메뉴 건너뛰기




Volumn 1808, Issue 9, 2011, Pages 2128-2135

Multivalent protein binding in carbohydrate-functionalized monolayers through protein-directed rearrangement and reorientation of glycolipids at the air-water interface

Author keywords

Aqueous monolayer; Infrared spectroscopy; Lipid rearrangement; Multivalent protein binding; Surface plasmon resonance

Indexed keywords

1,2 DI O HEXADECYL SN GLYCEROL; CARBOHYDRATE; CONCANAVALIN A; GLYCEROL DERIVATIVE; GLYCOLIPID; MANNOSE; UNCLASSIFIED DRUG; WATER;

EID: 79959951106     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.04.019     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • N. Sharon, and H. Lis Lectins as cell recognition molecules Science 246 1989 227 234 (Pubitemid 19264635)
    • (1989) Science , vol.246 , Issue.4927 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 2
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • DOI 10.1126/science.1059820
    • C.R. Bertozzi, and L.L. Kiessling Chemical glycobiology Science 291 2001 2357 2364 (Pubitemid 32231790)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 3
    • 34250693209 scopus 로고    scopus 로고
    • Deciphering the glycocode: The complexity and analytical challenge of glycomics
    • DOI 10.1016/j.cbpa.2007.05.002, PII S1367593107000518
    • K.T. Pilobello, and L.K. Mahal Deciphering the glycocode: the complexity and analytical challenge of glycomics Curr. Opin. Chem. Biol. 11 2007 300 305 (Pubitemid 46963071)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.3 , pp. 300-305
    • Pilobello, K.T.1    Mahal, L.K.2
  • 4
    • 0033638783 scopus 로고    scopus 로고
    • Synthetic multivalent ligands in the exploration of cell-surface interactions
    • L.L. Kiessling, J.E. Gestwicki, and L.E. Strong Synthetic multivalent ligands in the exploration of cell-surface interactions Curr. Opin. Chem. Biol. 4 2000 696 703
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 696-703
    • Kiessling, L.L.1    Gestwicki, J.E.2    Strong, L.E.3
  • 6
    • 34548725053 scopus 로고    scopus 로고
    • Quantitative analysis of carbohydrate-protein interactions using glycan microarrays: Determination of surface and solution dissociation constants
    • DOI 10.1021/ja072931h
    • P.-H. Liang, S.-K. Wang, and C.-H. Wong Quantitative analysis of carbohydrate-protein interactions using glycan microarrays: determination of surface and solution dissociation constants J. Am. Chem. Soc. 129 2007 11177 11184 (Pubitemid 47435721)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.36 , pp. 11177-11184
    • Liang, P.-H.1    Wang, S.-K.2    Wong, C.-H.3
  • 8
    • 0037462084 scopus 로고    scopus 로고
    • Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: The effect of hapten density
    • DOI 10.1021/ja029469f
    • T. Yang, O.K. Baryshnikova, H. Mao, M.A. Hojden, and P.S. Cremer Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: the effect of hapten density J. Am. Chem. Soc. 125 2003 4779 4784 (Pubitemid 36505369)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.16 , pp. 4779-4784
    • Yang, T.1    Baryshnikova, O.K.2    Mao, H.3    Holden, M.A.4    Cremer, P.S.5
  • 9
    • 70350049076 scopus 로고    scopus 로고
    • Biophysical interactions with model lipid membranes: Applications in drug discovery and drug delivery
    • C. Peetla, A. Stine, and V. Labhasetwar Biophysical interactions with model lipid membranes: applications in drug discovery and drug delivery Mol. Pharmaceutics 6 2009 1264 1276
    • (2009) Mol. Pharmaceutics , vol.6 , pp. 1264-1276
    • Peetla, C.1    Stine, A.2    Labhasetwar, V.3
  • 10
    • 33751421208 scopus 로고    scopus 로고
    • Molecular recognition at Langmuir monolayers
    • DOI 10.1016/j.cbpa.2006.09.010, PII S1367593106001499
    • R.M. Leblanc Molecular recognition at Langmuir monolayers Curr. Opin. Chem. Biol. 10 2006 529 536 (Pubitemid 44821890)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.6 , pp. 529-536
    • Leblanc, R.M.1
  • 11
    • 0028592578 scopus 로고
    • A kinetic study of concanavalin a binding to glycolipid monolayers by using a quartz crystal microbalance
    • Y. Ebara, and Y. Okahata A kinetic study of concanavalin a binding to glycolipid monolayers by using a quartz crystal microbalance J. Am. Chem. Soc. 116 1994 11209 11212
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11209-11212
    • Ebara, Y.1    Okahata, Y.2
  • 12
    • 0033038419 scopus 로고    scopus 로고
    • Molecular recognition of concanavalin A on mannoside diacetylene lipid monolayer at the air-water interface
    • DOI 10.1016/S0005-2736(99)00079-6, PII S0005273699000796
    • S. Wang, and R.M. Leblanc Molecular recognition of concanavalin A on mannoside diacetylene lipid monolayer at the air-water interface Biochim. Biophys. Acta 1419 1999 307 312 (Pubitemid 29322720)
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1419 , Issue.2 , pp. 307-312
    • Wang, S.1    Leblanc, R.M.2
  • 13
    • 16344387506 scopus 로고    scopus 로고
    • Fibroblast cell behavior on bound and adsorbed fibronectin onto hyaluronan and sulfated hyaluronan substrates
    • DOI 10.1021/bm049642v
    • R. Barbucci, A. Magnani, A. Chiumiento, D. Pasqui, I. Cangioli, and S. Lamponi Fibroblast cell behavior on bound and adsorbed fibronectin onto hyaluronan and sulfated hyaluronan substrates Biomacromolecules 6 2005 638 645 (Pubitemid 40467804)
    • (2005) Biomacromolecules , vol.6 , Issue.2 , pp. 638-645
    • Barbucci, R.1    Magnani, A.2    Chiumiento, A.3    Pasqui, D.4    Cangioli, I.5    Lamponi, S.6
  • 14
    • 0015516458 scopus 로고
    • Structure of concanavalin A at 2.4-å resolution
    • K.D. Hardman, and C.F. Ainsworth Structure of concanavalin A at 2.4-å resolution Biochemistry 11 1972 4910 4919
    • (1972) Biochemistry , vol.11 , pp. 4910-4919
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 15
    • 0017262126 scopus 로고
    • New evidence on the location of the saccharide-binding site of concanavalin A
    • J.W. Becker, G.N. Reeke Jr., B.A. Cunningham, and G.M. Edelman New evidence on the location of the saccharide-binding site of concanavalin A Nature 259 1976 406 409
    • (1976) Nature , vol.259 , pp. 406-409
    • Becker, J.W.1    Reeke, Jr.G.N.2    Cunningham, B.A.3    Edelman, G.M.4
  • 16
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • M.I. Page, and W.P. Jencks Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect Proc. Natl. Acad. Sci. U. S. A. 68 1971 1678 1683
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 18
    • 0033559562 scopus 로고    scopus 로고
    • The role of ligand density in the enzymatic glycosylation of carbohydrates presented on self-assembled monolayers of alkanethiolates on gold
    • B.T. Houseman, and M. Mrksich The role of ligand density in the enzymatic glycosylation of carbohydrates presented on self-assembled monolayers of alkanethiolates on gold Angew. Chem. Int. Ed. 38 1999 782 785 (Pubitemid 29146593)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.6 , pp. 782-785
    • Houseman, B.T.1    Mrksich, M.2
  • 19
    • 4644259960 scopus 로고    scopus 로고
    • A comparative analysis of localized and propagating surface plasmon resonance sensors: The binding of Concanavalin A to a monosaccharide functionalized self-assembled monolayer
    • DOI 10.1021/ja047118q
    • C.R. Yonzon, E. Jeoung, S. Zou, G.C. Schatz, M. Mrksich, and R.P. Van Duyne A comparative analysis of localized and propagating surface plasmon resonance sensors: the binding of concanavalin a to a monosaccharide functionalized self-assembled monolayer J. Am. Chem. Soc. 126 2004 12669 12676 (Pubitemid 39304946)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.39 , pp. 12669-12676
    • Yonzon, C.R.1    Jeoung, E.2    Zou, S.3    Schatz, G.C.4    Mrksich, M.5    Van Duyne, R.P.6
  • 20
    • 33947360777 scopus 로고    scopus 로고
    • Nonlabeled quartz crystal microbalance biosensor for bacterial detection using carbohydrate and lectin recognitions
    • DOI 10.1021/ac061986j
    • Z. Shen, M. Huang, C. Xiao, Y. Zhang, X. Zeng, and P. Wang Nonlabeled quartz crystal microbalance biosensor for bacterial detection using carbohydrate and lectin recognitions Anal. Chem. 79 2007 2312 2319 (Pubitemid 46449010)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2312-2319
    • Shen, Z.1    Huang, M.2    Xiao, C.3    Zhang, Y.4    Zeng, X.5    Wang, P.G.6
  • 21
    • 61849142157 scopus 로고    scopus 로고
    • Optimization of immobilized bacterial disaccharides for surface plasmon resonance imaging measurements of antibody binding
    • C.F. Grant, V. Kanda, H. Yu, D.R. Bundle, and M.T. McDermott Optimization of immobilized bacterial disaccharides for surface plasmon resonance imaging measurements of antibody binding Langmuir 24 2008 14125 14132
    • (2008) Langmuir , vol.24 , pp. 14125-14132
    • Grant, C.F.1    Kanda, V.2    Yu, H.3    Bundle, D.R.4    McDermott, M.T.5
  • 22
    • 62849092747 scopus 로고    scopus 로고
    • Surface functionalization of nanomaterials with dendritic groups: Toward enhanced binding to biological targets
    • A.L. Martin, B. Li, and E.R. Gillies Surface functionalization of nanomaterials with dendritic groups: toward enhanced binding to biological targets J. Am. Chem. Soc. 131 2009 734 741
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 734-741
    • Martin, A.L.1    Li, B.2    Gillies, E.R.3
  • 24
    • 0032556246 scopus 로고    scopus 로고
    • Probing low affinity and multivalent interactions with surface plasmon resonance: Ligands for concanavalin A
    • DOI 10.1021/ja9818506
    • D.A. Mann, M. Kanai, D.J. Maly, and L.L. Kiessling Probing low affinity and multivalent interactions with surface plasmon resonance: ligands for concanavalin A J. Am. Chem. Soc. 120 1998 10575 10582 (Pubitemid 28498799)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.41 , pp. 10575-10582
    • Mann, D.A.1    Kanai, M.2    Maly, D.J.3    Kiessling, L.L.4
  • 25
    • 61449223579 scopus 로고    scopus 로고
    • Regenerable tethered bilayer lipid membrane arrays for multiplexed label-free analysis of lipid-protein interactions on poly(dimethylsiloxane) microchips using SPR imaging
    • J.D. Taylor, M.J. Linman, T. Wilkop, and Q. Cheng Regenerable tethered bilayer lipid membrane arrays for multiplexed label-free analysis of lipid-protein interactions on poly(dimethylsiloxane) microchips using SPR imaging Anal. Chem. 81 2009 1146 1153
    • (2009) Anal. Chem. , vol.81 , pp. 1146-1153
    • Taylor, J.D.1    Linman, M.J.2    Wilkop, T.3    Cheng, Q.4
  • 26
    • 68549110369 scopus 로고    scopus 로고
    • Enhanced binding and biosensing of carbohydrate-functionalized monolayers to target proteins by surface molecular imprinting
    • H. Zheng, and X. Du Enhanced binding and biosensing of carbohydrate-functionalized monolayers to target proteins by surface molecular imprinting J. Phys. Chem. B 113 2009 11330 11377
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11330-11377
    • Zheng, H.1    Du, X.2
  • 27
    • 75649085273 scopus 로고    scopus 로고
    • Protein-directed spatial rearrangement of glycolipids at the air-water interface for bivalent protein binding: In situ infrared reflection absorption spectroscopy
    • H. Zheng, and X. Du Protein-directed spatial rearrangement of glycolipids at the air-water interface for bivalent protein binding: in situ infrared reflection absorption spectroscopy J. Phys. Chem. B 114 2010 577 584
    • (2010) J. Phys. Chem. B , vol.114 , pp. 577-584
    • Zheng, H.1    Du, X.2
  • 28
    • 0033963472 scopus 로고    scopus 로고
    • Synthesis of the sialyl Lewis X epitope attached to glycolipids with different core structures and their selectin-binding characteristics in a dynamic test system
    • C. Gege, J. Vogel, G. Bendas, U. Rothe, and R.R. Schmidt Synthesis of the sialyl Lewis X epitope attached to glycolipids with different core structures and their selectin-binding characteristics in a dynamic test system Chem. Eur. J. 6 2000 111 122
    • (2000) Chem. Eur. J. , vol.6 , pp. 111-122
    • Gege, C.1    Vogel, J.2    Bendas, G.3    Rothe, U.4    Schmidt, R.R.5
  • 29
    • 33947368541 scopus 로고    scopus 로고
    • Directed assembly of binary monolayers with a high protein affinity: Infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR)
    • DOI 10.1021/jp0653196
    • X. Du, and Y. Wang Directed assembly of binary monolayers with a high protein affinity: infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR) J. Phys. Chem. B 111 2007 2347 2356 (Pubitemid 46447569)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.9 , pp. 2347-2356
    • Du, X.1    Wang, Y.2
  • 30
    • 0034599661 scopus 로고    scopus 로고
    • Recent trends in the application of evanescent wave biosensors
    • DOI 10.1002/(SICI)1521-3773(20000403)39:7<1219::AID-ANIE1219>3.0. CO;2-5
    • T. Weimar Recent trends in the application of evanescent wave biosensors Angew. Chem. Int. Ed. 39 2000 1219 1221 (Pubitemid 30219909)
    • (2000) Angewandte Chemie - International Edition , vol.39 , Issue.7 , pp. 1219-1221
    • Weimar, T.1
  • 31
    • 0036712656 scopus 로고    scopus 로고
    • Analysis of biomolecular interactions using a miniaturized surface plasmon resonance sensor
    • DOI 10.1021/ac025669y
    • R.J. Whelan, T. Wohland, L. Neumann, B. Huang, B.K. Kobilka, and R.N. Zare Analysis of biomolecular interactions using a miniaturized surface plasmon resonance sensor Anal. Chem. 74 2002 4570 4576 (Pubitemid 35006449)
    • (2002) Analytical Chemistry , vol.74 , Issue.17 , pp. 4570-4576
    • Whelan, R.J.1    Wohland, T.2    Neumann, L.3    Huang, B.4    Kobilka, B.K.5    Zare, R.N.6
  • 32
    • 34547371683 scopus 로고    scopus 로고
    • Protein-directed assembly of binary monolayers at the interface and surface patterns of protein on the monolayers
    • DOI 10.1021/la700955f
    • X. Du, Y. Wang, Y. Ding, and R. Guo Protein-directed assembly of binary monolayers at the interface and surface patterns of protein on the monolayers Langmuir 23 2007 8142 8149 (Pubitemid 47155328)
    • (2007) Langmuir , vol.23 , Issue.15 , pp. 8142-8149
    • Du, X.1    Wang, Y.2    Ding, Y.3    Guo, R.4
  • 33
    • 14644414801 scopus 로고    scopus 로고
    • Langmuir monolayer approaches to protein recognition through molecular imprinting
    • DOI 10.1016/j.bios.2004.08.044, PII S0956566304004002
    • X. Du, V. Hlady, and D. Britt Langmuir monolayer approaches to protein recognition through molecular imprinting Biosens. Bioelectron. 20 2005 2053 2060 (Pubitemid 40312102)
    • (2005) Biosensors and Bioelectronics , vol.20 , Issue.10 SPEC. ISS. , pp. 2053-2060
    • Du, X.1    Hlady, V.2    Britt, D.3
  • 34
    • 5244297041 scopus 로고
    • Carbon-hydrogen stretching modes and the structure of n-alkyl chains. 1. Long, disordered chains
    • R.G. Snyder, H.L. Strauss, and C.A. Elliger Carbon-hydrogen stretching modes and the structure of n-alkyl chains. 1. Long, disordered chains J. Phys. Chem. 86 1982 5145 5150
    • (1982) J. Phys. Chem. , vol.86 , pp. 5145-5150
    • Snyder, R.G.1    Strauss, H.L.2    Elliger, C.A.3
  • 35
    • 0019323430 scopus 로고
    • The gel phase of dipalmitoyl phosphatidylcholine. An infrared characterization of the acyl chain packing
    • D.G. Cameron, H.L. Casal, E.F. Gudgin, and H.H. Mantsch The gel phase of dipalmitoyl phosphatidylcholine. An infrared characterization of the acyl chain packing Biochim. Biophys. Acta 596 1980 463 467
    • (1980) Biochim. Biophys. Acta , vol.596 , pp. 463-467
    • Cameron, D.G.1    Casal, H.L.2    Gudgin, E.F.3    Mantsch, H.H.4
  • 36
    • 33746576834 scopus 로고    scopus 로고
    • Miscibility of binary monolayers at the air - Water interface and interaction of protein with immobilized monolayers by surface plasmon resonance technique
    • DOI 10.1021/la0605642
    • Y. Wang, and X. Du Miscibility of binary monolayers at the air-water interface and interaction of protein with immobilized monolayers by surface plasmon resonance technique Langmuir 22 2006 6195 6202 (Pubitemid 44140316)
    • (2006) Langmuir , vol.22 , Issue.14 , pp. 6195-6202
    • Wang, Y.1    Du, X.2
  • 38
    • 46449107010 scopus 로고    scopus 로고
    • Biophysical characterization of nanoparticle endothelial model cell membrane interactions
    • DOI 10.1021/mp700140a
    • C. Peetla, and V. Labhasetwar Biophysical characterization of nanoparticle-endothelial model cell membrane interactions Mol. Pharmaceutics 5 2008 418 429 (Pubitemid 351929826)
    • (2008) Molecular Pharmaceutics , vol.5 , Issue.3 , pp. 418-429
    • Peetla, C.1    Labhasetwar, V.2
  • 39
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38 1986 181 364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 40
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 41
    • 0024997389 scopus 로고
    • Determination of the secondary structure content of proteins in aqueous solutions of their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
    • DOI 10.1021/bi00489a038
    • F. Dousseau, and M. Pezolet Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods Biochemistry 29 1990 8771 8779 (Pubitemid 20302774)
    • (1990) Biochemistry , vol.29 , Issue.37 , pp. 8771-8779
    • Dousseau, F.1    Pezolet, M.2
  • 43
    • 33644767320 scopus 로고    scopus 로고
    • Visualization and characterization of the infrared active amide i vibrations of proteins
    • DOI 10.1021/jp053956a
    • H.S. Chung, and A. Tokmakoff Visualization and characterization of the infrared active amide I vibrations of proteins J. Phys. Chem. B 110 2006 2888 2898 (Pubitemid 43342885)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.6 , pp. 2888-2898
    • Chung, H.S.1    Tokmakoff, A.2
  • 45
    • 0000110539 scopus 로고
    • External infrared reflection absorption spectrometry of monolayer films at the air-water interface
    • R. Mendelsohn, J.W. Brauner, and A. Gericke External infrared reflection absorption spectrometry of monolayer films at the air-water interface Annu. Rev. Phys. Chem. 46 1995 305 334
    • (1995) Annu. Rev. Phys. Chem. , vol.46 , pp. 305-334
    • Mendelsohn, R.1    Brauner, J.W.2    Gericke, A.3
  • 46
    • 0031546355 scopus 로고    scopus 로고
    • Quantitative determination of molecular chain tilt angles in monolayer films at the air/water interface: Infrared reflection/absorption spectroscopy of behenic acid methyl ester
    • C.R. Flach, A. Gericke, and R. Mendelsohn Quantitative determination of molecular chain tilt angles in monolayer films at the air/water interface-infrared reflection/absorption spectroscopy of behenic acid methyl ester J. Phys. Chem. B 101 1997 58 65 (Pubitemid 127611868)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.1 , pp. 58-65
    • Flach, C.R.1    Gericke, A.2    Mendelsohn, R.3
  • 47
    • 0031006190 scopus 로고    scopus 로고
    • Structure and orientation of lung surfactant SP-C and L-α- dipalmitoylphosphatidylcholine in aqueous monolayers
    • A. Gericke, C.R. Flach, and R. Mendelsohn Structure and orientation of lung surfactant SP-C and L-α-dipalmitoylphosphatidylcholine in aqueous monolayers Biophys. J. 73 1997 492 499 (Pubitemid 27274144)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 492-499
    • Gericke, A.1    Flach, C.R.2    Mendelsohn, R.3
  • 48
    • 77449130066 scopus 로고    scopus 로고
    • Infrared reflection-absorption spectroscopy: Principles and applications to lipid-protein interaction in Langmuir films
    • R. Mendelsohn, G. Mao, and C.R. Flach Infrared reflection-absorption spectroscopy: principles and applications to lipid-protein interaction in Langmuir films Biochim. Biophys. Acta 1798 2010 788 800
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 788-800
    • Mendelsohn, R.1    Mao, G.2    Flach, C.R.3
  • 50
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • E. Stengberg, B. Persson, H. Roos, and C. Urbaniczky Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins J. Colloid Interface Sci. 143 1991 513 526
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 513-526
    • Stengberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 51
    • 34547667120 scopus 로고    scopus 로고
    • Recent developments in the molecular imprinting of proteins
    • DOI 10.1016/j.biomaterials.2007.06.017, PII S0142961207004668
    • D.E. Hansen Recent developments in the molecular imprinting of proteins Biomaterials 28 2007 4178 4191 (Pubitemid 47212407)
    • (2007) Biomaterials , vol.28 , Issue.29 , pp. 4178-4191
    • Hansen, D.E.1
  • 52
    • 32344447685 scopus 로고    scopus 로고
    • Protein insertion and patterning of PEG bearing Langmuir monolayers
    • DOI 10.1021/bp050173y
    • H. Dhruv, R. Pepalla, M. Taveras, and D.W. Britt Protein insertion and patterning of PEG bearing Langmuir monolayers Biotechnol. Progr. 22 2006 150 155 (Pubitemid 43221540)
    • (2006) Biotechnology Progress , vol.22 , Issue.1 , pp. 150-155
    • Dhruv, H.1    Pepalla, R.2    Taveras, M.3    Britt, D.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.