메뉴 건너뛰기




Volumn 10, Issue 1, 2017, Pages 134-142

A Facile Two-Step Enzymatic Approach for Conjugating Proteins to Polysaccharide Chitosan at an Electrode Interface

Author keywords

Biofabrication; Chitosan; Nonspecific binding; Transglutaminase

Indexed keywords

CHITOSAN; GLUTAMINE; LYSYLTYROSYLLYSINE; POLYSACCHARIDE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 84995467115     PISSN: 18655025     EISSN: 18655033     Source Type: Journal    
DOI: 10.1007/s12195-016-0472-5     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 85010862380 scopus 로고    scopus 로고
    • Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase
    • Bhokisham, N., et al. Data on biochemical fluxes generated from biofabricated enzyme complexes assembled through engineered tags and microbial transglutaminase. Data Brief 2016. doi:10.1016/j.dib.2016.07.005.
    • (2016) Data Brief
    • Bhokisham, N.1
  • 2
    • 84976407600 scopus 로고    scopus 로고
    • Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase
    • Bhokisham, N., et al. Modular construction of multi-subunit protein complexes using engineered tags and microbial transglutaminase. Metab. Eng. 38:1–9, 2016. doi:10.1016/j.ymben.2016.05.004.
    • (2016) Metab. Eng. , vol.38 , pp. 1-9
    • Bhokisham, N.1
  • 3
    • 0036136270 scopus 로고    scopus 로고
    • Self-assembled monolayers as a tunable platform for biosensor applications
    • Chaki, N. K., and K. Vijayamohanan. Self-assembled monolayers as a tunable platform for biosensor applications. Biosens. Bioelectron. 17:1–12, 2002. doi:10.1016/S0956-5663(01)00277-9.
    • (2002) Biosens. Bioelectron. , vol.17 , pp. 1-12
    • Chaki, N.K.1    Vijayamohanan, K.2
  • 4
    • 59249107210 scopus 로고    scopus 로고
    • Reduction of non-specific protein adsorption using poly(ethylene) glycol (PEG) modified polyacrylate hydrogels in immunoassays for staphylococcal enterotoxin B detection
    • Charles, P., et al. Reduction of non-specific protein adsorption using poly(ethylene) glycol (PEG) modified polyacrylate hydrogels in immunoassays for staphylococcal enterotoxin B detection. Sensors 9:645, 2009.
    • (2009) Sensors , vol.9 , pp. 645
    • Charles, P.1
  • 5
    • 0036346623 scopus 로고    scopus 로고
    • In vitro protein–polysaccharide conjugation: tyrosinase-catalyzed conjugation of gelatin and chitosan
    • Chen, T., H. D. Embree, L.-Q. Wu, and G. F. Payne. In vitro protein–polysaccharide conjugation: tyrosinase-catalyzed conjugation of gelatin and chitosan. Biopolymers 64:292–302, 2002. doi:10.1002/bip.10196.
    • (2002) Biopolymers , vol.64 , pp. 292-302
    • Chen, T.1    Embree, H.D.2    Wu, L.-Q.3    Payne, G.F.4
  • 6
    • 84885029139 scopus 로고    scopus 로고
    • Anti-HER2 antibody and ScFvEGFR-conjugated antifouling magnetic iron oxide nanoparticles for targeting and magnetic resonance imaging of breast cancer
    • Chen, H., et al. Anti-HER2 antibody and ScFvEGFR-conjugated antifouling magnetic iron oxide nanoparticles for targeting and magnetic resonance imaging of breast cancer. Int. J. Nanomed. 8:3781–3794, 2013. doi:10.2147/IJN.S49069.
    • (2013) Int. J. Nanomed. , vol.8 , pp. 3781-3794
    • Chen, H.1
  • 7
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, H. W., and J. E. Coleman. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 245:1613–1625, 1970.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 8
    • 58249088930 scopus 로고    scopus 로고
    • AI-2 biosynthesis module in a magnetic nanofactory alters bacterial response via localized synthesis and delivery
    • Fernandes, R., and W. E. Bentley. AI-2 biosynthesis module in a magnetic nanofactory alters bacterial response via localized synthesis and delivery. Biotechnol. Bioeng. 102:390–399, 2009. doi:10.1002/bit.22078.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 390-399
    • Fernandes, R.1    Bentley, W.E.2
  • 9
    • 77949270750 scopus 로고    scopus 로고
    • Engineered biological nanofactories trigger quorum sensing response in targeted bacteria
    • Fernandes, R., V. Roy, H. C. Wu, and W. E. Bentley. Engineered biological nanofactories trigger quorum sensing response in targeted bacteria. Nat. Nanotechnol. 5:213–217, 2010. doi:10.1038/nnano.2009.457.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 213-217
    • Fernandes, R.1    Roy, V.2    Wu, H.C.3    Bentley, W.E.4
  • 10
    • 0038022646 scopus 로고    scopus 로고
    • Electrochemically induced deposition of a polysaccharide hydrogel onto a patterned surface
    • Fernandes, R., et al. Electrochemically induced deposition of a polysaccharide hydrogel onto a patterned surface. Langmuir 19:4058–4062, 2003. doi:10.1021/la027052h.
    • (2003) Langmuir , vol.19 , pp. 4058-4062
    • Fernandes, R.1
  • 11
    • 77950836054 scopus 로고    scopus 로고
    • Biological nanofactories facilitate spatially selective capture and manipulation of quorum sensing bacteria in a bioMEMS device
    • Fernandes, R., et al. Biological nanofactories facilitate spatially selective capture and manipulation of quorum sensing bacteria in a bioMEMS device. Lab Chip 10:1128–1134, 2010. doi:10.1039/B926846D.
    • (2010) Lab Chip , vol.10 , pp. 1128-1134
    • Fernandes, R.1
  • 12
    • 84905818967 scopus 로고    scopus 로고
    • Electronic modulation of biochemical signal generation. Nat
    • Gordonov, T. et al. Electronic modulation of biochemical signal generation. Nat. Nano 9:605–610, 2014. doi:10.1038/nnano.2014.151. http://www.nature.com/nnano/journal/v9/n8/abs/nnano.2014.151.html#supplementary-information.
    • (2014) Nano 9:605–610
    • Gordonov, T.1
  • 13
    • 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. 14:110–115, 2004. doi:10.1016/j.sbi.2003.12.001.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 14
    • 0035135778 scopus 로고    scopus 로고
    • Poly(l-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption
    • Huang, N.-P., et al. Poly(l-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption. Langmuir 17:489–498, 2001. doi:10.1021/la000736+.
    • (2001) Langmuir , vol.17 , pp. 489-498
    • Huang, N.-P.1
  • 15
    • 84874070976 scopus 로고    scopus 로고
    • Amplified and in situ detection of redox-active metabolite using a biobased redox capacitor
    • Kim, E., T. Gordonov, W. E. Bentley, and G. F. Payne. Amplified and in situ detection of redox-active metabolite using a biobased redox capacitor. Anal. Chem. 85:2102–2108, 2013. doi:10.1021/ac302703y.
    • (2013) Anal. Chem. , vol.85 , pp. 2102-2108
    • Kim, E.1    Gordonov, T.2    Bentley, W.E.3    Payne, G.F.4
  • 16
    • 84961291385 scopus 로고    scopus 로고
    • Chitosan to connect biology to electronics: fabricating the bio-device interface and communicating across this interface
    • Kim, E., et al. Chitosan to connect biology to electronics: fabricating the bio-device interface and communicating across this interface. Polymers 7:1, 2015.
    • (2015) Polymers , vol.7 , pp. 1
    • Kim, E.1
  • 17
    • 33646030628 scopus 로고    scopus 로고
    • Tyrosine-based, “Activatable Pro-Tag”: enzyme-catalyzed protein capture and release
    • Lewandowski, A. T., D. A. Small, T. Chen, G. F. Payne, and W. E. Bentley. Tyrosine-based, “Activatable Pro-Tag”: enzyme-catalyzed protein capture and release. Biotechnol. Bioeng. 93:1207–1215, 2006. doi:10.1002/bit.20840.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 1207-1215
    • Lewandowski, A.T.1    Small, D.A.2    Chen, T.3    Payne, G.F.4    Bentley, W.E.5
  • 18
    • 56249114828 scopus 로고    scopus 로고
    • Towards area-based in vitro metabolic engineering: assembly of Pfs enzyme onto patterned microfabricated chips
    • Lewandowski, A. T., et al. Towards area-based in vitro metabolic engineering: assembly of Pfs enzyme onto patterned microfabricated chips. Biotechnol. Prog. 24:1042–1051, 2008. doi:10.1002/btpr.44.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 1042-1051
    • Lewandowski, A.T.1
  • 19
    • 38449091849 scopus 로고    scopus 로고
    • Protein assembly onto patterned microfabricated devices through enzymatic activation of fusion pro-tag
    • Lewandowski, A. T., et al. Protein assembly onto patterned microfabricated devices through enzymatic activation of fusion pro-tag. Biotechnol. Bioeng. 99:499–507, 2008. doi:10.1002/bit.21580.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 499-507
    • Lewandowski, A.T.1
  • 20
    • 0031057467 scopus 로고    scopus 로고
    • Crosslinking kinetics of the human transglutaminase, factor XIII[A2], acting on fibrin gels and γ-chain peptides
    • Lewis, K. B., D. C. Teller, J. Fry, G. W. Lasser, and P. D. Bishop. Crosslinking kinetics of the human transglutaminase, factor XIII[A2], acting on fibrin gels and γ-chain peptides. Biochemistry 36:995–1002, 1997. doi:10.1021/bi961636z.
    • (1997) Biochemistry , vol.36 , pp. 995-1002
    • Lewis, K.B.1    Teller, D.C.2    Fry, J.3    Lasser, G.W.4    Bishop, P.D.5
  • 21
    • 84860374093 scopus 로고    scopus 로고
    • Biofabrication of stratified biofilm mimics for observation and control of bacterial signaling
    • Luo, X., et al. Biofabrication of stratified biofilm mimics for observation and control of bacterial signaling. Biomaterials 33:5136–5143, 2012. doi:10.1016/j.biomaterials.2012.03.037.
    • (2012) Biomaterials , vol.33 , pp. 5136-5143
    • Luo, X.1
  • 22
    • 77957562650 scopus 로고    scopus 로고
    • Biofabrication: a 21st century manufacturing paradigm
    • Mironov, V., et al. Biofabrication: a 21st century manufacturing paradigm. Biofabrication 1:022001, 2009.
    • (2009) Biofabrication , vol.1 , pp. 022001
    • Mironov, V.1
  • 23
    • 84878415861 scopus 로고    scopus 로고
    • Engineering of a bacterial tyrosinase for improved catalytic efficiency towards d-tyrosine using random and site directed mutagenesis approaches
    • Molloy, S., et al. Engineering of a bacterial tyrosinase for improved catalytic efficiency towards d-tyrosine using random and site directed mutagenesis approaches. Biotechnol. Bioeng. 110:1849–1857, 2013. doi:10.1002/bit.24859.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 1849-1857
    • Molloy, S.1
  • 24
    • 78650301445 scopus 로고    scopus 로고
    • Biomatrices and biomaterials for future developments of bioprinting and biofabrication
    • Nakamura, M., S. Iwanaga, C. Henmi, K. Arai, and Y. Nishiyama. Biomatrices and biomaterials for future developments of bioprinting and biofabrication. Biofabrication 2:014110, 2010.
    • (2010) Biofabrication , vol.2 , pp. 014110
    • Nakamura, M.1    Iwanaga, S.2    Henmi, C.3    Arai, K.4    Nishiyama, Y.5
  • 25
    • 5644242199 scopus 로고    scopus 로고
    • Biofabrication: using biological materials and biocatalysts to construct nanostructured assemblies
    • Wu, L.-Q., and G. F. Payne. Biofabrication: using biological materials and biocatalysts to construct nanostructured assemblies. Trends Biotechnol. 22:593–599, 2004. doi:10.1016/j.tibtech.2004.09.008.
    • (2004) Trends Biotechnol. , vol.22 , pp. 593-599
    • Wu, L.-Q.1    Payne, G.F.2
  • 26
    • 65549152209 scopus 로고    scopus 로고
    • Biofabrication of antibodies and antigens via IgG-binding domain engineered with activatable pentatyrosine pro-tag
    • Wu, H.-C., et al. Biofabrication of antibodies and antigens via IgG-binding domain engineered with activatable pentatyrosine pro-tag. Biotechnol. Bioeng. 103:231–240, 2009. doi:10.1002/bit.22238.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 231-240
    • Wu, H.-C.1
  • 27
    • 60849103099 scopus 로고    scopus 로고
    • Orthogonal enzymatic reactions for the assembly of proteins at electrode addresses
    • Yang, X., X.-W. Shi, Y. Liu, W. E. Bentley, and G. F. Payne. Orthogonal enzymatic reactions for the assembly of proteins at electrode addresses. Langmuir 25:338–344, 2009. doi:10.1021/la802618q.
    • (2009) Langmuir , vol.25 , pp. 338-344
    • Yang, X.1    Shi, X.-W.2    Liu, Y.3    Bentley, W.E.4    Payne, G.F.5
  • 28
    • 79952111219 scopus 로고    scopus 로고
    • Biofabrication to build the biology–device interface
    • Yi, L., et al. Biofabrication to build the biology–device interface. Biofabrication 2:022002, 2010.
    • (2010) Biofabrication , vol.2 , pp. 022002
    • Yi, L.1
  • 29
    • 33750939636 scopus 로고    scopus 로고
    • Chitosan-N-poly(ethylene oxide) brush polymers for reduced nonspecific protein adsorption
    • Zhou, Y., et al. Chitosan-N-poly(ethylene oxide) brush polymers for reduced nonspecific protein adsorption. J. Colloid Interface Sci. 305:62–71, 2007. doi:10.1016/j.jcis.2006.09.058.
    • (2007) J. Colloid Interface Sci. , vol.305 , pp. 62-71
    • Zhou, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.