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Volumn 18, Issue 4, 2007, Pages 312-317

Selection and analysis of solid-binding peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOMATERIALS; HYBRID MATERIALS; NUCLEATION;

EID: 34548530712     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2007.04.008     Document Type: Review
Times cited : (127)

References (57)
  • 2
    • 0030969778 scopus 로고    scopus 로고
    • Metal-recognition by repeating polypeptides
    • Brown S. Metal-recognition by repeating polypeptides. Nat Biotechnol 15 (1997) 269-272
    • (1997) Nat Biotechnol , vol.15 , pp. 269-272
    • Brown, S.1
  • 3
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
    • Whaley S.R., English D.S., Hu E.L., Barbara P.F., and Belcher A.M. Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly. Nature 405 (2000) 665-668
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.R.1    English, D.S.2    Hu, E.L.3    Barbara, P.F.4    Belcher, A.M.5
  • 4
    • 23644436999 scopus 로고    scopus 로고
    • Selecting peptides for use in nanoscale materials using phage displayed combinatorial peptide libraries
    • Kriplani K., and Kay B.K. Selecting peptides for use in nanoscale materials using phage displayed combinatorial peptide libraries. Curr Opin Biotechnol 16 (2005) 470-475
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 470-475
    • Kriplani, K.1    Kay, B.K.2
  • 5
    • 0000967152 scopus 로고    scopus 로고
    • Protein-mediated particle assembly
    • Brown S. Protein-mediated particle assembly. Nano Lett 1 (2001) 391-394
    • (2001) Nano Lett , vol.1 , pp. 391-394
    • Brown, S.1
  • 6
    • 33646023149 scopus 로고    scopus 로고
    • Screening and characterization of affinity peptide tags specific to polystyrene supports for the orientated immobilization of proteins
    • Kumada Y., Tokunaga Y., Imanaka H., Imamura K., Sakiyama T., Katoh S., and Nakanishi K. Screening and characterization of affinity peptide tags specific to polystyrene supports for the orientated immobilization of proteins. Biotechnol Prog 22 (2006) 401-405
    • (2006) Biotechnol Prog , vol.22 , pp. 401-405
    • Kumada, Y.1    Tokunaga, Y.2    Imanaka, H.3    Imamura, K.4    Sakiyama, T.5    Katoh, S.6    Nakanishi, K.7
  • 8
    • 20144363075 scopus 로고    scopus 로고
    • Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer
    • This article describes the isolation and thorough characterization of a linear dodecapeptide binding to the electrically conductive polymer chlorine-doped polypyrrole (PPyCl). The use of a bifunctional peptide consisting of a PPyCl-adhesive moiety and a RGD motif is shown to promote the adhesion of rat cells to the polymer.
    • Sanghvi A.B., Miller K.P., Belcher A.M., and Schmidt C.E. Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer. Nat Mater 4 (2005) 496-502. This article describes the isolation and thorough characterization of a linear dodecapeptide binding to the electrically conductive polymer chlorine-doped polypyrrole (PPyCl). The use of a bifunctional peptide consisting of a PPyCl-adhesive moiety and a RGD motif is shown to promote the adhesion of rat cells to the polymer.
    • (2005) Nat Mater , vol.4 , pp. 496-502
    • Sanghvi, A.B.1    Miller, K.P.2    Belcher, A.M.3    Schmidt, C.E.4
  • 9
    • 33745466002 scopus 로고    scopus 로고
    • Synthesis of gold nanoparticles using multifunctional peptides
    • Slocik J.M., Stone M.O., and Naik R.R. Synthesis of gold nanoparticles using multifunctional peptides. Small 1 (2005) 1048-1052
    • (2005) Small , vol.1 , pp. 1048-1052
    • Slocik, J.M.1    Stone, M.O.2    Naik, R.R.3
  • 12
    • 0034625319 scopus 로고    scopus 로고
    • A genetic analysis of crystal growth
    • Brown S., Sarikaya M., and Johnson E. A genetic analysis of crystal growth. J Mol Biol 299 (2000) 725-735
    • (2000) J Mol Biol , vol.299 , pp. 725-735
    • Brown, S.1    Sarikaya, M.2    Johnson, E.3
  • 13
    • 0002239134 scopus 로고    scopus 로고
    • Silica-precipitating peptides isolated from a combinatorial phage display peptide library
    • Naik R.R., Brott L.L., Clarson S.J., and Stone M.O. Silica-precipitating peptides isolated from a combinatorial phage display peptide library. J Nanosci Nanotechnol 2 (2002) 95-100
    • (2002) J Nanosci Nanotechnol , vol.2 , pp. 95-100
    • Naik, R.R.1    Brott, L.L.2    Clarson, S.J.3    Stone, M.O.4
  • 15
    • 16244366831 scopus 로고    scopus 로고
    • Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1)
    • Sano K., Sasaki H., and Shiba K. Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1). Langmuir 21 (2005) 3090-3095
    • (2005) Langmuir , vol.21 , pp. 3090-3095
    • Sano, K.1    Sasaki, H.2    Shiba, K.3
  • 16
    • 27744453373 scopus 로고    scopus 로고
    • Bioassisted room-temperature immobilization and mineralization of zinc oxide - the structural ordering of ZnO particles into a flower-type morphology
    • Umetsu M., Mizuta M., Tsumoto K., Ohara S., Takami S., Watanabe H., Kumagai I., and Adschiri T. Bioassisted room-temperature immobilization and mineralization of zinc oxide - the structural ordering of ZnO particles into a flower-type morphology. Adv Mater 17 (2005) 2571-2575
    • (2005) Adv Mater , vol.17 , pp. 2571-2575
    • Umetsu, M.1    Mizuta, M.2    Tsumoto, K.3    Ohara, S.4    Takami, S.5    Watanabe, H.6    Kumagai, I.7    Adschiri, T.8
  • 17
    • 33747464755 scopus 로고    scopus 로고
    • Biologically programmed synthesis of bimetallic nanostructures
    • Slocik J.M., and Naik R.R. Biologically programmed synthesis of bimetallic nanostructures. Adv Mater 18 (2006) 1988-1992
    • (2006) Adv Mater , vol.18 , pp. 1988-1992
    • Slocik, J.M.1    Naik, R.R.2
  • 18
    • 27644539424 scopus 로고    scopus 로고
    • Nonequilibrium synthesis and assembly of hybrid inorganic-protein nanostructures using an engineered DNA binding protein
    • A DNA-binding protein engineered with a C-terminal cuprous oxide-binding motif is used to promote the nucleation of a thermodynamically unexpected phase from precursor electrolytes. The resulting cuprous oxide core-protein shell nanoparticles are assembled in a circular geometry using DNA templates. These two operations reproduce key features of natural biomineralizing proteins: non-equilibrium inorganic synthesis and topological control of assembly.
    • Dai H., Choe W.S., Thai C.K., Sarikaya M., Traxler B.A., Baneyx F., and Schwartz D.T. Nonequilibrium synthesis and assembly of hybrid inorganic-protein nanostructures using an engineered DNA binding protein. J Am Chem Soc 127 (2005) 15637-15643. A DNA-binding protein engineered with a C-terminal cuprous oxide-binding motif is used to promote the nucleation of a thermodynamically unexpected phase from precursor electrolytes. The resulting cuprous oxide core-protein shell nanoparticles are assembled in a circular geometry using DNA templates. These two operations reproduce key features of natural biomineralizing proteins: non-equilibrium inorganic synthesis and topological control of assembly.
    • (2005) J Am Chem Soc , vol.127 , pp. 15637-15643
    • Dai, H.1    Choe, W.S.2    Thai, C.K.3    Sarikaya, M.4    Traxler, B.A.5    Baneyx, F.6    Schwartz, D.T.7
  • 21
    • 33744779881 scopus 로고    scopus 로고
    • Phages as templates for hybrid materials and mediators for nanomaterials synthesis
    • An excellent review of how the M13 filamentous bacteriophage is used to select solid-binding peptides, and how it may be engineered to mineralize, assemble and organize inorganic phases.
    • Merzlyak A., and Lee S.-W. Phages as templates for hybrid materials and mediators for nanomaterials synthesis. Curr Opin Chem Biol 10 (2006) 246-252. An excellent review of how the M13 filamentous bacteriophage is used to select solid-binding peptides, and how it may be engineered to mineralize, assemble and organize inorganic phases.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 246-252
    • Merzlyak, A.1    Lee, S.-W.2
  • 22
    • 23144466183 scopus 로고    scopus 로고
    • Programmable assembly of nanoarchitectures using genetically engineered viruses
    • Huang Y., Chiang C.Y., Lee S.-K., Gao L., Hu E.L., De Yoreo J., and Belcher A.M. Programmable assembly of nanoarchitectures using genetically engineered viruses. Nano Lett 5 (2005) 1429-1434
    • (2005) Nano Lett , vol.5 , pp. 1429-1434
    • Huang, Y.1    Chiang, C.Y.2    Lee, S.-K.3    Gao, L.4    Hu, E.L.5    De Yoreo, J.6    Belcher, A.M.7
  • 23
    • 33749351709 scopus 로고    scopus 로고
    • Assembly of multimeric phage nanostructures through leucine zipper interactions
    • Sweeney R.Y., Park E.Y., Iverson B., and Georgiou G. Assembly of multimeric phage nanostructures through leucine zipper interactions. Biotechnol Bioeng 95 (2006) 539-545
    • (2006) Biotechnol Bioeng , vol.95 , pp. 539-545
    • Sweeney, R.Y.1    Park, E.Y.2    Iverson, B.3    Georgiou, G.4
  • 25
    • 32244441753 scopus 로고    scopus 로고
    • Utilization of the pleiotropy of a peptidic aptamer to fabricate heterogeneous nanodot-containing multilayer structures
    • Sano K.-I., Sasaki H., and Shiba K. Utilization of the pleiotropy of a peptidic aptamer to fabricate heterogeneous nanodot-containing multilayer structures. J Am Chem Soc 128 (2006) 1717-1722
    • (2006) J Am Chem Soc , vol.128 , pp. 1717-1722
    • Sano, K.-I.1    Sasaki, H.2    Shiba, K.3
  • 26
    • 33644631590 scopus 로고    scopus 로고
    • Spontaneous assembly of viruses on multilayered polymer surfaces
    • A layer-by-layer assembly technique is used to achieve liquid crystalline ordering of M13 bacteriophages into two-dimensional monolayers. The ability of engineered phage monolayers to bind gold and GaN nanoparticles and to template the mineralization of cobalt is demonstrated.
    • Yoo P.J., Nam K.T., Qi J., Lee S.-K., Park J., Belcher A.M., and Hammond P.T. Spontaneous assembly of viruses on multilayered polymer surfaces. Nat Mater 5 (2006) 234-240. A layer-by-layer assembly technique is used to achieve liquid crystalline ordering of M13 bacteriophages into two-dimensional monolayers. The ability of engineered phage monolayers to bind gold and GaN nanoparticles and to template the mineralization of cobalt is demonstrated.
    • (2006) Nat Mater , vol.5 , pp. 234-240
    • Yoo, P.J.1    Nam, K.T.2    Qi, J.3    Lee, S.-K.4    Park, J.5    Belcher, A.M.6    Hammond, P.T.7
  • 27
    • 33646577838 scopus 로고    scopus 로고
    • Virus-enabled synthesis and assembly of nanowires for lithium ion battery electrodes
    • The first demonstration of the bionanofabrication of a complex functional device. Flexible battery electrodes are constructed by mineralizing cobalt oxide on organized monolayers of an engineered M13 bacteriophage assembled on polyelectrolyte multilayers.
    • Nam K.T., Kim D.W., Yoo P.J., Chiang C.Y., Meethong N., Hammond P.T., Chiang Y.-M., and Belcher A.M. Virus-enabled synthesis and assembly of nanowires for lithium ion battery electrodes. Science 312 (2006) 885-888. The first demonstration of the bionanofabrication of a complex functional device. Flexible battery electrodes are constructed by mineralizing cobalt oxide on organized monolayers of an engineered M13 bacteriophage assembled on polyelectrolyte multilayers.
    • (2006) Science , vol.312 , pp. 885-888
    • Nam, K.T.1    Kim, D.W.2    Yoo, P.J.3    Chiang, C.Y.4    Meethong, N.5    Hammond, P.T.6    Chiang, Y.-M.7    Belcher, A.M.8
  • 28
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions
    • Lu Z., Murray K.S., Van Cleave V., LaVallie E.R., Stahl M.L., and McCoy J.M. Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions. Biotechnology 13 (1995) 366-372
    • (1995) Biotechnology , vol.13 , pp. 366-372
    • Lu, Z.1    Murray, K.S.2    Van Cleave, V.3    LaVallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6
  • 29
    • 2342418578 scopus 로고    scopus 로고
    • Through-mask anodic patterning of copper surfaces and film stability in biological media
    • Dai H., Thai C.K., Sarikaya M., Baneyx F., and Schwartz D.T. Through-mask anodic patterning of copper surfaces and film stability in biological media. Langmuir 20 (2004) 3483-3486
    • (2004) Langmuir , vol.20 , pp. 3483-3486
    • Dai, H.1    Thai, C.K.2    Sarikaya, M.3    Baneyx, F.4    Schwartz, D.T.5
  • 30
    • 33646565661 scopus 로고    scopus 로고
    • Biomolecular recognition of crystal defects: a diffuse selection approach
    • Sinensky A.K., and Belcher A.M. Biomolecular recognition of crystal defects: a diffuse selection approach. Adv Mater 18 (2006) 991-996
    • (2006) Adv Mater , vol.18 , pp. 991-996
    • Sinensky, A.K.1    Belcher, A.M.2
  • 32
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray J.J. The interaction of proteins with solid surfaces. Curr Opin Struct Biol 14 (2004) 110-115
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 33
    • 0036571188 scopus 로고    scopus 로고
    • The interaction of water with solid surfaces: fundamental aspects revisited
    • Henderson M.A. The interaction of water with solid surfaces: fundamental aspects revisited. Surf Sci Rep 46 (2002) 5-308
    • (2002) Surf Sci Rep , vol.46 , pp. 5-308
    • Henderson, M.A.1
  • 34
    • 27844542166 scopus 로고    scopus 로고
    • Enzymatic synthesis of layered titanium phosphates at low temperature and neutral pH by cell-surface display of silicatein-alpha
    • Curnow P., Bessette P.H., Kisailus D., Murr M.M., Daugherty P.S., and Morse D.E. Enzymatic synthesis of layered titanium phosphates at low temperature and neutral pH by cell-surface display of silicatein-alpha. J Am Chem Soc 127 (2005) 15749-15755
    • (2005) J Am Chem Soc , vol.127 , pp. 15749-15755
    • Curnow, P.1    Bessette, P.H.2    Kisailus, D.3    Murr, M.M.4    Daugherty, P.S.5    Morse, D.E.6
  • 35
    • 31544483013 scopus 로고    scopus 로고
    • Cobalt ion mediated self-assembly of genetically engineered bacteriophage for biomimetic Co-Pt hybrid material
    • Lee S.-K., Yun D.S., and Belcher A.M. Cobalt ion mediated self-assembly of genetically engineered bacteriophage for biomimetic Co-Pt hybrid material. Biomacromolecules 7 (2006) 14-17
    • (2006) Biomacromolecules , vol.7 , pp. 14-17
    • Lee, S.-K.1    Yun, D.S.2    Belcher, A.M.3
  • 36
    • 23144436953 scopus 로고    scopus 로고
    • Probing the interface between biomolecules and inorganic materials using yeast surface display and genetic engineering
    • Peelle B.R., Krauland E.M., Wittrup K.D., and Belcher A.M. Probing the interface between biomolecules and inorganic materials using yeast surface display and genetic engineering. Acta Biomater 1 (2005) 145-154
    • (2005) Acta Biomater , vol.1 , pp. 145-154
    • Peelle, B.R.1    Krauland, E.M.2    Wittrup, K.D.3    Belcher, A.M.4
  • 37
  • 38
    • 23144455709 scopus 로고    scopus 로고
    • Design criteria for engineering inorganic material-specific peptides
    • A very interesting study on the first efforts to establish design rules for the rationale design of peptides exhibiting promiscuous or selective solid-binding behavior.
    • Peelle B.R., Krauland E.M., Wittrup K.D., and Belcher A.M. Design criteria for engineering inorganic material-specific peptides. Langmuir 21 (2005) 6929-6933. A very interesting study on the first efforts to establish design rules for the rationale design of peptides exhibiting promiscuous or selective solid-binding behavior.
    • (2005) Langmuir , vol.21 , pp. 6929-6933
    • Peelle, B.R.1    Krauland, E.M.2    Wittrup, K.D.3    Belcher, A.M.4
  • 39
  • 41
    • 9744243512 scopus 로고    scopus 로고
    • Binding specificity of a peptide on semiconductor surfaces
    • Goede K., Busch P., and Grundmann M. Binding specificity of a peptide on semiconductor surfaces. Nano Lett 4 (2004) 2115-2120
    • (2004) Nano Lett , vol.4 , pp. 2115-2120
    • Goede, K.1    Busch, P.2    Grundmann, M.3
  • 42
    • 33644555846 scopus 로고    scopus 로고
    • Identification of peptides for the surface functionalization of perovskite ferroelectrics
    • Reiss B.D., Rai G.-R., Auciello O., Ocola L.E., and Firestone M.A. Identification of peptides for the surface functionalization of perovskite ferroelectrics. Appl Phys Lett 88 (2006) 083901-083903
    • (2006) Appl Phys Lett , vol.88 , pp. 083901-083903
    • Reiss, B.D.1    Rai, G.-R.2    Auciello, O.3    Ocola, L.E.4    Firestone, M.A.5
  • 44
    • 5444244426 scopus 로고    scopus 로고
    • Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability
    • Kase D., Kulp III J.L., Yudasaka M., Evans J.S., Iijima S., and Shiba K. Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability. Langmuir 20 (2004) 8939-8941
    • (2004) Langmuir , vol.20 , pp. 8939-8941
    • Kase, D.1    Kulp III, J.L.2    Yudasaka, M.3    Evans, J.S.4    Iijima, S.5    Shiba, K.6
  • 46
    • 33846512184 scopus 로고    scopus 로고
    • Peptide motifs that recognize differences in polymer-film surfaces
    • Serizawa T., Sawuda T., and Kitayama T. Peptide motifs that recognize differences in polymer-film surfaces. Angew Chem Int Ed 46 (2007) 723-726
    • (2007) Angew Chem Int Ed , vol.46 , pp. 723-726
    • Serizawa, T.1    Sawuda, T.2    Kitayama, T.3
  • 47
    • 20344405234 scopus 로고    scopus 로고
    • Differential adhesion of amino acids to inorganic surfaces
    • A fluorescence microscopy study of the adhesion of homopeptides built from the 20 standard amino acids on nine different materials in three solvents (water, HEPES buffer, and DMSO).
    • Willett R.L., Baldwin K.W., West K.W., and Pfeiffer L.N. Differential adhesion of amino acids to inorganic surfaces. Proc Natl Acad Sci U S A 102 (2005) 7817-7822. A fluorescence microscopy study of the adhesion of homopeptides built from the 20 standard amino acids on nine different materials in three solvents (water, HEPES buffer, and DMSO).
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 7817-7822
    • Willett, R.L.1    Baldwin, K.W.2    West, K.W.3    Pfeiffer, L.N.4
  • 49
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • Sano K., and Shiba K. A hexapeptide motif that electrostatically binds to the surface of titanium. J Am Chem Soc 125 (2003) 14234-14235
    • (2003) J Am Chem Soc , vol.125 , pp. 14234-14235
    • Sano, K.1    Shiba, K.2
  • 50
    • 33748537017 scopus 로고    scopus 로고
    • Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance
    • A detailed comparative study of the adsorption kinetics of a three-repeat gold-binding peptide on its cognate metal using QCM and SPR.
    • Tamerler C., Oren E.E., Duman M., Venkatasubramanian E., and Sarikaya M. Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance. Langmuir 22 (2006) 7712-7718. A detailed comparative study of the adsorption kinetics of a three-repeat gold-binding peptide on its cognate metal using QCM and SPR.
    • (2006) Langmuir , vol.22 , pp. 7712-7718
    • Tamerler, C.1    Oren, E.E.2    Duman, M.3    Venkatasubramanian, E.4    Sarikaya, M.5
  • 51
    • 18644365143 scopus 로고    scopus 로고
    • Molecular dynamics simulations on constraint metal binding peptides
    • Kantarci N., Tamerler C., Sarikaya M., Haliloglu T., and Doruker P. Molecular dynamics simulations on constraint metal binding peptides. Polymer 46 (2005) 4307-4313
    • (2005) Polymer , vol.46 , pp. 4307-4313
    • Kantarci, N.1    Tamerler, C.2    Sarikaya, M.3    Haliloglu, T.4    Doruker, P.5
  • 52
    • 16244386486 scopus 로고    scopus 로고
    • Metal recognition of septapeptides via polypod molecular architecture
    • Oren E.E., Tamerler C., and Sarikaya M. Metal recognition of septapeptides via polypod molecular architecture. Nano Lett 5 (2005) 415-419
    • (2005) Nano Lett , vol.5 , pp. 415-419
    • Oren, E.E.1    Tamerler, C.2    Sarikaya, M.3
  • 53
    • 33646444107 scopus 로고    scopus 로고
    • A solid-state NMR study of the dynamics and interactions of phenylalanine rings in a statherin fragment bound to hydroxyapatite crystals
    • Gibson J.M., Popham J.M., Raghunathan V., Stayton P.S., and Drobny G.P. A solid-state NMR study of the dynamics and interactions of phenylalanine rings in a statherin fragment bound to hydroxyapatite crystals. J Am Chem Soc 128 (2006) 5364-5370
    • (2006) J Am Chem Soc , vol.128 , pp. 5364-5370
    • Gibson, J.M.1    Popham, J.M.2    Raghunathan, V.3    Stayton, P.S.4    Drobny, G.P.5
  • 54
    • 31144458548 scopus 로고    scopus 로고
    • Molecular "tuning" of crystal growth by nacre-associated polypeptides
    • Kim I.W., Darragh M.R., Orme C., and Evans J.S. Molecular "tuning" of crystal growth by nacre-associated polypeptides. Cryst Growth Des 6 (2006) 5-10
    • (2006) Cryst Growth Des , vol.6 , pp. 5-10
    • Kim, I.W.1    Darragh, M.R.2    Orme, C.3    Evans, J.S.4
  • 55
    • 1542345315 scopus 로고    scopus 로고
    • Probing the orientation of surface-immobilized immunoglobin G by time-of-flight secondary ion mass spectroscopy
    • Wang H., Castner D.G., Ratner D.B., and Jiang S. Probing the orientation of surface-immobilized immunoglobin G by time-of-flight secondary ion mass spectroscopy. Langmuir 20 (2004) 1877-1887
    • (2004) Langmuir , vol.20 , pp. 1877-1887
    • Wang, H.1    Castner, D.G.2    Ratner, D.B.3    Jiang, S.4
  • 56
    • 30344443630 scopus 로고    scopus 로고
    • Part III: Surface-enhanced Raman scattering of amino acids and their homodipeptide monolayers deposited onto colloidal gold surface
    • Podstawka E., Ozaki Y., and Proniewicz L.M. Part III: Surface-enhanced Raman scattering of amino acids and their homodipeptide monolayers deposited onto colloidal gold surface. Appl Spectrosc (2005)
    • (2005) Appl Spectrosc
    • Podstawka, E.1    Ozaki, Y.2    Proniewicz, L.M.3
  • 57
    • 29444438030 scopus 로고    scopus 로고
    • Probing the conformational features of a phage display polypeptide sequence directed against single-walled carbon nanohorn surfaces
    • Kulp III J.L., Shiba K., and Evans J.S. Probing the conformational features of a phage display polypeptide sequence directed against single-walled carbon nanohorn surfaces. Langmuir 21 (2005) 11907-11914
    • (2005) Langmuir , vol.21 , pp. 11907-11914
    • Kulp III, J.L.1    Shiba, K.2    Evans, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.