship approaches to nanotoxicology: Current status and future potential. Toxicology2013, 313, 15–23.
    • (2013) Toxicology , vol.313 , pp. 15-23
    • Winkler, D.A.1    Mombelli, E.2    Pietroiusti, A.3    Tran, L.4    Worth, A.5    Fadeel, B.6    McCall, M.J.7
  • 6
    • 66749166478 scopus 로고    scopus 로고
    • Functionalized carbon nanotubes specifically bind to α-chymotrypsin’s catalytic site and regulate its enzymatic function
    • Zhang, B.; Xing, Y. H.; Li, Z. W.; Zhou, H. Y.; Mu, Q. X.; Yan, B. Functionalized carbon nanotubes specifically bind to α-chymotrypsin’s catalytic site and regulate its enzymatic function. Nano Lett.2009, 9, 2280–2284.
    • (2009) Nano Lett. , vol.9 , pp. 2280-2284
    • Zhang, B.1    Xing, Y.H.2    Li, Z.W.3    Zhou, H.Y.4    Mu, Q.X.5    Yan, B.6
  • 7
    • 43149095577 scopus 로고    scopus 로고
    • A nano-combinatorial library strategy for the discovery of nanotubes with reduced protein-binding, cytotoxicity, and immune response
    • Zhou, H. Y.; Mu, Q. X.; Gao, N. N.; Liu, A. F.; Xing, Y. H.; Gao, S. L.; Zhang, Q.; Qu, G. B.; Chen, Y. Y.; Liu, G. et al. A nano-combinatorial library strategy for the discovery of nanotubes with reduced protein-binding, cytotoxicity, and immune response. Nano Lett.2008, 8, 859–865.
    • (2008) Nano Lett. , vol.8 , pp. 859-865
    • Zhou, H.Y.1    Mu, Q.X.2    Gao, N.N.3    Liu, A.F.4    Xing, Y.H.5    Gao, S.L.6    Zhang, Q.7    Qu, G.B.8    Chen, Y.Y.9    Liu, G.10
  • 8
    • 27944496941 scopus 로고    scopus 로고
    • Cell-specific targeting of nanoparticles by multivalent attachment of small molecules
    • Weissleder, R.; Kelly, K.; Sun, E. Y.; Shtatland, T.; Josephson, L. Cell-specific targeting of nanoparticles by multivalent attachment of small molecules. Nat. Biotechnol.2005, 23, 1418–1423.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1418-1423
    • Weissleder, R.1    Kelly, K.2    Sun, E.Y.3    Shtatland, T.4    Josephson, L.5
  • 9
    • 25144471199 scopus 로고    scopus 로고
    • Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles
    • You, C. C.; De, M.; Han, G.; Rotello, V. M. Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles. J. Am. Chem. Soc.2005, 127, 12873–12881.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12873-12881
    • You, C.C.1    De, M.2    Han, G.3    Rotello, V.M.4
  • 10
    • 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. USA2007, 104, 2050–2055.
    • (2007) Proc. Natl. Acad. Sci. USA , 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
  • 11
    • 84864241697 scopus 로고    scopus 로고
    • Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells
    • Lesniak, A.; Fenaroli, F.; Monopoli, M. R.; Aberg, C.; Dawson, K. A.; Salvati, A. Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells. ACS Nano2012, 6, 5845–5857.
    • (2012) ACS Nano , vol.6 , pp. 5845-5857
    • Lesniak, A.1    Fenaroli, F.2    Monopoli, M.R.3    Aberg, C.4    Dawson, K.A.5    Salvati, A.6
  • 12
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist, M.; Stigler, J.; Elia, G.; Lynch, I.; Cedervall, T.; Dawson, K. A. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci. USA2008, 105, 14265–14270.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 14
    • 84888880735 scopus 로고    scopus 로고
    • Particle carriers for combating multidrug-resistant cancer
    • Yan, Y.; Bjoernmalm, M.; Caruso, F. Particle carriers for combating multidrug-resistant cancer. ACS Nano2013, 7, 9512–9517.
    • (2013) ACS Nano , vol.7 , pp. 9512-9517
    • Yan, Y.1    Bjoernmalm, M.2    Caruso, F.3
  • 16
    • 3042673717 scopus 로고    scopus 로고
    • Expression and localization of acetylcholine-esterase at the neuromuscular junction
    • Rotundo, R. L. Expression and localization of acetylcholine-esterase at the neuromuscular junction. J. Neurocytol.2003, 32, 743–766.
    • (2003) J. Neurocytol. , vol.32 , pp. 743-766
    • Rotundo, R.L.1
  • 17
    • 0141818332 scopus 로고    scopus 로고
    • Cholinergic function and Alzheimer’s disease
    • Giacobini, E. Cholinergic function and Alzheimer’s disease. Int. J. Geriatr Psych.2003, 18, S1–S5.
    • (2003) Int. J. Geriatr Psych. , vol.18 , pp. 1-5
    • Giacobini, E.1
  • 18
  • 19
    • 0018078940 scopus 로고
    • Correlation of cholinergic abnormalities with senile plaques and mental test-scores in senile dementia
    • Perry, E. K.; Tomlinson, B. E.; Blessed, G.; Bergmann, K.; Gibson, P. H.; Perry, R. H. Correlation of cholinergic abnormalities with senile plaques and mental test-scores in senile dementia. Brit. Med. J.1978, 2, 1457–1459.
    • (1978) Brit. Med. J. , vol.2 , pp. 1457-1459
    • Perry, E.K.1    Tomlinson, B.E.2    Blessed, G.3    Bergmann, K.4    Gibson, P.H.5    Perry, R.H.6
  • 22
    • 65749117793 scopus 로고    scopus 로고
    • Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy
    • Aggarwal, P.; Hall, J. B.; McLeland, C. B.; Dobrovolskaia, M. A.; McNeil, S. E. Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv. Drug Deliver. Rev.2009, 61, 428–437.
    • (2009) Adv. Drug Deliver. Rev. , vol.61 , pp. 428-437
    • Aggarwal, P.1    Hall, J.B.2    McLeland, C.B.3    Dobrovolskaia, M.A.4    McNeil, S.E.5
  • 24
    • 41749116115 scopus 로고    scopus 로고
    • Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter
    • Mu, Q. X.; Liu, W.; Xing, Y. H.; Zhou, H. Y.; Li, Z. W.; Zhang, Y.; Ji, L. H.; Wang, F.; Si, Z. K.; Zhang, B. et al. Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter. J. Phys. Chem. C2008, 112, 3300–3307.
    • (2008) J. Phys. Chem. C , vol.112 , pp. 3300-3307
    • Mu, Q.X.1    Liu, W.2    Xing, Y.H.3    Zhou, H.Y.4    Li, Z.W.5    Zhang, Y.6    Ji, L.H.7    Wang, F.8    Si, Z.K.9    Zhang, B.10
  • 25
    • 79851497437 scopus 로고    scopus 로고
    • Enhancing cell recognition by scrutinizing cell surfaces with a nanoparticle array
    • Zhou, H. Y.; Jiao, P. F.; Yang, L.; Li, X.; Yan, B. Enhancing cell recognition by scrutinizing cell surfaces with a nanoparticle array. J. Am. Chem. Soc.2011, 133, 680–682.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 680-682
    • Zhou, H.Y.1    Jiao, P.F.2    Yang, L.3    Li, X.4    Yan, B.5
  • 26
    • 77952827185 scopus 로고    scopus 로고
    • Structural confirmation and quantification of individual ligands from the surface of multi-functionalized gold nanoparticles
    • Zhou, H. Y.; Li, X.; Lemoff, A.; Zhang, B.; Yan, B. Structural confirmation and quantification of individual ligands from the surface of multi-functionalized gold nanoparticles. Analyst2010, 135, 1210–1213.
    • (2010) Analyst , vol.135 , pp. 1210-1213
    • Zhou, H.Y.1    Li, X.2    Lemoff, A.3    Zhang, B.4    Yan, B.5
  • 27
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y.; Barkley, M. D. Toward understanding tryptophan fluorescence in proteins. Biochem.1998, 37, 9976–9982.
    • (1998) Biochem. , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 28
    • 0039632504 scopus 로고
    • The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration
    • Crammer, J.; Neuberger, A. The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration. Biochem. J.1943, 37, 302–310.
    • (1943) Biochem. J. , vol.37 , pp. 302-310
    • Crammer, J.1    Neuberger, A.2
  • 29
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • Teale, F. W. J.; Weber, G. Ultraviolet fluorescence of the aromatic amino acids. Biochem. J.1957, 65, 476–482.
    • (1957) Biochem. J. , vol.65 , pp. 476-482
    • Teale, F.W.J.1    Weber, G.2
  • 31
    • 67949124727 scopus 로고    scopus 로고
    • Optimal sparse descriptor selection for QSAR using Bayesian methods
    • Burden, F. R.; Winkler, D. A. Optimal sparse descriptor selection for QSAR using Bayesian methods. QSAR Comb. Sci.2009, 28, 645–653.
    • (2009) QSAR Comb. Sci. , vol.28 , pp. 645-653
    • Burden, F.R.1    Winkler, D.A.2
  • 32
    • 0033549850 scopus 로고    scopus 로고
    • Robust QSAR models using Bayesian regularized neural networks
    • Burden, F. R.; Winkler, D. A. Robust QSAR models using Bayesian regularized neural networks. J. Med. Chem.1999, 42, 3183–3187.
    • (1999) J. Med. Chem. , vol.42 , pp. 3183-3187
    • Burden, F.R.1    Winkler, D.A.2
  • 33
    • 76749109588 scopus 로고    scopus 로고
    • An optimal self-pruning neural network and nonlinear descriptor selection in QSAR
    • Burden, F. R.; Winkler, D. A. An optimal self-pruning neural network and nonlinear descriptor selection in QSAR. QSAR Comb. Sci.2009, 28, 1092–1097.
    • (2009) QSAR Comb. Sci. , vol.28 , pp. 1092-1097
    • Burden, F.R.1    Winkler, D.A.2
  • 34
    • 84879698395 scopus 로고    scopus 로고
    • Aqueous solubility prediction: Do crystal lattice interactions help?
    • Salahinejad, M.; Le, T. C.; Winkler, D. A. Aqueous solubility prediction: Do crystal lattice interactions help? Mol. Pharmaceut.2013, 10, 2757–2766.
    • (2013) Mol. Pharmaceut. , vol.10 , pp. 2757-2766
    • Salahinejad, M.1    Le, T.C.2    Winkler, D.A.3
  • 35
    • 84873023995 scopus 로고    scopus 로고
    • Capturing the crystal: Prediction of enthalpy of sublimation, crystal lattice energy, and melting points of organic compounds
    • Salahinejad, M.; Le, T. C.; Winkler, D. A. Capturing the crystal: Prediction of enthalpy of sublimation, crystal lattice energy, and melting points of organic compounds. J. Chem. Inf. Model.2013, 53, 223–229.
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 223-229
    • Salahinejad, M.1    Le, T.C.2    Winkler, D.A.3
  • 36
    • 84886785069 scopus 로고    scopus 로고
    • Structures of human acetylcholinesterase bound to dihydrotanshinone I and territrem B show peripheral site flexibility
    • Cheung, J.; Gary, E. N.; Shiomi, K.; Rosenberry, T. L. Structures of human acetylcholinesterase bound to dihydrotanshinone I and territrem B show peripheral site flexibility. ACS Med. Chem. Lett.2013, 4, 1091–1096.
    • (2013) ACS Med. Chem. Lett. , vol.4 , pp. 1091-1096
    • Cheung, J.1    Gary, E.N.2    Shiomi, K.3    Rosenberry, T.L.4
  • 37
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman, G. L.; Courtney, K. D.; Andres, V.; Featherstone, R. M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol.1961, 7, 88–95.
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres, V.3    Featherstone, R.M.4
  • 38
    • 0017348776 scopus 로고
    • Hydrophobic quencher of protein fluorescence-2,2,2-trichloroethanol
    • Eftink, M. R.; Zajicek, J. L.; Ghiron, C. A. Hydrophobic quencher of protein fluorescence-2,2,2-trichloroethanol. Biochim. Biophys. Acta1977, 491, 473–481.
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 473-481
    • Eftink, M.R.1    Zajicek, J.L.2    Ghiron, C.A.3
  • 39
    • 33846390425 scopus 로고    scopus 로고
    • DRAGON software: An easy approach to molecular descriptor calculations
    • Mauri, A.; Consonni, V.; Pavan, M.; Todeschini, R. DRAGON software: An easy approach to molecular descriptor calculations. MATCHCommun. Math. Co.2006, 56, 237–248.
    • (2006) MATCHCommun. Math. Co. , vol.56 , pp. 237-248
    • Mauri, A.1    Consonni, V.2    Pavan, M.3    Todeschini, R.4
  • 40
    • 84861059886 scopus 로고    scopus 로고
    • Quantitative structure-property relationship modeling of diverse materials properties
    • Le, T.; Epa, V. C.; Burden, F. R.; Winkler, D. A. Quantitative structure-property relationship modeling of diverse materials properties. Chem. Rev.2012, 112, 2889–2919.
    • (2012) Chem. Rev. , vol.112 , pp. 2889-2919
    • Le, T.1    Epa, V.C.2    Burden, F.R.3    Winkler, D.A.4
  • 41
    • 0028543366 scopus 로고
    • Training feed forward networks with the Marquardt algorithm
    • Hagan, M. T.; Menhaj, M. Training feed forward networks with the Marquardt algorithm. IEEE Trans. Neural Netw.1994, 5, 989–993.
    • (1994) IEEE Trans. Neural Netw. , vol.5 , pp. 989-993
    • Hagan, M.T.1    Menhaj, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.