메뉴 건너뛰기




Volumn , Issue , 2013, Pages 417-433

Identification and Application of Polymer-Binding Peptides

Author keywords

Interface; Peptide; Phage display; Surface functionalization; Synthetic polymer

Indexed keywords


EID: 84888713935     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118592403.ch15     Document Type: Chapter
Times cited : (1)

References (115)
  • 1
    • 0029724374 scopus 로고    scopus 로고
    • Surface treatments of polymers for biocompatibility
    • Elbert, D.L., Hubbell, J.A. (1996) Surface treatments of polymers for biocompatibility. Annu. Rev. Mater. Sci. 26: 365-394.
    • (1996) Annu. Rev. Mater. Sci , vol.26 , pp. 365-394
    • Elbert, D.L.1    Hubbell, J.A.2
  • 2
    • 28444452616 scopus 로고    scopus 로고
    • Surface chemistry of biodegradable polymers for drug delivery systems
    • Ha, C.-S., Gardella, J. (2005) Surface chemistry of biodegradable polymers for drug delivery systems. Chem. Rev. 105: 4205-4237.
    • (2005) Chem. Rev , vol.105 , pp. 4205-4237
    • Ha, C.-S.1    Gardella, J.2
  • 3
    • 0031987390 scopus 로고    scopus 로고
    • Structure and reactivity of water at biomaterial surfaces
    • Vogler, E. (1998) Structure and reactivity of water at biomaterial surfaces. Adv. Colloid Interface Sci. 74: 69-186.
    • (1998) Adv. Colloid Interface Sci , vol.74 , pp. 69-186
    • Vogler, E.1
  • 4
    • 0037051037 scopus 로고    scopus 로고
    • Biological surface science
    • Kasemo, B. (2002) Biological surface science. Surf. Sci. 500: 656-677.
    • (2002) Surf. Sci , vol.500 , pp. 656-677
    • Kasemo, B.1
  • 5
    • 4344583135 scopus 로고    scopus 로고
    • Effects of the chemical structure and the surface properties of polymeric biomaterials on their biocompatibility
    • Wang, Y.-X., Robertson, J., Spillman, W., Claus, R. (2004) Effects of the chemical structure and the surface properties of polymeric biomaterials on their biocompatibility. Pharm. Res. 21: 1362-1435.
    • (2004) Pharm. Res , vol.21 , pp. 1362-1435
    • Wang, Y.-X.1    Robertson, J.2    Spillman, W.3    Claus, R.4
  • 6
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228: 1315-1322.
    • (1985) Science , vol.228 , pp. 1315-1322
    • Smith, G.1
  • 7
    • 79960153201 scopus 로고    scopus 로고
    • Specific interactions between synthetic polymers and biologically identified peptides
    • Serizawa, T., Matsuno, H., Sawada, T. (2011) Specific interactions between synthetic polymers and biologically identified peptides. J. Mater. Chem. 21: 10252-10260.
    • (2011) J. Mater. Chem , vol.21 , pp. 10252-10260
    • Serizawa, T.1    Matsuno, H.2    Sawada, T.3
  • 8
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou, G., Stathopoulos, C., Daugherty, P., Nayak, A., Iverson, B., Curtiss, R. (1997) Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat. Biotechnol. 15: 29-63.
    • (1997) Nat. Biotechnol , vol.15 , pp. 29-63
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.3    Nayak, A.4    Iverson, B.5    Curtiss, R.6
  • 10
    • 0033597103 scopus 로고    scopus 로고
    • Instruments for oral disease-intervention strategies: recombinant Lactobacillus casei expressing tetanus toxin fragment C for vaccination or myelin proteins for oral tolerance induction in multiple sclerosis
    • Maassen, C., Laman, J., den Bak-Glashouwer, M., Tielen, F., van Holten-Neelen, J., Hoogteijling, L., Antonissen, C., Leer, R., Pouwels, P., Boersma, W., Shaw, D. (1999) Instruments for oral disease-intervention strategies: recombinant Lactobacillus casei expressing tetanus toxin fragment C for vaccination or myelin proteins for oral tolerance induction in multiple sclerosis. Vaccine 17: 2117-2145.
    • (1999) Vaccine , vol.17 , pp. 2117-2145
    • Maassen, C.1    Laman, J.2    den Bak-Glashouwer, M.3    Tielen, F.4    van Holten-Neelen, J.5    Hoogteijling, L.6    Antonissen, C.7    Leer, R.8    Pouwels, P.9    Boersma, W.10    Shaw, D.11
  • 11
    • 0033970095 scopus 로고    scopus 로고
    • New approaches for cell-specific targeting: identification of cell-selective peptides from combinatorial libraries
    • Brown, K. (2000) New approaches for cell-specific targeting: identification of cell-selective peptides from combinatorial libraries. Curr. Opin. Chem. Biol. 4: 16-37.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 16-37
    • Brown, K.1
  • 12
    • 0036603593 scopus 로고    scopus 로고
    • In vitro selection as a powerful tool for the applied evolution of proteins and peptides
    • Dower, W., Mattheakis, L. (2002) In vitro selection as a powerful tool for the applied evolution of proteins and peptides. Curr. Opin. Chem. Biol. 6: 390-398.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 390-398
    • Dower, W.1    Mattheakis, L.2
  • 13
    • 0035471140 scopus 로고    scopus 로고
    • Protein design and phage display
    • Hoess, R. (2001) Protein design and phage display. Chem. Rev. 101: 3205-3223.
    • (2001) Chem. Rev. , vol.101 , pp. 3205-3223
    • Hoess, R.1
  • 14
    • 39749198122 scopus 로고    scopus 로고
    • Biofunctional polymer nanoparticles for intra-articular targeting and retention in cartilage
    • Rothenfluh, D., Bermudez, H., O'Neil, C., Hubbell, J. (2008) Biofunctional polymer nanoparticles for intra-articular targeting and retention in cartilage. Nat. Mater. 7: 248-254.
    • (2008) Nat. Mater. , vol.7 , pp. 248-254
    • Rothenfluh, D.1    Bermudez, H.2    O'Neil, C.3    Hubbell, J.4
  • 15
    • 2442478726 scopus 로고    scopus 로고
    • A chitin-oligomer binding peptide obtained by screening of a phage display random peptide library and its affinity modulation corresponding to oxidation-reduction state
    • Fukusaki, E., Ogawa, K., Okazawa, A., Kajiyama, S., Kobayashi, A. (2004) A chitin-oligomer binding peptide obtained by screening of a phage display random peptide library and its affinity modulation corresponding to oxidation-reduction state. J. Mol. Catal. B: Enzym. 28: 181-184.
    • (2004) J. Mol. Catal. B: Enzym. , vol.28 , pp. 181-184
    • Fukusaki, E.1    Ogawa, K.2    Okazawa, A.3    Kajiyama, S.4    Kobayashi, A.5
  • 16
    • 34548308800 scopus 로고    scopus 로고
    • Cellulose-binding heptapeptides identified by phage display methods
    • Serizawa, T., Iida, K., Matsuno, H., Kurita, K. (2007) Cellulose-binding heptapeptides identified by phage display methods. Chem. Lett. 36: 988-989.
    • (2007) Chem. Lett. , vol.36 , pp. 988-989
    • Serizawa, T.1    Iida, K.2    Matsuno, H.3    Kurita, K.4
  • 17
    • 0026669435 scopus 로고
    • Engineered iron oxide-adhesion mutants of the Escherichia coli phage lambda receptor
    • Brown, S. (1992) Engineered iron oxide-adhesion mutants of the Escherichia coli phage lambda receptor. Proc. Natl Acad. Sci. USA 89: 8651-8656.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8651-8656
    • Brown, S.1
  • 18
    • 0033831214 scopus 로고    scopus 로고
    • Identification of inorganic crystal-specific sequences using phage display combinatorial library of short peptides: a feasibility study
    • Gaskin, D.J.H., Starck, K., Vulfson, E.N. (2000) Identification of inorganic crystal-specific sequences using phage display combinatorial library of short peptides: a feasibility study. Biotechnol. Lett. 22: 1211-2427.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 1211-2427
    • Gaskin, D.J.H.1    Starck, K.2    Vulfson, E.N.3
  • 20
    • 34547340976 scopus 로고    scopus 로고
    • Interactions of biomolecules with inorganic materials: principles, applications and future prospects
    • Patwardhan, S.V., Patwardhan, G., Perry, C.C. (2007) Interactions of biomolecules with inorganic materials: principles, applications and future prospects. J. Mater. Chem. 17: 2875-5759.
    • (2007) J. Mater. Chem. , vol.17 , pp. 2875-5759
    • Patwardhan, S.V.1    Patwardhan, G.2    Perry, C.C.3
  • 21
    • 34548530712 scopus 로고    scopus 로고
    • Selection and analysis of solid-binding peptides
    • Baneyx, F., Schwartz, D. (2007) Selection and analysis of solid-binding peptides. Curr. Opin. Biotechnol. 18: 312-319.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 312-319
    • Baneyx, F.1    Schwartz, D.2
  • 22
    • 0027199771 scopus 로고
    • Direct selection of antibodies that coordinate metals from semisynthetic combinatorial libraries
    • Barbas, C., Rosenblum, J., Lerner, R. (1993) Direct selection of antibodies that coordinate metals from semisynthetic combinatorial libraries. Proc. Natl Acad. Sci. USA 90: 6385-6394.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6385-6394
    • Barbas, C.1    Rosenblum, J.2    Lerner, R.3
  • 23
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • Sano, K.-I., Shiba, K. (2003) A hexapeptide motif that electrostatically binds to the surface of titanium. J. Am. Chem. Soc. 125: 14234-14239.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14234-14239
    • Sano, K.-I.1    Shiba, K.2
  • 26
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
    • Whaley, S., English, D., Hu, E., Barbara, P., Belcher, A. (2000) Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly. Nature 405: 665-673.
    • (2000) Nature , vol.405 , pp. 665-673
    • Whaley, S.1    English, D.2    Hu, E.3    Barbara, P.4    Belcher, A.5
  • 27
    • 0037012921 scopus 로고    scopus 로고
    • Ordering of quantum dots using genetically engineered viruses
    • Lee, S.-W., Mao, C., Flynn, C., Belcher, A. (2002) Ordering of quantum dots using genetically engineered viruses. Science 296: 892-897.
    • (2002) Science , vol.296 , pp. 892-897
    • Lee, S.-W.1    Mao, C.2    Flynn, C.3    Belcher, A.4
  • 28
    • 27744453373 scopus 로고    scopus 로고
    • Bioassisted room-temperature immobilization and mineralization of zinc oxide - the structural ordering of ZnO nanoparticles into a flower-type morphology
    • Umetsu, M., Mizuta, M., Tsumoto, K., Ohara, S., Takami, S., Watanabe, H., Kumagai, I., Adschiri, T. (2005) Bioassisted room-temperature immobilization and mineralization of zinc oxide - the structural ordering of ZnO nanoparticles into a flower-type morphology. Adv. Mater. 17: 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
  • 30
    • 0030969778 scopus 로고    scopus 로고
    • Metal-recognition by repeating polypeptides
    • Brown, S. (1997) Metal-recognition by repeating polypeptides. Nat. Biotechnol. 15: 269-272.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 269-272
    • Brown, S.1
  • 31
    • 0034625319 scopus 로고    scopus 로고
    • A genetic analysis of crystal growth
    • Brown, S., Sarikaya, M., Johnson, E. (2000) A genetic analysis of crystal growth. J. Mol. Biol. 299: 725-760.
    • (2000) J. Mol. Biol. , vol.299 , pp. 725-760
    • Brown, S.1    Sarikaya, M.2    Johnson, E.3
  • 32
    • 0036879208 scopus 로고    scopus 로고
    • Biomimetic synthesis and patterning of silver nanoparticles
    • Naik, R., Stringer, S., Agarwal, G., Jones, S., Stone, M. (2002) Biomimetic synthesis and patterning of silver nanoparticles. Nat. Mater. 1: 169-172.
    • (2002) Nat. Mater. , vol.1 , pp. 169-172
    • Naik, R.1    Stringer, S.2    Agarwal, G.3    Jones, S.4    Stone, M.5
  • 35
    • 33746544108 scopus 로고    scopus 로고
    • Direct measurements of interactions between polypeptides and carbon nanotubes
    • Li, X., Chen, W., Zhan, Q., Dai, L., Sowards, L., Pender, M., Naik, R. (2006) Direct measurements of interactions between polypeptides and carbon nanotubes. J. Phys. Chem. B 110: 12621-12626.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 12621-12626
    • Li, X.1    Chen, W.2    Zhan, Q.3    Dai, L.4    Sowards, L.5    Pender, M.6    Naik, R.7
  • 36
    • 0142106876 scopus 로고    scopus 로고
    • Binary nanomaterials based on nanocarbons: a case for probing carbon nanohorns' biorecognition properties
    • Zhu, J., Kase, D., Shiba, K., Kasuya, D., Yudasaka, M., Iijima, S. (2003) Binary nanomaterials based on nanocarbons: a case for probing carbon nanohorns' biorecognition properties. Nano Lett. 3: 1033-1036.
    • (2003) Nano Lett. , vol.3 , pp. 1033-1036
    • Zhu, J.1    Kase, D.2    Shiba, K.3    Kasuya, D.4    Yudasaka, M.5    Iijima, S.6
  • 37
    • 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, J., Yudasaka, M., Evans, J., Iijima, S., Shiba, K. (2004) Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability. Langmuir 20: 8939-8941.
    • (2004) Langmuir , vol.20 , pp. 8939-8941
    • Kase, D.1    Kulp, J.2    Yudasaka, M.3    Evans, J.4    Iijima, S.5    Shiba, K.6
  • 38
    • 2442495455 scopus 로고    scopus 로고
    • A screening of phage displayed peptides for the recognition of fullerene (C60)
    • Morita, Y., Ohsugi, T., Iwasa, Y. (2004) A screening of phage displayed peptides for the recognition of fullerene (C60). J. Mol. Catal. B: Enzym. 28: 185-190.
    • (2004) J. Mol. Catal. B: Enzym. , vol.28 , pp. 185-190
    • Morita, Y.1    Ohsugi, T.2    Iwasa, Y.3
  • 39
    • 70349910227 scopus 로고    scopus 로고
    • Affinity-based screening of peptides recognizing assembly states of self-assembling peptide nanomaterials
    • Sawada, T., Takahashi, T., Mihara, H. (2009) Affinity-based screening of peptides recognizing assembly states of self-assembling peptide nanomaterials. J. Am. Chem. Soc. 131: 14434-14441.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14434-14441
    • Sawada, T.1    Takahashi, T.2    Mihara, H.3
  • 40
    • 84858011831 scopus 로고    scopus 로고
    • Dense surface functionalization using peptides that recognize differences in organized structures of self-assembling nanomaterials
    • Mol doi: 10.1039/C1032MB05435C
    • Sawada, T., Mihara, H. (2012) Dense surface functionalization using peptides that recognize differences in organized structures of self-assembling nanomaterials. Mol. BioSyst. doi: 10.1039/C1032MB05435C.
    • (2012) BioSyst
    • Sawada, T.1    Mihara, H.2
  • 41
    • 0028962883 scopus 로고
    • Characterization of phage that bind plastic from phage-displayed random peptide libraries
    • Adey, N., Mataragnon, A., Rider, J., Carter, J., Kay, B. (1995) Characterization of phage that bind plastic from phage-displayed random peptide libraries. Gene 156: 27-31.
    • (1995) Gene , vol.156 , pp. 27-31
    • Adey, N.1    Mataragnon, A.2    Rider, J.3    Carter, J.4    Kay, B.5
  • 42
    • 0001783802 scopus 로고    scopus 로고
    • Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer
    • Berglund, J., Lindbladh, C., Mosbach, K., Nicholls, I.A. (1998) Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer. Anal. Commun. 35: 3-10.
    • (1998) Anal. Commun. , vol.35 , pp. 3-10
    • Berglund, J.1    Lindbladh, C.2    Mosbach, K.3    Nicholls, I.A.4
  • 43
    • 20144363075 scopus 로고    scopus 로고
    • Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer
    • Sanghvi, A., Miller, K., Belcher, A., Schmidt, C. (2005) Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer. Nat. Mater. 4: 496-998.
    • (2005) Nat. Mater. , vol.4 , pp. 496-998
    • Sanghvi, A.1    Miller, K.2    Belcher, A.3    Schmidt, C.4
  • 44
    • 33745466002 scopus 로고    scopus 로고
    • Synthesis of gold nanoparticles using multifunctional peptides
    • Slocik, J., Stone, M., Naik, R. (2005) Synthesis of gold nanoparticles using multifunctional peptides. Small 1: 1048-1100.
    • (2005) Small , vol.1 , pp. 1048-1100
    • Slocik, J.1    Stone, M.2    Naik, R.3
  • 45
    • 16244366831 scopus 로고    scopus 로고
    • Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1)
    • Sano, K.-I., Sasaki, H., Shiba, K. (2005) Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1). Langmuir 21: 3090-3095.
    • (2005) Langmuir , vol.21 , pp. 3090-3095
    • Sano, K.-I.1    Sasaki, H.2    Shiba, K.3
  • 47
    • 33747464755 scopus 로고    scopus 로고
    • Biologically programmed synthesis of bimetallic nanostructures
    • Slocik, J.M., Naik, R.R. (2006) Biologically programmed synthesis of bimetallic nanostructures. Adv. Mater. 18: 1988-1992.
    • (2006) Adv. Mater. , vol.18 , pp. 1988-1992
    • Slocik, J.M.1    Naik, R.R.2
  • 48
    • 16244386486 scopus 로고    scopus 로고
    • Metal recognition of septapeptides via polypod molecular architecture
    • Oren, E., Tamerler, C., Sarikaya, M. (2005) Metal recognition of septapeptides via polypod molecular architecture. Nano Lett. 5: 415-424.
    • (2005) Nano Lett. , vol.5 , pp. 415-424
    • Oren, E.1    Tamerler, C.2    Sarikaya, M.3
  • 49
    • 31544432595 scopus 로고    scopus 로고
    • Peptide-mediated formation of single-wall carbon nanotube composites
    • Pender, M., Sowards, L., Hartgerink, J., Stone, M., Naik, R. (2006) Peptide-mediated formation of single-wall carbon nanotube composites. Nano Lett. 6: 40-44.
    • (2006) Nano Lett. , vol.6 , pp. 40-44
    • Pender, M.1    Sowards, L.2    Hartgerink, J.3    Stone, M.4    Naik, R.5
  • 50
    • 32244441753 scopus 로고    scopus 로고
    • Utilization of the pleiotropy of a peptidic aptamer to fabricate heterogeneous nanodot-containing multilayer nanostructures
    • Sano, K.-I., Sasaki, H., Shiba, K. (2006) Utilization of the pleiotropy of a peptidic aptamer to fabricate heterogeneous nanodot-containing multilayer nanostructures. J. Am. Chem. Soc. 128: 1717-1722.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1717-1722
    • Sano, K.-I.1    Sasaki, H.2    Shiba, K.3
  • 51
    • 33947126568 scopus 로고    scopus 로고
    • Realizing a two-dimensional ordered array of ferritin molecules directly on a solid surface utilizing carbonaceous material affinity peptides
    • Matsui, T., Matsukawa, N., Iwahori, K., Sano, K. I., Shiba, K., Yamashita, I. (2007) Realizing a two-dimensional ordered array of ferritin molecules directly on a solid surface utilizing carbonaceous material affinity peptides. Langmuir 23: 1615-1618.
    • (2007) Langmuir , vol.23 , pp. 1615-1618
    • Matsui, T.1    Matsukawa, N.2    Iwahori, K.3    Sano, K.I.4    Shiba, K.5    Yamashita, I.6
  • 53
    • 32244448431 scopus 로고    scopus 로고
    • Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials
    • K.-I. Sano, K. Ajima, K. Iwahori, M. Yudasaka, S., Iijima, I. Yamashita, K. Shiba (2005) Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials. Small 1: 826-858.
    • (2005) Small , vol.1 , pp. 826-858
    • Sano, K.-I.1    Ajima, K.2    Iwahori, K.3    Yudasaka, M.4    Iijima, S.5    Yamashita, I.6    Shiba, K.7
  • 54
  • 55
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • Kehoe, J., Kay, B. (2005) Filamentous phage display in the new millennium. Chem. Rev. 105: 4056-4072.
    • (2005) Chem. Rev. , vol.105 , pp. 4056-4072
    • Kehoe, J.1    Kay, B.2
  • 56
    • 11044235782 scopus 로고    scopus 로고
    • The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies
    • Menendez, A., Scott, J. (2005) The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies. Anal. Biochem. 336: 145-157.
    • (2005) Anal. Biochem. , vol.336 , pp. 145-157
    • Menendez, A.1    Scott, J.2
  • 57
    • 23144466183 scopus 로고    scopus 로고
    • Programmable assembly of nanoarchitectures using genetically engineered viruses
    • Huang, Y., Chiang, C.-Y., Lee, S.K., Gao, Y., Hu, E.L., Yoreo, J.D., Belcher, A.M. (2005) Programmable assembly of nanoarchitectures using genetically engineered viruses. Nano Lett. 5: 1429-1434.
    • (2005) Nano Lett. , vol.5 , pp. 1429-1434
    • Huang, Y.1    Chiang, C.-Y.2    Lee, S.K.3    Gao, Y.4    Hu, E.L.5    Yoreo, J.D.6    Belcher, A.M.7
  • 58
    • 33748537017 scopus 로고    scopus 로고
    • Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance
    • Tamerler, C., Oren, E., Duman, M., Venkatasubramanian, E., Sarikaya, M. (2006) Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance. Langmuir 22: 7712-7720.
    • (2006) Langmuir , vol.22 , pp. 7712-7720
    • Tamerler, C.1    Oren, E.2    Duman, M.3    Venkatasubramanian, E.4    Sarikaya, M.5
  • 59
    • 34547239512 scopus 로고    scopus 로고
    • Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides
    • Seker, U., Wilson, B., Dincer, S., Kim, I., Oren, E., Evans, J., Tamerler, C., Sarikaya, M. (2007) Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides. Langmuir 23: 7895-7900.
    • (2007) Langmuir , vol.23 , pp. 7895-7900
    • Seker, U.1    Wilson, B.2    Dincer, S.3    Kim, I.4    Oren, E.5    Evans, J.6    Tamerler, C.7    Sarikaya, M.8
  • 60
  • 61
    • 69049104185 scopus 로고    scopus 로고
    • High-affinity peptide-based collagen targeting using synthetic phage mimics: from phage display to dendrimer display
    • Helms, B., Reulen, S., Nijhuis, S., de Graaf-Heuvelmans, P., Merkx, M., Meijer, E. (2009) High-affinity peptide-based collagen targeting using synthetic phage mimics: from phage display to dendrimer display. J. Am. Chem. Soc. 131: 11683-11688.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11683-11688
    • Helms, B.1    Reulen, S.2    Nijhuis, S.3    de Graaf-Heuvelmans, P.4    Merkx, M.5    Meijer, E.6
  • 62
    • 32244448431 scopus 로고    scopus 로고
    • Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials
    • Sano, K.-I., Ajima, K., Iwahori, K., Yudasaka, M., Iijima, S., Yamashita, I., Shiba, K. (2005) Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials. Small 1: 826-858.
    • (2005) Small , vol.1 , pp. 826-858
    • Sano, K.-I.1    Ajima, K.2    Iwahori, K.3    Yudasaka, M.4    Iijima, S.5    Yamashita, I.6    Shiba, K.7
  • 63
    • 64149118082 scopus 로고    scopus 로고
    • Quantitative affinity of genetically engineered repeating polypeptides to inorganic surfaces
    • Seker, U., Wilson, B., Sahin, D., Tamerler, C., Sarikaya, M. (2009) Quantitative affinity of genetically engineered repeating polypeptides to inorganic surfaces. Biomacromolecules 10: 250-257.
    • (2009) Biomacromolecules , vol.10 , pp. 250-257
    • Seker, U.1    Wilson, B.2    Sahin, D.3    Tamerler, C.4    Sarikaya, M.5
  • 64
    • 18644365143 scopus 로고    scopus 로고
    • Molecular dynamics simulations on constraint metal binding peptides
    • Kantarci, N., Tamerler, C., Sarikaya, M., Haliloglu, T., Doruker, P. (2005) Molecular dynamics simulations on constraint metal binding peptides. Polymer 46: 4307-4313.
    • (2005) Polymer , vol.46 , pp. 4307-4313
    • Kantarci, N.1    Tamerler, C.2    Sarikaya, M.3    Haliloglu, T.4    Doruker, P.5
  • 66
    • 0001943070 scopus 로고
    • Living and highly syndiotactic polymerization of methyl methacrylate and other methacrylates by tert-butyllithiumtrialkylaluminium in toluene
    • Kitayama, T., Shinozaki, T., Sakamoto, T., Yamamoto, M., Hatada, K. (1989) Living and highly syndiotactic polymerization of methyl methacrylate and other methacrylates by tert-butyllithiumtrialkylaluminium in toluene. Makromol. Chem. 15: 167-185.
    • (1989) Makromol. Chem. , vol.15 , pp. 167-185
    • Kitayama, T.1    Shinozaki, T.2    Sakamoto, T.3    Yamamoto, M.4    Hatada, K.5
  • 69
    • 35948972439 scopus 로고    scopus 로고
    • Highly specific affinities of short peptides against synthetic polymers
    • Serizawa, T., Sawada, T., Matsuno, H. (2007) Highly specific affinities of short peptides against synthetic polymers. Langmuir 23: 11127-11133.
    • (2007) Langmuir , vol.23 , pp. 11127-11133
    • Serizawa, T.1    Sawada, T.2    Matsuno, H.3
  • 70
    • 49249089456 scopus 로고    scopus 로고
    • Directional affinity of short peptides for synthetic polymers
    • Date, T., Tanaka, K., Nagamura, T., Serizawa, T. (2008) Directional affinity of short peptides for synthetic polymers. Chem. Mater. 20: 4536-4538.
    • (2008) Chem. Mater. , vol.20 , pp. 4536-4538
    • Date, T.1    Tanaka, K.2    Nagamura, T.3    Serizawa, T.4
  • 71
    • 33846512184 scopus 로고    scopus 로고
    • Peptide motifs that recognize differences in polymer-film surfaces
    • Serizawa, T., Sawada, T., Kitayama, T. (2007) Peptide motifs that recognize differences in polymer-film surfaces. Angew. Chem., Int. Ed. 46: 723-729.
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 723-729
    • Serizawa, T.1    Sawada, T.2    Kitayama, T.3
  • 72
    • 0033337423 scopus 로고    scopus 로고
    • Wettability and microstructure of polymer surfaces: stereochemical and conformational aspects
    • Tretinnikov, O.N. (1999) Wettability and microstructure of polymer surfaces: stereochemical and conformational aspects. J. Adhes. Sci. Technol. 13: 1085-1102.
    • (1999) J. Adhes. Sci. Technol. , vol.13 , pp. 1085-1102
    • Tretinnikov, O.N.1
  • 73
    • 84859564360 scopus 로고    scopus 로고
    • Surface modification of stereoregular and stereocomplex poly(methyl methacrylate) films with biologically identified peptides
    • Date, T., Yoshino, S., Matsuno, H., Serizawa, T. (2012) Surface modification of stereoregular and stereocomplex poly(methyl methacrylate) films with biologically identified peptides. Polym. J. 44: 366-369.
    • (2012) Polym. J. , vol.44 , pp. 366-369
    • Date, T.1    Yoshino, S.2    Matsuno, H.3    Serizawa, T.4
  • 74
    • 15044344886 scopus 로고    scopus 로고
    • Bulk and surface modifications of polylactide
    • Wang, S., Cui, W., Bei, J. (2005) Bulk and surface modifications of polylactide. Anal. Bioanal. Chem. 381: 547-556.
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 547-556
    • Wang, S.1    Cui, W.2    Bei, J.3
  • 75
    • 33750250642 scopus 로고    scopus 로고
    • Biodegradable polymeric scaffolds. Improvements in bone tissue engineering through controlled drug delivery
    • Holland, T.A., Mikos, A.G. (2006) Biodegradable polymeric scaffolds. Improvements in bone tissue engineering through controlled drug delivery. Adv. Biochem. Eng./Biotechnol. 102: 161-185.
    • (2006) Adv. Biochem. Eng./Biotechnol. , vol.102 , pp. 161-185
    • Holland, T.A.1    Mikos, A.G.2
  • 76
    • 47349131273 scopus 로고    scopus 로고
    • Biological selection of peptides for poly(l-lactide) substrates
    • Matsuno, H., Sekine, J., Yajima, H., Serizawa, T. (2008) Biological selection of peptides for poly(l-lactide) substrates. Langmuir 24: 6399-6403.
    • (2008) Langmuir , vol.24 , pp. 6399-6403
    • Matsuno, H.1    Sekine, J.2    Yajima, H.3    Serizawa, T.4
  • 77
    • 34547523062 scopus 로고    scopus 로고
    • Isolation of peptides that can recognize syndiotactic polystyrene
    • Serizawa, T., Techawanitchai, P., Matsuno, H. (2007) Isolation of peptides that can recognize syndiotactic polystyrene. ChemBioChem 8: 989-993.
    • (2007) ChemBioChem , vol.8 , pp. 989-993
    • Serizawa, T.1    Techawanitchai, P.2    Matsuno, H.3
  • 78
    • 0032187109 scopus 로고    scopus 로고
    • The presence of nanopores in mesophase of syndiotactic polystyrene estimated from gas sorption behaviour
    • Tsutsui, K., Tsujita, Y., Yoshimizu, H. (1998) The presence of nanopores in mesophase of syndiotactic polystyrene estimated from gas sorption behaviour. Polymer: 5177-5182.
    • (1998) Polymer , pp. 5177-5182
    • Tsutsui, K.1    Tsujita, Y.2    Yoshimizu, H.3
  • 79
    • 0033152241 scopus 로고    scopus 로고
    • The structural organization in syndiotactic polystyrene film induced by toluene vapour sorption
    • Tsutsui, K., Katsumata, T., Yamamoto, Y., Fukatsu, H., Yoshimizu, H., Kinoshita, T., Tsujita, Y. (1999) The structural organization in syndiotactic polystyrene film induced by toluene vapour sorption. Polymer 40: 3815-3819.
    • (1999) Polymer , vol.40 , pp. 3815-3819
    • Tsutsui, K.1    Katsumata, T.2    Yamamoto, Y.3    Fukatsu, H.4    Yoshimizu, H.5    Kinoshita, T.6    Tsujita, Y.7
  • 80
    • 16344368277 scopus 로고    scopus 로고
    • Structure and properties of the mesophase of syndiotactic polystyrene. V: preferential sorption performance of the mesophase for aromatic hydrocarbons
    • Yamamoto, Y., Nakai, Y., Katsumata, T., Tsutsui, K., Tsujita, Y., Yoshimizu, H., Okamoto, S. (2005) Structure and properties of the mesophase of syndiotactic polystyrene. V: preferential sorption performance of the mesophase for aromatic hydrocarbons. J. Mol. Struct. 739: 13-30.
    • (2005) J. Mol. Struct. , vol.739 , pp. 13-30
    • Yamamoto, Y.1    Nakai, Y.2    Katsumata, T.3    Tsutsui, K.4    Tsujita, Y.5    Yoshimizu, H.6    Okamoto, S.7
  • 82
    • 0029483704 scopus 로고
    • Polymer photovoltaic cells: enhanced efficiencies via a network of internal donor-acceptor heterojunctions
    • Yu, G., Gao, J., Hummelen, J., Wudl, F., Heeger, A. (1995) Polymer photovoltaic cells: enhanced efficiencies via a network of internal donor-acceptor heterojunctions. Science 270: 1789-1791.
    • (1995) Science , vol.270 , pp. 1789-1791
    • Yu, G.1    Gao, J.2    Hummelen, J.3    Wudl, F.4    Heeger, A.5
  • 83
    • 54949116202 scopus 로고    scopus 로고
    • Fluorescent conjugated polyelectrolytes for biomacromolecule detection
    • Feng, F., He, F., An, L., Wang, S., Li, Y., Zhu, D. (2008) Fluorescent conjugated polyelectrolytes for biomacromolecule detection. Adv. Mater. 20: 2959-2969.
    • (2008) Adv. Mater. , vol.20 , pp. 2959-2969
    • Feng, F.1    He, F.2    An, L.3    Wang, S.4    Li, Y.5    Zhu, D.6
  • 84
    • 78650404445 scopus 로고    scopus 로고
    • Biological identification of peptides that specifically bind to poly(phenylene vinylene) surfaces: recognition of the branched or linear structure of the conjugated polymer
    • Ejima, H., Matsuno, H., Serizawa, T. (2010) Biological identification of peptides that specifically bind to poly(phenylene vinylene) surfaces: recognition of the branched or linear structure of the conjugated polymer. Langmuir 26: 17278-17285.
    • (2010) Langmuir , vol.26 , pp. 17278-17285
    • Ejima, H.1    Matsuno, H.2    Serizawa, T.3
  • 85
    • 17044444652 scopus 로고    scopus 로고
    • Photomechanics: directed bending of a polymer film by light
    • Yu, Y., Nakano, M., Ikeda, T. (2003) Photomechanics: directed bending of a polymer film by light. Nature 425: 145.
    • (2003) Nature , vol.425 , pp. 145
    • Yu, Y.1    Nakano, M.2    Ikeda, T.3
  • 86
    • 31444454427 scopus 로고    scopus 로고
    • Azobenzene-tethered T7 promoter for efficient photoregulation of transcription
    • Liu, M., Asanuma, H., Komiyama, M. (2006) Azobenzene-tethered T7 promoter for efficient photoregulation of transcription. J. Am. Chem. Soc. 128: 1009-1015.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1009-1015
    • Liu, M.1    Asanuma, H.2    Komiyama, M.3
  • 88
    • 34547576746 scopus 로고    scopus 로고
    • Temperatureresponsive cell culture surfaces for regenerative medicine with cell sheet engineering
    • Yamato, M., Akiyama, Y., Kobayashi, J., Yang, J., Kikuchi, A., Okano, T. (2007) Temperatureresponsive cell culture surfaces for regenerative medicine with cell sheet engineering. Prog. Polym. Sci. 32: 1123-1133.
    • (2007) Prog. Polym. Sci. , vol.32 , pp. 1123-1133
    • Yamato, M.1    Akiyama, Y.2    Kobayashi, J.3    Yang, J.4    Kikuchi, A.5    Okano, T.6
  • 89
    • 0142119372 scopus 로고    scopus 로고
    • Design of environment-sensitive supramolecular assemblies for intracellular drug delivery: polymeric micelles that are responsive to intracellular pH change
    • Bae, Y., Fukushima, S., Harada, A., Kataoka, K. (2003) Design of environment-sensitive supramolecular assemblies for intracellular drug delivery: polymeric micelles that are responsive to intracellular pH change. Angew. Chem., Int. Ed. 42: 4640-4643.
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 4640-4643
    • Bae, Y.1    Fukushima, S.2    Harada, A.3    Kataoka, K.4
  • 90
    • 11944269634 scopus 로고
    • A polymer gel with electrically driven motility
    • Osada, Y., Okuzaki, H., Hori, H. (1992) A polymer gel with electrically driven motility. Nature 355: 242-244.
    • (1992) Nature , vol.355 , pp. 242-244
    • Osada, Y.1    Okuzaki, H.2    Hori, H.3
  • 91
    • 0033600290 scopus 로고    scopus 로고
    • A reversibly antigen-responsive hydrogel
    • Miyata, T., Asami, N., Uragami, T. (1999) A reversibly antigen-responsive hydrogel. Nature 399: 766-775.
    • (1999) Nature , vol.399 , pp. 766-775
    • Miyata, T.1    Asami, N.2    Uragami, T.3
  • 93
    • 57749185245 scopus 로고    scopus 로고
    • Directional BMP-2 for functionalization of titanium surfaces
    • Kashiwagi, K., Tsuji, T., Shiba, K. (2009) Directional BMP-2 for functionalization of titanium surfaces. Biomaterials 30: 1166-1175.
    • (2009) Biomaterials , vol.30 , pp. 1166-1175
    • Kashiwagi, K.1    Tsuji, T.2    Shiba, K.3
  • 99
    • 23144466183 scopus 로고    scopus 로고
    • Programmable assembly of nanoarchitectures using genetically encoded viruses
    • Huang, Y., Chiang, C.-Y., Lee, S., Gao, Y., Hu, E., De Yoreo, J., Belcher, A. (2005) Programmable assembly of nanoarchitectures using genetically encoded viruses. Nano Lett. 5: 1429-1434.
    • (2005) Nano Lett. , vol.5 , pp. 1429-1434
    • Huang, Y.1    Chiang, C.-Y.2    Lee, S.3    Gao, Y.4    Hu, E.5    De Yoreo, J.6    Belcher, A.7
  • 100
    • 78651445334 scopus 로고    scopus 로고
    • Binding analysis of peptides that recognize preferentially cis-azobenzene groups of synthetic polymers
    • Chen, J., Serizawa, T., Komiyama, M. (2011) Binding analysis of peptides that recognize preferentially cis-azobenzene groups of synthetic polymers. J. Pept. Sci. 17: 163-171.
    • (2011) J. Pept. Sci. , vol.17 , pp. 163-171
    • Chen, J.1    Serizawa, T.2    Komiyama, M.3
  • 101
    • 79954583378 scopus 로고    scopus 로고
    • Recognition of photoresponsive polymer targets by protein fused with cis-form azobenzene-binding peptide
    • Chen, J., Serizawa, T., Komiyama, M. (2011) Recognition of photoresponsive polymer targets by protein fused with cis-form azobenzene-binding peptide. Chem. Lett. 40: 482-483.
    • (2011) Chem. Lett. , vol.40 , pp. 482-483
    • Chen, J.1    Serizawa, T.2    Komiyama, M.3
  • 102
    • 10844280763 scopus 로고    scopus 로고
    • Functional gold nanoparticles for recognition and catalysis
    • Pasquato, L., Pengo, P., Scrimin, P. (2004) Functional gold nanoparticles for recognition and catalysis. J. Mater. Chem. 14: 3481-3487.
    • (2004) J. Mater. Chem , vol.14 , pp. 3481-3487
    • Pasquato, L.1    Pengo, P.2    Scrimin, P.3
  • 103
    • 36948998624 scopus 로고    scopus 로고
    • Interparticle coupling effect on the surface plasmon resonance of gold nanoparticles: from theory to applications
    • Ghosh, S., Pal, T. (2007) Interparticle coupling effect on the surface plasmon resonance of gold nanoparticles: from theory to applications. Chem. Rev. 107: 4797-4862.
    • (2007) Chem. Rev. , vol.107 , pp. 4797-4862
    • Ghosh, S.1    Pal, T.2
  • 104
    • 56349166047 scopus 로고    scopus 로고
    • Applications of nanoparticles in biology
    • De, M., Ghosh, P.S., Rotello, V.M. (2008) Applications of nanoparticles in biology. Adv. Mater. 20: 4225-4241.
    • (2008) Adv. Mater. , vol.20 , pp. 4225-4241
    • De, M.1    Ghosh, P.S.2    Rotello, V.M.3
  • 105
    • 74949134551 scopus 로고    scopus 로고
    • Novel synthetic route to peptide-capped gold nanoparticles
    • Serizawa, T., Hirai, Y., Aizawa, M. (2009) Novel synthetic route to peptide-capped gold nanoparticles. Langmuir 25: 12229-12234.
    • (2009) Langmuir , vol.25 , pp. 12229-12234
    • Serizawa, T.1    Hirai, Y.2    Aizawa, M.3
  • 106
    • 0345979435 scopus 로고    scopus 로고
    • Formation and structure of self-assembled monolayers
    • Ulman, A. (1996) Formation and structure of self-assembled monolayers. Chem. Rev. 96: 1533-1554.
    • (1996) Chem. Rev , vol.96 , pp. 1533-1554
    • Ulman, A.1
  • 107
    • 26844451426 scopus 로고    scopus 로고
    • Engineering silicon oxide surfaces using selfassembled monolayers
    • Onclin, S., Ravoo, B.J., Reinhoudt, D.N. (2005) Engineering silicon oxide surfaces using selfassembled monolayers. Angew. Chem. Int. Ed. 44: 6282-6304.
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 6282-6304
    • Onclin, S.1    Ravoo, B.J.2    Reinhoudt, D.N.3
  • 108
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • Love, J.C., Estroff, L.A., Kriebel, J.K., Nuzzo, R.G., Whitesides, G.M. (2005) Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 105: 1103-1169.
    • (2005) Chem. Rev , vol.105 , pp. 1103-1169
    • Love, J.C.1    Estroff, L.A.2    Kriebel, J.K.3    Nuzzo, R.G.4    Whitesides, G.M.5
  • 109
    • 79957976588 scopus 로고    scopus 로고
    • Polymer-binding peptides for the noncovalent modification of polymer surfaces: effects of peptide density on the subsequent immobilization of functional proteins
    • Date, T., Sekine, J., Matsuno, H., Serizawa, T. (2011) Polymer-binding peptides for the noncovalent modification of polymer surfaces: effects of peptide density on the subsequent immobilization of functional proteins. ACS Appl. Mater. Interfaces 3: 351-360.
    • (2011) ACS Appl. Mater. Interfaces , vol.3 , pp. 351-360
    • Date, T.1    Sekine, J.2    Matsuno, H.3    Serizawa, T.4
  • 110
    • 79251584337 scopus 로고    scopus 로고
    • Peptide-based switching of polymer fluorescence in aqueous phase
    • Ejima, H., Kikuchi, H., Matsuno, H., Yajima, H., Serizawa, T. (2010) Peptide-based switching of polymer fluorescence in aqueous phase. Chem. Mater. 22: 6032-6034.
    • (2010) Chem. Mater , vol.22 , pp. 6032-6034
    • Ejima, H.1    Kikuchi, H.2    Matsuno, H.3    Yajima, H.4    Serizawa, T.5
  • 111
    • 0009883254 scopus 로고
    • Method for enhancing the sensitivity of fluorescent chemosensors: energy migration in conjugated polymers
    • Zhou, Q., Swager, T.M. (1995) Method for enhancing the sensitivity of fluorescent chemosensors: energy migration in conjugated polymers. J. Am. Chem. Soc. 117: 7017-7018.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7017-7018
    • Zhou, Q.1    Swager, T.M.2
  • 112
    • 0033607186 scopus 로고    scopus 로고
    • Highly sensitive biological and chemical sensors based on reversible fluorescence quenching in a conjugated polymer
    • Chen, L., McBranch, D., Wang, H., Helgeson, R., Wudl, F., Whitten, D. (1999) Highly sensitive biological and chemical sensors based on reversible fluorescence quenching in a conjugated polymer. Proc. Natl Acad. Sci. USA 96: 12287-12292.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12287-12292
    • Chen, L.1    McBranch, D.2    Wang, H.3    Helgeson, R.4    Wudl, F.5    Whitten, D.6
  • 113
    • 34248332079 scopus 로고    scopus 로고
    • Chemical sensors based on amplifying fluorescent conjugated polymers
    • Thomas, S., Joly, G., Swager, T. (2007) Chemical sensors based on amplifying fluorescent conjugated polymers. Chem. Rev. 107: 1339-1386.
    • (2007) Chem. Rev. , vol.107 , pp. 1339-1386
    • Thomas, S.1    Joly, G.2    Swager, T.3
  • 114
    • 34548639390 scopus 로고    scopus 로고
    • Conjugated polymers as optical probes for protein interactions and protein conformations
    • Herland, A., Inganäs, O. (2007) Conjugated polymers as optical probes for protein interactions and protein conformations. Macromol. Rapid Commun. 28: 1703-1713.
    • (2007) Macromol. Rapid Commun. , vol.28 , pp. 1703-1713
    • Herland, A.1    Inganäs, O.2
  • 115
    • 0030848621 scopus 로고    scopus 로고
    • Fuzzy nanoassemblies: toward layered polymeric multicomposites
    • Decher, G. (1997) Fuzzy nanoassemblies: toward layered polymeric multicomposites. Science 277: 1232-1237.
    • (1997) Science , vol.277 , pp. 1232-1237
    • Decher, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.