메뉴 건너뛰기




Volumn 32, Issue 29, 2011, Pages 7241-7252

Effect of gold nanoparticle morphology on adsorbed protein structure and function

Author keywords

Nanoparticle morphology; Protein adsorption; Protein nanoparticle conjugates; Surface energy

Indexed keywords

ADSORBED ENZYME; BIOMEDICAL APPLICATIONS; ENZYMATIC ACTIVITIES; GOLD NANOPARTICLES; GOLD NANOROD; GOLD NANOSPHERES; NANOPARTICLE MORPHOLOGY; PROTEIN ADSORPTION; PROTEIN LOADINGS; PROTEIN STRUCTURES; PROTEIN-NANOPARTICLE CONJUGATES; SECONDARY STRUCTURES; SURFACE COVERAGES; SURFACE DENSITY; SURFACE ENERGIES; TARGET MOLECULE;

EID: 79960846411     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.05.091     Document Type: Article
Times cited : (265)

References (62)
  • 1
    • 0000160454 scopus 로고
    • The Bakerian Lecture: experimental relations of gold (and other metals) to light
    • Faraday M. The Bakerian Lecture: experimental relations of gold (and other metals) to light. Philos Trans Royal Soc London 1857, 147:145-181.
    • (1857) Philos Trans Royal Soc London , vol.147 , pp. 145-181
    • Faraday, M.1
  • 2
    • 3242684959 scopus 로고    scopus 로고
    • Room temperature, high-yield synthesis of multiple shapes of gold nanoparticles in aqueous solution
    • Sau T.K., Murphy C.J. Room temperature, high-yield synthesis of multiple shapes of gold nanoparticles in aqueous solution. J Am Chem Soc 2004, 126:8648-8649.
    • (2004) J Am Chem Soc , vol.126 , pp. 8648-8649
    • Sau, T.K.1    Murphy, C.J.2
  • 4
    • 33845218226 scopus 로고    scopus 로고
    • h symmetry: from octahedra to cubes
    • h symmetry: from octahedra to cubes. J Am Chem Soc 2006, 128:14863-14870.
    • (2006) J Am Chem Soc , vol.128 , pp. 14863-14870
    • Seo, D.1    Park, J.C.2    Song, H.3
  • 6
    • 0036270364 scopus 로고    scopus 로고
    • Growth and form of gold nanorods prepared by seed-mediated, surfactant-directed synthesis
    • Johnson C.J., Dujardin E., Davis S.A., Murphy C.J., Mann S. Growth and form of gold nanorods prepared by seed-mediated, surfactant-directed synthesis. J Mater Chem 2002, 12:1765-1770.
    • (2002) J Mater Chem , vol.12 , pp. 1765-1770
    • Johnson, C.J.1    Dujardin, E.2    Davis, S.A.3    Murphy, C.J.4    Mann, S.5
  • 7
    • 58249124542 scopus 로고    scopus 로고
    • Skrabalak. Shape-controlled synthesis of metal nanocrystals: simple chemistry meets complex physics
    • Xia Y., Xiong Y., Lim B. Skrabalak. Shape-controlled synthesis of metal nanocrystals: simple chemistry meets complex physics. Angew Chem Int Ed Engl 2009, 48:60-103.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 60-103
    • Xia, Y.1    Xiong, Y.2    Lim, B.3
  • 8
    • 77951641729 scopus 로고    scopus 로고
    • Nonspherical noble metal nanoparticles: colloid-chemical synthesis and morphology control
    • Sau T.K., Rogach A.L. Nonspherical noble metal nanoparticles: colloid-chemical synthesis and morphology control. Adv Mater 2009, 21:1-24.
    • (2009) Adv Mater , vol.21 , pp. 1-24
    • Sau, T.K.1    Rogach, A.L.2
  • 9
    • 33644642166 scopus 로고    scopus 로고
    • Why gold nanoparticles are more precious than pretty gold: noble metal surface plasmon resonance and its enhancement of the radiative and nonradiative properties of nanocrystals of different shapes
    • Eustis S., El-Sayed M.A. Why gold nanoparticles are more precious than pretty gold: noble metal surface plasmon resonance and its enhancement of the radiative and nonradiative properties of nanocrystals of different shapes. Chem Soc Rev 2006, 35:209-217.
    • (2006) Chem Soc Rev , vol.35 , pp. 209-217
    • Eustis, S.1    El-Sayed, M.A.2
  • 10
    • 0000817598 scopus 로고    scopus 로고
    • Size and temperature dependence of the plasmon absorption of colloidal gold nanoparticles
    • Link S., El-Sayed M.A. Size and temperature dependence of the plasmon absorption of colloidal gold nanoparticles. J Phys Chem B 1999, 103:4212-4217.
    • (1999) J Phys Chem B , vol.103 , pp. 4212-4217
    • Link, S.1    El-Sayed, M.A.2
  • 11
    • 33646228165 scopus 로고    scopus 로고
    • Calculated absorption and scattering properties of gold nanoparticles of different size, shape, and composition: applications in biological imaging and biomedicine
    • Jain P.K., Lee K.S., El-Sayed I.H., El-Sayed M.A. Calculated absorption and scattering properties of gold nanoparticles of different size, shape, and composition: applications in biological imaging and biomedicine. J Phys Chem B 2006, 110:7238-7248.
    • (2006) J Phys Chem B , vol.110 , pp. 7238-7248
    • Jain, P.K.1    Lee, K.S.2    El-Sayed, I.H.3    El-Sayed, M.A.4
  • 12
    • 42449095051 scopus 로고    scopus 로고
    • Multi-functional gold nanoparticles for drug delivery
    • Han G., Ghosh P., Rotello V.M. Multi-functional gold nanoparticles for drug delivery. Adv Exp Med Biol 2007, 620:48-56.
    • (2007) Adv Exp Med Biol , vol.620 , pp. 48-56
    • Han, G.1    Ghosh, P.2    Rotello, V.M.3
  • 13
    • 58049206937 scopus 로고    scopus 로고
    • Efficient gene delivery vectors by tuning the surface charge density of amino acid-functionalized gold nanoparticles
    • Ghosh P.S., Kim C.-K., Han G., Forbes N.S., Rotello V.M. Efficient gene delivery vectors by tuning the surface charge density of amino acid-functionalized gold nanoparticles. ACS Nano 2008, 2:2213-2218.
    • (2008) ACS Nano , vol.2 , pp. 2213-2218
    • Ghosh, P.S.1    Kim, C.-K.2    Han, G.3    Forbes, N.S.4    Rotello, V.M.5
  • 14
    • 77949762340 scopus 로고    scopus 로고
    • Targeting of drugs and nanoparticles to tumors
    • Ruoslahti E., Bhatia S.N., Sailor M.J. Targeting of drugs and nanoparticles to tumors. J Cell Biol 2010, 188:759-768.
    • (2010) J Cell Biol , vol.188 , pp. 759-768
    • Ruoslahti, E.1    Bhatia, S.N.2    Sailor, M.J.3
  • 15
    • 33244457595 scopus 로고    scopus 로고
    • Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods
    • Huang X., El-Sayed I.H., Qian W., El-Sayed M.A. Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods. J Am Chem Soc 2006, 128:2115-2120.
    • (2006) J Am Chem Soc , vol.128 , pp. 2115-2120
    • Huang, X.1    El-Sayed, I.H.2    Qian, W.3    El-Sayed, M.A.4
  • 17
    • 65949096862 scopus 로고    scopus 로고
    • Computationally guided photothermal tumor therapy using long-circulating gold nanorod antennas
    • von Maltzahn G., Park J.H., Agrawal A., Bandaru N.K., Das S.K., Sailor M.J., et al. Computationally guided photothermal tumor therapy using long-circulating gold nanorod antennas. Cancer Res 2009, 69:3892-3900.
    • (2009) Cancer Res , vol.69 , pp. 3892-3900
    • von Maltzahn, G.1    Park, J.H.2    Agrawal, A.3    Bandaru, N.K.4    Das, S.K.5    Sailor, M.J.6
  • 21
    • 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., et al. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 2007, 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
  • 22
    • 70249141572 scopus 로고    scopus 로고
    • A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
    • Röker C., Pötzl M., Zhang F., Parak W.J., Nienhaus G.U. A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles. Nat Nanotechnol 2009, 4:577-580.
    • (2009) Nat Nanotechnol , vol.4 , pp. 577-580
    • Röker, C.1    Pötzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 23
    • 4043075579 scopus 로고    scopus 로고
    • Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme
    • Vertegel A.A., Siegel R.W., Dordick J.S. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir 2004, 20:6800-6807.
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 24
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • Asuri P., Bale S.S., Pangule R.C., Shah D.A., Kane R.S., Dordick J.S. Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 2007, 23:12318-12321.
    • (2007) Langmuir , vol.23 , pp. 12318-12321
    • Asuri, P.1    Bale, S.S.2    Pangule, R.C.3    Shah, D.A.4    Kane, R.S.5    Dordick, J.S.6
  • 26
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry
    • Roach P., Farrar D., Perry C.C. Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc 2006, 128:3939-3945.
    • (2006) J Am Chem Soc , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 27
    • 29844434629 scopus 로고    scopus 로고
    • Gold nanoparticle-cytochrome c complexes: the effect of nanoparticle ligand charge on protein structure
    • Aubin-Tam M.E., Hamad-Schifferli K. Gold nanoparticle-cytochrome c complexes: the effect of nanoparticle ligand charge on protein structure. Langmuir 2005, 21:12080-12084.
    • (2005) Langmuir , vol.21 , pp. 12080-12084
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 28
    • 52649165549 scopus 로고    scopus 로고
    • Structure and function of nanoparticle-protein conjugates
    • Aubin-Tam M.E., Hamad-Schifferli K. Structure and function of nanoparticle-protein conjugates. Biomed Mater 2008, 3:034001.
    • (2008) Biomed Mater , vol.3 , pp. 034001
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 30
    • 33847781099 scopus 로고    scopus 로고
    • Probing the interactions of proteins and nanoparticles
    • Klein J. Probing the interactions of proteins and nanoparticles. Proc Natl Acad Sci USA 2007, 104:2029-2030.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2029-2030
    • Klein, J.1
  • 32
    • 0035797987 scopus 로고    scopus 로고
    • Evidence for bilayer assembly of cationic surfactants on the surface of gold nanorods
    • Nikoobakht B., El-Sayed M.A. Evidence for bilayer assembly of cationic surfactants on the surface of gold nanorods. Langmuir 2001, 17:6368-6374.
    • (2001) Langmuir , vol.17 , pp. 6368-6374
    • Nikoobakht, B.1    El-Sayed, M.A.2
  • 33
    • 0345979435 scopus 로고    scopus 로고
    • Formation and structure of self-assembled monolayers
    • Ulman A. Formation and structure of self-assembled monolayers. Chem Rev 1996, 96:1533-1554.
    • (1996) Chem Rev , vol.96 , pp. 1533-1554
    • Ulman, A.1
  • 35
    • 0035976235 scopus 로고    scopus 로고
    • Seeding growth for size control of 5-40 nm diameter gold nanoparticles
    • Jana N.R., Gearheart L., Murphy C.J. Seeding growth for size control of 5-40 nm diameter gold nanoparticles. Langmuir 2001, 17:6782-6786.
    • (2001) Langmuir , vol.17 , pp. 6782-6786
    • Jana, N.R.1    Gearheart, L.2    Murphy, C.J.3
  • 36
    • 0038175155 scopus 로고    scopus 로고
    • Preparation and growth mechanism of gold nanorods (nrs) using seed-mediated growth method
    • Nikoobakht B., El-Sayed M.A. Preparation and growth mechanism of gold nanorods (nrs) using seed-mediated growth method. Chem Mater 2003, 15:1957-1962.
    • (2003) Chem Mater , vol.15 , pp. 1957-1962
    • Nikoobakht, B.1    El-Sayed, M.A.2
  • 37
    • 52649153565 scopus 로고    scopus 로고
    • Ligand customization and DNA functionalization of gold nanorods via round-trip phase transfer ligand exchange
    • Wijaya A., Hamad-Schifferli K. Ligand customization and DNA functionalization of gold nanorods via round-trip phase transfer ligand exchange. Langmuir 2008, 24:9966-9969.
    • (2008) Langmuir , vol.24 , pp. 9966-9969
    • Wijaya, A.1    Hamad-Schifferli, K.2
  • 39
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield N.J. Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 2007, 1:2876-2890.
    • (2007) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 40
    • 0021809359 scopus 로고
    • Structure of α-chymotrypsin refined at 1.68Å resolution
    • Tsukada H., Blow D.M. Structure of α-chymotrypsin refined at 1.68Å resolution. J Mol Biol 1985, 184:703-711.
    • (1985) J Mol Biol , vol.184 , pp. 703-711
    • Tsukada, H.1    Blow, D.M.2
  • 41
    • 0019871883 scopus 로고
    • Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme
    • Kato S., Okamura M., Shimamoto N., Utiyama H. Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme. Biochemistry 1981, 20:1080-1085.
    • (1981) Biochemistry , vol.20 , pp. 1080-1085
    • Kato, S.1    Okamura, M.2    Shimamoto, N.3    Utiyama, H.4
  • 42
    • 0242330803 scopus 로고    scopus 로고
    • Reversible "irreversible" inhibition of chymotrypsin using nanoparticle receptors
    • Fischer N.O., Verma A., Goodman C.M., Simard J.M., Rotello V.M. Reversible "irreversible" inhibition of chymotrypsin using nanoparticle receptors. J Am Chem Soc 2003, 125:13387-13391.
    • (2003) J Am Chem Soc , vol.125 , pp. 13387-13391
    • Fischer, N.O.1    Verma, A.2    Goodman, C.M.3    Simard, J.M.4    Rotello, V.M.5
  • 43
    • 63149188558 scopus 로고    scopus 로고
    • Cellular uptake and cytotoxicity of gold nanorods: molecular origin of cytotoxicity and surface effects
    • Alkilany A.M., Nagaria P.K., Hexel C.R., Shaw T.J., Murphy C.J., Wyatt M.D. Cellular uptake and cytotoxicity of gold nanorods: molecular origin of cytotoxicity and surface effects. Small 2009, 5:701-708.
    • (2009) Small , vol.5 , pp. 701-708
    • Alkilany, A.M.1    Nagaria, P.K.2    Hexel, C.R.3    Shaw, T.J.4    Murphy, C.J.5    Wyatt, M.D.6
  • 44
    • 3242775472 scopus 로고    scopus 로고
    • Toxicity of gold nanoparticles functionalized with cationic and anionic side chains
    • Goodman C.M., McCusker C.D., Yilmax T., Rotello V.M. Toxicity of gold nanoparticles functionalized with cationic and anionic side chains. Bioconjug Chem 2004, 15:897-900.
    • (2004) Bioconjug Chem , vol.15 , pp. 897-900
    • Goodman, C.M.1    McCusker, C.D.2    Yilmax, T.3    Rotello, V.M.4
  • 45
    • 34248155667 scopus 로고    scopus 로고
    • Systematic investigation of the thermodynamics of HSA adsorption to n-iso-propylacrylamide/n-tert-butylacrylamide copolymer nanoparticles: effects of particle size and hydrophobicity
    • Lindman S., Lynch I., Thulin E., Nilsson H., Dawson K.A., Linse S. Systematic investigation of the thermodynamics of HSA adsorption to n-iso-propylacrylamide/n-tert-butylacrylamide copolymer nanoparticles: effects of particle size and hydrophobicity. Nano Lett 2007, 7:914-920.
    • (2007) Nano Lett , vol.7 , pp. 914-920
    • Lindman, S.1    Lynch, I.2    Thulin, E.3    Nilsson, H.4    Dawson, K.A.5    Linse, S.6
  • 46
    • 77958474675 scopus 로고    scopus 로고
    • Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme for experiment and molecular dynamics
    • Meersman F., Atilgan C., Miles A.J., Bader R., Shang W., Matagne A., et al. Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme for experiment and molecular dynamics. Biophys J 2010, 22:2255-2263.
    • (2010) Biophys J , vol.22 , pp. 2255-2263
    • Meersman, F.1    Atilgan, C.2    Miles, A.J.3    Bader, R.4    Shang, W.5    Matagne, A.6
  • 47
    • 58149157464 scopus 로고    scopus 로고
    • Conformational changes of α-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study
    • Razael-Ghaleh N., Amininasab M., Nemat-Gorgani M. Conformational changes of α-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study. Biophys J 2008, 95:4139-4147.
    • (2008) Biophys J , vol.95 , pp. 4139-4147
    • Razael-Ghaleh, N.1    Amininasab, M.2    Nemat-Gorgani, M.3
  • 48
    • 34547575591 scopus 로고    scopus 로고
    • On the universal scaling behavior of the distance decay of plasmon coupling in metal nanoparticle pairs: a plasmon ruler equation
    • Jain P.K., Huang W., El-Sayed M.A. On the universal scaling behavior of the distance decay of plasmon coupling in metal nanoparticle pairs: a plasmon ruler equation. Nano Lett 2007, 7:2080-2088.
    • (2007) Nano Lett , vol.7 , pp. 2080-2088
    • Jain, P.K.1    Huang, W.2    El-Sayed, M.A.3
  • 49
    • 47149101965 scopus 로고    scopus 로고
    • Surface plasmon coupling and its universal size scaling in metal nanostructures of complex geometry: elongated particle pairs and nanosphere trimers
    • Jain P.K., El-Sayed M.A. Surface plasmon coupling and its universal size scaling in metal nanostructures of complex geometry: elongated particle pairs and nanosphere trimers. J Phys Chem C Nanomater Interfaces 2008, 112:2954-2960.
    • (2008) J Phys Chem C Nanomater Interfaces , vol.112 , pp. 2954-2960
    • Jain, P.K.1    El-Sayed, M.A.2
  • 50
    • 6444238024 scopus 로고    scopus 로고
    • Monolayer-controlled substrate selectivity using noncovalent enzyme-nanoparticle conjugates
    • Hong R., Emrick T., Rotello V.M. Monolayer-controlled substrate selectivity using noncovalent enzyme-nanoparticle conjugates. J Am Chem Soc 2004, 126:13572-13573.
    • (2004) J Am Chem Soc , vol.126 , pp. 13572-13573
    • Hong, R.1    Emrick, T.2    Rotello, V.M.3
  • 51
    • 77955175216 scopus 로고    scopus 로고
    • Strategies in the design of nanoparticles for therapeutic applications
    • Petros R.A., DeSimone J.M. Strategies in the design of nanoparticles for therapeutic applications. Nat Rev Drug Discov 2010, 9:615-627.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 615-627
    • Petros, R.A.1    DeSimone, J.M.2
  • 52
  • 53
    • 4043127847 scopus 로고    scopus 로고
    • Principles of nucleation and growth
    • P.M. Dove, J.J. DeYoreo, S. Weiner (Eds.)
    • De Yoreo J.J., Vekilov P.G. Principles of nucleation and growth. Rev mineral geochem 2003, vol. 54:57-93. P.M. Dove, J.J. DeYoreo, S. Weiner (Eds.).
    • (2003) Rev mineral geochem , vol.54 , pp. 57-93
    • De Yoreo, J.J.1    Vekilov, P.G.2
  • 54
    • 33745748175 scopus 로고    scopus 로고
    • Engineering protein activity and stability through control of the nanoscale environment
    • Asuri P., Karajanagi S., Yim T.-G., Kane R.S., Dordick J.S. Engineering protein activity and stability through control of the nanoscale environment. Langmuir 2006, 22:5833-5836.
    • (2006) Langmuir , vol.22 , pp. 5833-5836
    • Asuri, P.1    Karajanagi, S.2    Yim, T.-G.3    Kane, R.S.4    Dordick, J.S.5
  • 55
    • 34447291808 scopus 로고    scopus 로고
    • Binding of lyzosyme to phospholipid bilayers: evidence for protein aggregation upon membrane association
    • Gorbenko G.P., Ioffe V.M., Kinnunen P.K.J. Binding of lyzosyme to phospholipid bilayers: evidence for protein aggregation upon membrane association. Biophys J 2007, 93:140-153.
    • (2007) Biophys J , vol.93 , pp. 140-153
    • Gorbenko, G.P.1    Ioffe, V.M.2    Kinnunen, P.K.J.3
  • 56
    • 63649114518 scopus 로고    scopus 로고
    • Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH
    • Zhang D., Neumann O., Wang H., Yuwono V.M., Barhoumi A., Perham M., et al. Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH. Nano Lett 2009, 9:666-671.
    • (2009) Nano Lett , vol.9 , pp. 666-671
    • Zhang, D.1    Neumann, O.2    Wang, H.3    Yuwono, V.M.4    Barhoumi, A.5    Perham, M.6
  • 57
    • 54049144209 scopus 로고    scopus 로고
    • Effect of surface concentration on secondary and tertiary conformational changes of lysozyme adsorbed on silica nanoparticles
    • Wu X., Narsimhan G. Effect of surface concentration on secondary and tertiary conformational changes of lysozyme adsorbed on silica nanoparticles. Biochim Biophys Acta 2008, 1784:1694-1701.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1694-1701
    • Wu, X.1    Narsimhan, G.2
  • 58
    • 0007601535 scopus 로고
    • The adsorption of gases on plane surfaces of glass, mica, and platinum
    • Langmuir I. The adsorption of gases on plane surfaces of glass, mica, and platinum. J Am Chem Soc 1918, 40:1361.
    • (1918) J Am Chem Soc , vol.40 , pp. 1361
    • Langmuir, I.1
  • 59
    • 0001674603 scopus 로고
    • Über die adsorption in lösungen
    • Freundlich H. Über die adsorption in lösungen. Z Phyz Chem 1907, 57:385.
    • (1907) Z Phyz Chem , vol.57 , pp. 385
    • Freundlich, H.1
  • 60
    • 0035863843 scopus 로고    scopus 로고
    • Interactions of proteins with immobilized metal ions: a comparative analysis using various isotherm models
    • Sharma S., Agarwal G.P. Interactions of proteins with immobilized metal ions: a comparative analysis using various isotherm models. Anal Biochem 2001, 288:126-140.
    • (2001) Anal Biochem , vol.288 , pp. 126-140
    • Sharma, S.1    Agarwal, G.P.2
  • 62
    • 72449188290 scopus 로고    scopus 로고
    • What is the correct form of BET isotherm for modeling liquid phase adsorption?
    • Ebadi A., Mohammadzadeh J.S.S., Khudiev A. What is the correct form of BET isotherm for modeling liquid phase adsorption?. Adsorption 2009, 15:65-73.
    • (2009) Adsorption , vol.15 , pp. 65-73
    • Ebadi, A.1    Mohammadzadeh, J.S.S.2    Khudiev, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.