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Volumn 161, Issue 2, 2012, Pages 164-174

Designing the nanoparticle-biomolecule interface for "targeting and therapeutic delivery"

Author keywords

Bio nano interface; Engineered interface; Nanoparticle targeting; Receptor recognition

Indexed keywords

ACTIVE TARGETING; BIOLOGICAL FLUIDS; CELLULAR MACHINERY; ENDOGENOUS PROCESS; IN-SITU; IN-VIVO; INTEGRATION OF KNOWLEDGE; LIVING ORGANISMS; NANO-SCALE MATERIALS; NANOARCHITECTURES; NANOSCALE INTERACTIONS; PHYSIO-CHEMICAL; RECEPTOR RECOGNITION; SELECTIVE TRANSPORT; SPECIFIC SITES; SPECIFIC SURFACE; SUB-CELLULAR; SURFACE ADSORPTION; SURROUNDING ENVIRONMENT; THERAPEUTIC DELIVERY; TRANSPORT MECHANISM;

EID: 84862646346     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2012.04.009     Document Type: Review
Times cited : (339)

References (136)
  • 1
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • S.D. Conner, S.L. Schmid, Regulated portals of entry into the cell, Nature 422 (2003) 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 2
    • 7044235459 scopus 로고    scopus 로고
    • Intracellular trafficking pathways and drug delivery: Fluorescence imaging of living and fixed cells
    • P. Watson, A.T. Jones, D.J. Stephens, Intracellular trafficking pathways and drug delivery: fluorescence imaging of living and fixed cells, Adv. Drug Deliv. Rev. 57 (2005) 43-61.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 43-61
    • Watson, P.1    Jones, A.T.2    Stephens, D.J.3
  • 7
    • 79952302512 scopus 로고    scopus 로고
    • Physical-chemical aspects of protein corona: Relevance to in vitro and in vivo biological impacts of nanoparticles
    • M.P. Monopoli, D. Walczyk, A. Campbell, G. Elia, I. Lynch, F. Baldelli Bombelli, K.A. Dawson, Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles, J. Am. Chem. Soc. 133 (2011) 2525-2534.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525-2534
    • Monopoli, M.P.1    Walczyk, D.2    Campbell, A.3    Elia, G.4    Lynch, I.5    Baldelli Bombelli, F.6    Dawson, K.A.7
  • 10
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • M. Lundqvist, J. Stigler, G. Elia, I. Lynch, T. Cedervall, K.A. Dawson, Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts, Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 14265-14270.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 13
    • 80052269121 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of mineral nanoparticles derived from human body fluids and analyzed by liquid chromatography-tandem mass spectrometry
    • J. Martel, D. Young, A. Young, C.-Y. Wu, C.-D. Chen, J.-S. Yu, J.D. Young, Comprehensive proteomic analysis of mineral nanoparticles derived from human body fluids and analyzed by liquid chromatography-tandem mass spectrometry, Anal. Biochem. 418 (2011) 111-125.
    • (2011) Anal. Biochem. , vol.418 , pp. 111-125
    • Martel, J.1    Young, D.2    Young, A.3    Wu, C.-Y.4    Chen, C.-D.5    Yu, J.-S.6    Young, J.D.7
  • 14
    • 24144452456 scopus 로고    scopus 로고
    • Adsorption kinetics of plasma proteins on solid lipid nanoparticles for drug targeting
    • T.M. Goppert, R.H. Muller, Adsorption kinetics of plasma proteins on solid lipid nanoparticles for drug targeting, Int. J. Pharm. 302 (2005) 172-186.
    • (2005) Int. J. Pharm. , vol.302 , pp. 172-186
    • Goppert, T.M.1    Muller, R.H.2
  • 16
    • 70249136214 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions: What does the cell see?
    • I. Lynch, A. Salvati, K.A. Dawson, Protein-nanoparticle interactions: what does the cell see? Nat. Nano 4 (2009) 546-547.
    • (2009) Nat. Nano , vol.4 , pp. 546-547
    • Lynch, I.1    Salvati, A.2    Dawson, K.A.3
  • 18
    • 65149104167 scopus 로고    scopus 로고
    • Immobilization of anti-transferrin on nano-gold and its immune recognition of transferrin
    • P.H. Yang, W. Wei, H.H. Cai, J. Feng, J.Y. Cai, Immobilization of anti-transferrin on nano-gold and its immune recognition of transferrin, Spectrosc. Spectr. Anal. 29 (2009) 1398-1401.
    • (2009) Spectrosc. Spectr. Anal. , vol.29 , pp. 1398-1401
    • Yang, P.H.1    Wei, W.2    Cai, H.H.3    Feng, J.4    Cai, J.Y.5
  • 19
    • 77952745203 scopus 로고    scopus 로고
    • Active and passive tumor targeting of a novel poorly soluble cyclin dependent kinase inhibitor, JNJ-7706621
    • F. Danhier, B. Ucakar, N. Magotteaux, M.E. Brewster, V. Préat, Active and passive tumor targeting of a novel poorly soluble cyclin dependent kinase inhibitor, JNJ-7706621, Int. J. Pharm. 392 (2010) 20-28.
    • (2010) Int. J. Pharm. , vol.392 , pp. 20-28
    • Danhier, F.1    Ucakar, B.2    Magotteaux, N.3    Brewster, M.E.4    Préat, V.5
  • 20
    • 77952584926 scopus 로고    scopus 로고
    • Reducing non-specific binding and uptake of nanoparticles and improving cell targeting with an antifouling PEO-b-P[gamma]MPS copolymer coating
    • H. Chen, L. Wang, J. Yeh, X. Wu, Z. Cao, Y.A. Wang, M. Zhang, L. Yang, H. Mao, Reducing non-specific binding and uptake of nanoparticles and improving cell targeting with an antifouling PEO-b-P[gamma]MPS copolymer coating, Biomaterials 31 (2010) 5397-5407.
    • (2010) Biomaterials , vol.31 , pp. 5397-5407
    • Chen, H.1    Wang, L.2    Yeh, J.3    Wu, X.4    Cao, Z.5    Wang, Y.A.6    Zhang, M.7    Yang, L.8    Mao, H.9
  • 21
    • 76149117212 scopus 로고    scopus 로고
    • Nuclear targeting of gold nanoparticles in cancer cells induces DNA damage, causing cytokinesis arrest and apoptosis
    • B. Kang, M.A. Mackey, M.A. El-Sayed, Nuclear targeting of gold nanoparticles in cancer cells induces DNA damage, causing cytokinesis arrest and apoptosis, J. Am. Chem. Soc. 132 (2010) 1517-1519.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1517-1519
    • Kang, B.1    Mackey, M.A.2    El-Sayed, M.A.3
  • 23
    • 33750690503 scopus 로고    scopus 로고
    • In vitro assessment of transferrin-conjugated liposomes as drug delivery systems for inhalation therapy of lung cancer
    • S. Anabousi, U. Bakowsky, M. Schneider, H. Huwer, C.-M. Lehr, C. Ehrhardt, In vitro assessment of transferrin-conjugated liposomes as drug delivery systems for inhalation therapy of lung cancer, Eur. J. Pharm. Sci. 29 (2006) 367-374.
    • (2006) Eur. J. Pharm. Sci. , vol.29 , pp. 367-374
    • Anabousi, S.1    Bakowsky, U.2    Schneider, M.3    Huwer, H.4    Lehr, C.-M.5    Ehrhardt, C.6
  • 24
    • 59649102668 scopus 로고    scopus 로고
    • Transferrin- and transferrin-receptor-antibody-modified nanoparticles enable drug delivery across the blood-brain barrier (BBB)
    • K. Ulbrich, T. Hekmatara, E. Herbert, J. Kreuter, Transferrin- and transferrin-receptor-antibody-modified nanoparticles enable drug delivery across the blood-brain barrier (BBB), Eur. J. Pharm. Biopharm. 71 (2009) 251-256.
    • (2009) Eur. J. Pharm. Biopharm. , vol.71 , pp. 251-256
    • Ulbrich, K.1    Hekmatara, T.2    Herbert, E.3    Kreuter, J.4
  • 25
  • 26
    • 75749088450 scopus 로고    scopus 로고
    • Mechanism of active targeting in solid tumors with transferrin-containing gold nanoparticles
    • C.H.J. Choi, C.A. Alabi, P. Webster, M.E. Davis, Mechanism of active targeting in solid tumors with transferrin-containing gold nanoparticles, Proc. Natl. Acad. Sci. 107 (2010) 1235-1240.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 1235-1240
    • Choi, C.H.J.1    Alabi, C.A.2    Webster, P.3    Davis, M.E.4
  • 27
    • 78650538843 scopus 로고    scopus 로고
    • Targeting the insulin receptor: Nanoparticles for drug delivery across the blood-brain barrier (BBB)
    • K. Ulbrich, T. Knobloch, J. Kreuter, Targeting the insulin receptor: nanoparticles for drug delivery across the blood-brain barrier (BBB), J. Drug Target. 19 (2011) 125-132.
    • (2011) J. Drug Target. , vol.19 , pp. 125-132
    • Ulbrich, K.1    Knobloch, T.2    Kreuter, J.3
  • 30
    • 77953028922 scopus 로고    scopus 로고
    • EGFP-EGF1 protein-conjugated PEG-PLA nanoparticles for tissue factor targeted drug delivery
    • H. Mei, W. Shi, Z. Pang, H. Wang, W. Lu, X. Jiang, J. Deng, T. Guo, Y. Hu, EGFP-EGF1 protein-conjugated PEG-PLA nanoparticles for tissue factor targeted drug delivery, Biomaterials. 31 (2010) 5619-5626.
    • (2010) Biomaterials , vol.31 , pp. 5619-5626
    • Mei, H.1    Shi, W.2    Pang, Z.3    Wang, H.4    Lu, W.5    Jiang, X.6    Deng, J.7    Guo, T.8    Hu, Y.9
  • 32
    • 29244489232 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-targeted immunoliposomes significantly enhance the efficacy of multiple anticancer drugs in vivo
    • C. Mamot, D.C. Drummond, C.O. Noble, V. Kallab, Z. Guo, K. Hong, D.B. Kirpotin, J.W. Park, Epidermal growth factor receptor-targeted immunoliposomes significantly enhance the efficacy of multiple anticancer drugs in vivo, Cancer Res. 65 (2005) 11631-11638.
    • (2005) Cancer Res. , vol.65 , pp. 11631-11638
    • Mamot, C.1    Drummond, D.C.2    Noble, C.O.3    Kallab, V.4    Guo, Z.5    Hong, K.6    Kirpotin, D.B.7    Park, J.W.8
  • 33
    • 68749092564 scopus 로고    scopus 로고
    • Targeted epidermal growth factor receptor nanoparticle bioconjugates for breast cancer therapy
    • S. Acharya, F. Dilnawaz, S.K. Sahoo, Targeted epidermal growth factor receptor nanoparticle bioconjugates for breast cancer therapy, Biomaterials 30 (2009) 5737-5750.
    • (2009) Biomaterials , vol.30 , pp. 5737-5750
    • Acharya, S.1    Dilnawaz, F.2    Sahoo, S.K.3
  • 36
    • 77949762340 scopus 로고    scopus 로고
    • Targeting of drugs and nanoparticles to tumors
    • E. Ruoslahti, S.N. Bhatia, M.J. Sailor, Targeting of drugs and nanoparticles to tumors, J. Cell Biol. 188 (2010) 759-768.
    • (2010) J. Cell Biol. , vol.188 , pp. 759-768
    • Ruoslahti, E.1    Bhatia, S.N.2    Sailor, M.J.3
  • 37
    • 77955562994 scopus 로고    scopus 로고
    • The complex role of multivalency in nanoparticles targeting the transferrin receptor for cancer therapies
    • J. Wang, S.M. Tian, R.A. Petros, M.E. Napier, J.M. DeSimone, The complex role of multivalency in nanoparticles targeting the transferrin receptor for cancer therapies, J. Am. Chem. Soc. 132 (2010) 11306-11313.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11306-11313
    • Wang, J.1    Tian, S.M.2    Petros, R.A.3    Napier, M.E.4    DeSimone, J.M.5
  • 38
    • 0025094141 scopus 로고
    • The role of transferrin in the mechanism of cellular iron uptake
    • K. Thorstensen, I. Romslo, The role of transferrin in the mechanism of cellular iron uptake, Biochem. J. 271 (1990) 1-10.
    • (1990) Biochem. J. , vol.271 , pp. 1-10
    • Thorstensen, K.1    Romslo, I.2
  • 39
    • 33750019824 scopus 로고    scopus 로고
    • The transferrin receptor part II: Targeted delivery of therapeutic agents into cancer cells
    • T.R. Daniels, T. Delgado, G. Helguera, M.L. Penichet, The transferrin receptor part II: targeted delivery of therapeutic agents into cancer cells, Clin. Immunol. 121 (2006) 159-176.
    • (2006) Clin. Immunol. , vol.121 , pp. 159-176
    • Daniels, T.R.1    Delgado, T.2    Helguera, G.3    Penichet, M.L.4
  • 40
    • 0033652083 scopus 로고    scopus 로고
    • Improvement of MRI probes to allow efficient detection of gene expression
    • D. Hogemann, L. Josephson, R. Weissleder, J.P. Basilion, Improvement of MRI probes to allow efficient detection of gene expression, Bioconjug. Chem. 11 (2000) 941-946.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 941-946
    • Hogemann, D.1    Josephson, L.2    Weissleder, R.3    Basilion, J.P.4
  • 41
    • 34547302844 scopus 로고    scopus 로고
    • Elucidating the mechanism of cellular uptake and removal of protein-coated gold nanoparticles of different sizes and shapes
    • B.D. Chithrani, W.C.W. Chan, Elucidating the mechanism of cellular uptake and removal of protein-coated gold nanoparticles of different sizes and shapes, Nano Lett. 7 (2007) 1542-1550.
    • (2007) Nano Lett. , vol.7 , pp. 1542-1550
    • Chithrani, B.D.1    Chan, W.C.W.2
  • 42
    • 84855268371 scopus 로고    scopus 로고
    • Role of cell cycle on the cellular uptake and dilution of nanoparticles in a cell population
    • J.A. Kim, C. Aberg, A. Salvati, K.A. Dawson, Role of cell cycle on the cellular uptake and dilution of nanoparticles in a cell population, Nat. Nano 7 (2012) 62-68.
    • (2012) Nat. Nano , vol.7 , pp. 62-68
    • Kim, J.A.1    Aberg, C.2    Salvati, A.3    Dawson, K.A.4
  • 43
    • 82255163011 scopus 로고    scopus 로고
    • Experimental and theoretical comparison of intracellular import of polymeric nanoparticles and small molecules: Toward models of uptake kinetics
    • A. Salvati, C. Ãberg, T. dos Santos, J. Varela, P. Pinto, I. Lynch, K.A. Dawson, Experimental and theoretical comparison of intracellular import of polymeric nanoparticles and small molecules: toward models of uptake kinetics, Nanomedicine 7 (2011) 818-826.
    • (2011) Nanomedicine , vol.7 , pp. 818-826
    • Salvati, A.1    Ãberg, C.2    Dos Santos, T.3    Varela, J.4    Pinto, P.5    Lynch, I.6    Dawson, K.A.7
  • 45
    • 78149366902 scopus 로고    scopus 로고
    • Serum heat inactivation affects protein corona composition and nanoparticle uptake
    • A. Lesniak, A. Campbell, M.P. Monopoli, I. Lynch, A. Salvati, K.A. Dawson, Serum heat inactivation affects protein corona composition and nanoparticle uptake, Biomaterials 31 (2010) 9511-9518.
    • (2010) Biomaterials , vol.31 , pp. 9511-9518
    • Lesniak, A.1    Campbell, A.2    Monopoli, M.P.3    Lynch, I.4    Salvati, A.5    Dawson, K.A.6
  • 46
    • 0022858683 scopus 로고
    • A new concept for macromolecular therapeutics in cancer chemotherapy: Mechanism of tumoritropic accumulation of proteins and the antitumor agent SMANCS
    • Y. Matsumura, H. Maeda, A new concept for macromolecular therapeutics in cancer chemotherapy: mechanism of tumoritropic accumulation of proteins and the antitumor agent SMANCS, Cancer Res. 46 (1986) 6387-6392.
    • (1986) Cancer Res. , vol.46 , pp. 6387-6392
    • Matsumura, Y.1    Maeda, H.2
  • 47
    • 77954313055 scopus 로고    scopus 로고
    • Stealth nanoparticles: High density but sheddable PEG is a key for tumor targeting
    • S.D. Li, L. Huang, Stealth nanoparticles: High density but sheddable PEG is a key for tumor targeting, J. Control. Release. 145 (2010) 178-181.
    • (2010) J. Control. Release , vol.145 , pp. 178-181
    • Li, S.D.1    Huang, L.2
  • 48
    • 2542491949 scopus 로고    scopus 로고
    • Ethylene glycol monolayer protected nanoparticles: Synthesis, characterization, and interactions with biological molecules
    • M. Zheng, Z.G. Li, X.Y. Huang, Ethylene glycol monolayer protected nanoparticles: synthesis, characterization, and interactions with biological molecules, Langmuir 20 (2004) 4226-4235.
    • (2004) Langmuir , vol.20 , pp. 4226-4235
    • Zheng, M.1    Li, Z.G.2    Huang, X.Y.3
  • 49
    • 77951908020 scopus 로고    scopus 로고
    • Influence of polyethyleneglycol modification on phagocytic uptake of polymeric nanoparticles mediated by immunoglobulin G and complement activation
    • A. Yang, W. Liu, Z. Li, L. Jiang, H. Xu, X. Yang, Influence of polyethyleneglycol modification on phagocytic uptake of polymeric nanoparticles mediated by immunoglobulin G and complement activation, J. Nanosci. Nanotechnol. 10 (2010) 622-628.
    • (2010) J. Nanosci. Nanotechnol. , vol.10 , pp. 622-628
    • Yang, A.1    Liu, W.2    Li, Z.3    Jiang, L.4    Xu, H.5    Yang, X.6
  • 50
    • 28844488494 scopus 로고    scopus 로고
    • Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles
    • D.E. Owens, N.A. Peppas, Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles, Int. J. Pharm. 307 (2006) 93-102.
    • (2006) Int. J. Pharm. , vol.307 , pp. 93-102
    • Owens, D.E.1    Peppas, N.A.2
  • 51
    • 33646384586 scopus 로고    scopus 로고
    • Parameters influencing the stealthiness of colloidal drug delivery systems
    • A. Vonarbourg, C. Passirani, P. Saulnier, J.P. Benoit, Parameters influencing the stealthiness of colloidal drug delivery systems, Biomaterials 27 (2006) 4356-4373.
    • (2006) Biomaterials , vol.27 , pp. 4356-4373
    • Vonarbourg, A.1    Passirani, C.2    Saulnier, P.3    Benoit, J.P.4
  • 52
    • 78649538085 scopus 로고    scopus 로고
    • Distinct polymer architecture mediates switching of complement activation pathways at the nanosphere-serum interface: Implications for stealth nanoparticle engineering
    • I. Hamad, O. Al-Hanbali, A.C. Hunter, K.J. Rutt, T.L. Andresen, S.M. Moghimi, Distinct polymer architecture mediates switching of complement activation pathways at the nanosphere-serum interface: implications for stealth nanoparticle engineering, ACS Nano 4 (2010) 6629-6638.
    • (2010) ACS Nano , vol.4 , pp. 6629-6638
    • Hamad, I.1    Al-Hanbali, O.2    Hunter, A.C.3    Rutt, K.J.4    Andresen, T.L.5    Moghimi, S.M.6
  • 54
    • 34848918210 scopus 로고    scopus 로고
    • Impact of tumor-specific targeting on the biodistribution and efficacy of siRNA nanoparticles measured by multimodality in vivo imaging
    • D.W. Bartlett, H. Su, I.J. Hildebrandt, W.A. Weber, M.E. Davis, Impact of tumor-specific targeting on the biodistribution and efficacy of siRNA nanoparticles measured by multimodality in vivo imaging, Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 15549-15554.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15549-15554
    • Bartlett, D.W.1    Su, H.2    Hildebrandt, I.J.3    Weber, W.A.4    Davis, M.E.5
  • 55
    • 34547910668 scopus 로고    scopus 로고
    • Time-dependent changes in opsonin amount associated on nanoparticles alter their hepatic uptake characteristics
    • S. Nagayama, K.-i. Ogawara, Y. Fukuoka, K. Higaki, T. Kimura, Time-dependent changes in opsonin amount associated on nanoparticles alter their hepatic uptake characteristics, Int. J. Pharm. 342 (2007) 215-221.
    • (2007) Int. J. Pharm. , vol.342 , pp. 215-221
    • Nagayama, S.1    Ogawara, K.-I.2    Fukuoka, Y.3    Higaki, K.4    Kimura, T.5
  • 56
    • 35349010059 scopus 로고    scopus 로고
    • The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century
    • I. Lynch, T. Cedervall, M. Lundqvist, C. Cabaleiro-Lago, S. Linse, K.A. Dawson, The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century, Adv. Colloid Interface Sci. 134-35 (2007) 167-174.
    • (2007) Adv. Colloid Interface Sci. , vol.134-135 , pp. 167-174
    • Lynch, I.1    Cedervall, T.2    Lundqvist, M.3    Cabaleiro-Lago, C.4    Linse, S.5    Dawson, K.A.6
  • 57
    • 51049108389 scopus 로고    scopus 로고
    • Preclinical studies to understand nanoparticle interaction with the immune system and its potential effects on nanoparticle biodistribution
    • M.A. Dobrovolskaia, P. Aggarwal, J.B. Hall, S.E. McNeil, Preclinical studies to understand nanoparticle interaction with the immune system and its potential effects on nanoparticle biodistribution, Mol. Pharm. 5 (2008) 487-495.
    • (2008) Mol. Pharm. , vol.5 , pp. 487-495
    • Dobrovolskaia, M.A.1    Aggarwal, P.2    Hall, J.B.3    McNeil, S.E.4
  • 58
    • 78650606928 scopus 로고    scopus 로고
    • Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation
    • Z.J. Deng, M. Liang, M. Monteiro, I. Toth, R.F. Minchin, Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation, Nat. Nano 6 (2011) 39-44.
    • (2011) Nat. Nano , vol.6 , pp. 39-44
    • Deng, Z.J.1    Liang, M.2    Monteiro, M.3    Toth, I.4    Minchin, R.F.5
  • 59
    • 78650606296 scopus 로고    scopus 로고
    • Nanobiotechnology: Nanoparticle coronas take shape
    • M.P. Monopoli, F.B. Bombelli, K.A. Dawson, Nanobiotechnology: nanoparticle coronas take shape, Nat. Nano 6 (2011) 11-12.
    • (2011) Nat. Nano , vol.6 , pp. 11-12
    • Monopoli, M.P.1    Bombelli, F.B.2    Dawson, K.A.3
  • 60
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
    • P. Roach, D. Farrar, C.C. Perry, Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry, J. Am. Chem. Soc. 128 (2006) 3939-3945.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 61
    • 62749100589 scopus 로고    scopus 로고
    • Cytochrome c on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity
    • W. Shang, J.H. Nuffer, V.A. Muniz-Papandrea, W. Colon, R.W. Siegel, J.S. Dordick, Cytochrome c on silica nanoparticles: influence of nanoparticle size on protein structure, stability, and activity, Small 5 (2009) 470-476.
    • (2009) Small , vol.5 , pp. 470-476
    • Shang, W.1    Nuffer, J.H.2    Muniz-Papandrea, V.A.3    Colon, W.4    Siegel, R.W.5    Dordick, J.S.6
  • 62
    • 0032485414 scopus 로고    scopus 로고
    • Analysis of plasma protein adsorption on polymeric nanoparticles with different surface characteristics
    • M. Luck, B.R. Paulke, W. Schroder, T. Blunk, R.H. Muller, Analysis of plasma protein adsorption on polymeric nanoparticles with different surface characteristics, J. Biomed. Mater. Res. 39 (1998) 478-485.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 478-485
    • Luck, M.1    Paulke, B.R.2    Schroder, W.3    Blunk, T.4    Muller, R.H.5
  • 63
    • 0033970172 scopus 로고    scopus 로고
    • Nanoparticles with decreasing surface hydrophobicities: Influence on plasma protein adsorption
    • A. Gessner, R. Waicz, A. Lieske, B.R. Paulke, K. Mader, R.H. Muller, Nanoparticles with decreasing surface hydrophobicities: influence on plasma protein adsorption, Int. J. Pharm. 196 (2000) 245-249.
    • (2000) Int. J. Pharm. , vol.196 , pp. 245-249
    • Gessner, A.1    Waicz, R.2    Lieske, A.3    Paulke, B.R.4    Mader, K.5    Muller, R.H.6
  • 64
    • 1842832660 scopus 로고    scopus 로고
    • Influence of surface charge density on protein adsorption on polymeric nanoparticles: Analysis by two-dimensional electrophoresis
    • A. Gessner, A. Lieske, B.R. Paulke, R.H. Muller, Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis, Eur. J. Pharm. Biopharm. 54 (2002) 165-170.
    • (2002) Eur. J. Pharm. Biopharm. , vol.54 , pp. 165-170
    • Gessner, A.1    Lieske, A.2    Paulke, B.R.3    Muller, R.H.4
  • 66
    • 0022078121 scopus 로고
    • Adsorption of proteins out of plasma and solutions in narrow spaces
    • L. Vroman, A.L. Adams, Adsorption of proteins out of plasma and solutions in narrow spaces, J. Colloid Interface Sci. 111 (1986) 391-402.
    • (1986) J. Colloid Interface Sci. , vol.111 , pp. 391-402
    • Vroman, L.1    Adams, A.L.2
  • 68
    • 6344294066 scopus 로고    scopus 로고
    • Influence of the surface properties on nanoparticle-mediated transport of drugs to the brain
    • J. Kreuter, Influence of the surface properties on nanoparticle-mediated transport of drugs to the brain, J. Nanosci. Nanotechnol. 4 (2004) 484-488.
    • (2004) J. Nanosci. Nanotechnol. , vol.4 , pp. 484-488
    • Kreuter, J.1
  • 69
    • 9644272479 scopus 로고    scopus 로고
    • Pre-coating with serum albumin reduces receptor-mediated hepatic disposition of polystyrene nanosphere: Implications for rational design of nanoparticles
    • K.-i. Ogawara, K. Furumoto, S. Nagayama, K. Minato, K. Higaki, T. Kai, T. Kimura, Pre-coating with serum albumin reduces receptor-mediated hepatic disposition of polystyrene nanosphere: implications for rational design of nanoparticles, J. Control. Release 100 (2004) 451-455.
    • (2004) J. Control. Release , vol.100 , pp. 451-455
    • Ogawara, K.-I.1    Furumoto, K.2    Nagayama, S.3    Minato, K.4    Higaki, K.5    Kai, T.6    Kimura, T.7
  • 70
    • 0035210289 scopus 로고    scopus 로고
    • Interactions of liposomes with cells in vitro and in vivo: Opsonins and receptors
    • T. Ishida, H. Harashima, H. Kiwada, Interactions of liposomes with cells in vitro and in vivo: opsonins and receptors, Curr. Drug Metab. 2 (2001) 397-409.
    • (2001) Curr. Drug Metab. , vol.2 , pp. 397-409
    • Ishida, T.1    Harashima, H.2    Kiwada, H.3
  • 71
    • 0036085551 scopus 로고    scopus 로고
    • Experimental and calculated parameters on particle phagocytosis by alveolar macrophages
    • P. Camner, M. Lundborg, L. Lastbom, P. Gerde, N. Gross, C. Jarstrand, Experimental and calculated parameters on particle phagocytosis by alveolar macrophages, J. Appl. Physiol. 92 (2002) 2608-2616.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2608-2616
    • Camner, P.1    Lundborg, M.2    Lastbom, L.3    Gerde, P.4    Gross, N.5    Jarstrand, C.6
  • 73
    • 56449122424 scopus 로고    scopus 로고
    • The influence of protein adsorption on nanoparticle association with cultured endothelial cells
    • M.S. Ehrenberg, A.E. Friedman, J.N. Finkelstein, G. Oberdörster, J.L. McGrath, The influence of protein adsorption on nanoparticle association with cultured endothelial cells, Biomaterials 30 (2009) 603-610.
    • (2009) Biomaterials , vol.30 , pp. 603-610
    • Ehrenberg, M.S.1    Friedman, A.E.2    Finkelstein, J.N.3    Oberdörster, G.4    McGrath, J.L.5
  • 76
    • 33846312153 scopus 로고    scopus 로고
    • The binding avidity of a nanoparticle-based multivalent targeted drug delivery platform
    • S. Hong, P.R. Leroueil, I.J. Majoros, B.G. Orr, J.R. Baker, M.M.B. Holl, The binding avidity of a nanoparticle-based multivalent targeted drug delivery platform, Chem. Biol. 14 (2007) 107-115.
    • (2007) Chem. Biol. , vol.14 , pp. 107-115
    • Hong, S.1    Leroueil, P.R.2    Majoros, I.J.3    Orr, B.G.4    Baker, J.R.5    Holl, M.M.B.6
  • 77
    • 0347694971 scopus 로고    scopus 로고
    • On the nature of the multivalency effect: A thermodynamic model
    • P.I. Kitov, D.R. Bundle, On the nature of the multivalency effect: a thermodynamic model, J. Am. Chem. Soc. 125 (2003) 16271-16284.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16271-16284
    • Kitov, P.I.1    Bundle, D.R.2
  • 78
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • M. Mammen, S.K. Choi, G.M. Whitesides, Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors, Angew. Chem. Int. Edit. 37 (1998) 2755-2794.
    • (1998) Angew. Chem. Int. Edit. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 79
    • 70349100806 scopus 로고    scopus 로고
    • Theory of free energy and entropy in noncovalent binding
    • H.X. Zhou, M.K. Gilson, Theory of free energy and entropy in noncovalent binding, Chem. Rev. 109 (2009) 4092-4107.
    • (2009) Chem. Rev. , vol.109 , pp. 4092-4107
    • Zhou, H.X.1    Gilson, M.K.2
  • 80
    • 0034868445 scopus 로고    scopus 로고
    • NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
    • M.J. Stone, NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding, Acc. Chem. Res. 34 (2001) 379-388.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 379-388
    • Stone, M.J.1
  • 81
    • 67649361537 scopus 로고    scopus 로고
    • Bioanalytical applications of biomolecule-functionalized nanometer-sized doped silica particles
    • D. Knopp, D.P. Tang, R. Niessner, Bioanalytical applications of biomolecule-functionalized nanometer-sized doped silica particles, Anal. Chim. Acta 647 (2009) 14-30.
    • (2009) Anal. Chim. Acta , vol.647 , pp. 14-30
    • Knopp, D.1    Tang, D.P.2    Niessner, R.3
  • 82
    • 0034291676 scopus 로고    scopus 로고
    • Functional polymer microspheres
    • H. Kawaguchi, Functional polymer microspheres, Prog. Polym. Sci. 25 (2000) 1171-1210.
    • (2000) Prog. Polym. Sci. , vol.25 , pp. 1171-1210
    • Kawaguchi, H.1
  • 83
    • 0037307878 scopus 로고    scopus 로고
    • Plasmon resonant particles for biological detection
    • D.A. Schultz, Plasmon resonant particles for biological detection, Curr. Opin. Biotechnol. 14 (2003) 13-22.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 13-22
    • Schultz, D.A.1
  • 85
    • 77950207533 scopus 로고    scopus 로고
    • Surface modification, functionalization and bioconjugation of colloidal inorganic nanoparticles
    • R.A. Sperling, W.J. Parak, Surface modification, functionalization and bioconjugation of colloidal inorganic nanoparticles, Philos. Trans. R. Soc. A-Math. Phys. Eng. Sci. 368 (2010) 1333-1383.
    • (2010) Philos. Trans. R. Soc. A-Math. Phys. Eng. Sci. , vol.368 , pp. 1333-1383
    • Sperling, R.A.1    Parak, W.J.2
  • 86
    • 45149100245 scopus 로고    scopus 로고
    • Covalently dye-linked, surface-controlled, and bioconjugated organically modified silica nanoparticles as targeted probes for optical imaging
    • R. Kumar, I. Roy, T.Y. Hulchanskyy, L.N. Goswami, A.C. Bonoiu, E.J. Bergey, K.M. Tramposch, A. Maitra, P.N. Prasad, Covalently dye-linked, surface-controlled, and bioconjugated organically modified silica nanoparticles as targeted probes for optical imaging, ACS Nano 2 (2008) 449-456.
    • (2008) ACS Nano , vol.2 , pp. 449-456
    • Kumar, R.1    Roy, I.2    Hulchanskyy, T.Y.3    Goswami, L.N.4    Bonoiu, A.C.5    Bergey, E.J.6    Tramposch, K.M.7    Maitra, A.8    Prasad, P.N.9
  • 87
    • 58149481283 scopus 로고    scopus 로고
    • A facilemethod to synthesize carboxyl-functionalized magnetic polystyrene nanospheres
    • N.N. Guan, C. Liu, D.J. Sun, J. Xu, A facilemethod to synthesize carboxyl-functionalized magnetic polystyrene nanospheres, Colloids Surf. A-Physicochem. Eng. Aspects 335 (2009) 174-180.
    • (2009) Colloids Surf. A-Physicochem. Eng. Aspects , vol.335 , pp. 174-180
    • Guan, N.N.1    Liu, C.2    Sun, D.J.3    Xu, J.4
  • 88
    • 33645525556 scopus 로고    scopus 로고
    • Synthesis and characterization of paramagnetic microparticles through emulsion-templated free radical polymerization
    • H. Shang, W.S. Chang, S. Kan, S.A. Majetich, G.U. Lee, Synthesis and characterization of paramagnetic microparticles through emulsion-templated free radical polymerization, Langmuir 22 (2006) 2516-2522.
    • (2006) Langmuir , vol.22 , pp. 2516-2522
    • Shang, H.1    Chang, W.S.2    Kan, S.3    Majetich, S.A.4    Lee, G.U.5
  • 89
    • 58049220470 scopus 로고    scopus 로고
    • PEGylated gold nanoparticles conjugated to monoclonal F19 antibodies as targeted labeling agents for human pancreatic carcinoma tissue
    • W. Eck, G. Craig, A. Sigdel, G. Ritter, L.J. Old, L. Tang, M.F. Brennan, P.J. Allen, M.D. Mason, PEGylated gold nanoparticles conjugated to monoclonal F19 antibodies as targeted labeling agents for human pancreatic carcinoma tissue, ACS Nano 2 (2008) 2263-2272.
    • (2008) ACS Nano , vol.2 , pp. 2263-2272
    • Eck, W.1    Craig, G.2    Sigdel, A.3    Ritter, G.4    Old, L.J.5    Tang, L.6    Brennan, M.F.7    Allen, P.J.8    Mason, M.D.9
  • 90
    • 33847216926 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability
    • D.X. Li, Q. He, Y. Cui, L. Duan, J.B. Li, Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability, Biochem. Biophys. Res. Commun. 355 (2007) 488-493.
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 488-493
    • Li, D.X.1    He, Q.2    Cui, Y.3    Duan, L.4    Li, J.B.5
  • 91
    • 33748581355 scopus 로고    scopus 로고
    • Electroactive silica nanoparticles for biological labeling13
    • J. Wang, G. Liu, Y. Lin, Electroactive silica nanoparticles for biological labeling13, Small 2 (2006) 1134-1138.
    • (2006) Small , vol.2 , pp. 1134-1138
    • Wang, J.1    Liu, G.2    Lin, Y.3
  • 92
    • 0033166986 scopus 로고    scopus 로고
    • Grafting protein ligand monolayers onto the surface of microparticles for probing the accessibility of cell surface receptors
    • A. Frey, B. Meckelein, M.A. Schmidt, Grafting protein ligand monolayers onto the surface of microparticles for probing the accessibility of cell surface receptors, Bioconjug. Chem. 10 (1999) 562-571.
    • (1999) Bioconjug. Chem. , vol.10 , pp. 562-571
    • Frey, A.1    Meckelein, B.2    Schmidt, M.A.3
  • 93
    • 56749170938 scopus 로고    scopus 로고
    • Bio-molecule-conjugated fluorescent organically modified silica nanoparticles as optical probes for cancer cell imaging
    • J. Qian, X. Li, M. Wei, X.W. Gao, Z.P. Xu, S.L. He, Bio-molecule- conjugated fluorescent organically modified silica nanoparticles as optical probes for cancer cell imaging, Opt. Express 16 (2008) 19568-19578.
    • (2008) Opt. Express , vol.16 , pp. 19568-19578
    • Qian, J.1    Li, X.2    Wei, M.3    Gao, X.W.4    Xu, Z.P.5    He, S.L.6
  • 94
    • 34347335596 scopus 로고    scopus 로고
    • Multifunctional nanoparticles possessing magnetic, long-lived fluorescence and bio-affinity properties for time-resolved fluorescence cell imaging
    • J. Wu, Z.Q. Ye, G.L. Wang, J.L. Yuan, Multifunctional nanoparticles possessing magnetic, long-lived fluorescence and bio-affinity properties for time-resolved fluorescence cell imaging, Talanta 72 (2007) 1693-1697.
    • (2007) Talanta , vol.72 , pp. 1693-1697
    • Wu, J.1    Ye, Z.Q.2    Wang, G.L.3    Yuan, J.L.4
  • 95
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations
    • R.E. Hansen, J.R. Winther, An introduction to methods for analyzing thiols and disulfides: reactions, reagents, and practical considerations, Anal. Biochem. 394 (2009) 147-158.
    • (2009) Anal. Biochem. , vol.394 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 97
    • 75449105002 scopus 로고    scopus 로고
    • A quantitative evaluation of the molecular binding affinity between a monoclonal antibody conjugated to a nanoparticle and an antigen by surface plasmon resonance
    • N. Debotton, H. Zer, M. Parnes, O. Harush-Frenkel, J. Kadouche, S. Benita, A quantitative evaluation of the molecular binding affinity between a monoclonal antibody conjugated to a nanoparticle and an antigen by surface plasmon resonance, Eur. J. Pharm. Biopharm. 74 (2010) 148-156.
    • (2010) Eur. J. Pharm. Biopharm. , vol.74 , pp. 148-156
    • Debotton, N.1    Zer, H.2    Parnes, M.3    Harush-Frenkel, O.4    Kadouche, J.5    Benita, S.6
  • 98
    • 55049107089 scopus 로고    scopus 로고
    • Preparation of poly(ethylene glycol) protected nanoparticles with variable bioconjugate ligand density
    • M.E. Gindy, S.X. Ji, T.R. Hoye, A.Z. Panagiotopoulos, R.K. Prud'homme, Preparation of poly(ethylene glycol) protected nanoparticles with variable bioconjugate ligand density, Biomacromolecules 9 (2008) 2705-2711.
    • (2008) Biomacromolecules , vol.9 , pp. 2705-2711
    • Gindy, M.E.1    Ji, S.X.2    Hoye, T.R.3    Panagiotopoulos, A.Z.4    Prud'homme, R.K.5
  • 99
    • 33748517626 scopus 로고    scopus 로고
    • Azide/alkyne-"click" reactions: Applications in material science and organic synthesis
    • W.H. Binder, C. Kluger, Azide/alkyne-"click" reactions: applications in material science and organic synthesis, Curr. Org. Chem. 10 (2006) 1791-1815.
    • (2006) Curr. Org. Chem. , vol.10 , pp. 1791-1815
    • Binder, W.H.1    Kluger, C.2
  • 100
    • 33744946037 scopus 로고    scopus 로고
    • Triazole cycloaddition as a general route for functionalization of Au nanoparticles
    • D.A. Fleming, C.J. Thode, M.E. Williams, Triazole cycloaddition as a general route for functionalization of Au nanoparticles, Chem. Mater. 18 (2006) 2327-2334.
    • (2006) Chem. Mater. , vol.18 , pp. 2327-2334
    • Fleming, D.A.1    Thode, C.J.2    Williams, M.E.3
  • 101
    • 77951045250 scopus 로고    scopus 로고
    • Polyvalent Oligonucleotide Iron Oxide Nanoparticle "Click" Conjugates
    • J.I. Cutler, D. Zheng, X.Y. Xu, D.A. Giljohann, C.A. Mirkin, Polyvalent Oligonucleotide Iron Oxide Nanoparticle "Click" Conjugates, Nano Lett. 10 (2010) 1477-1480.
    • (2010) Nano Lett. , vol.10 , pp. 1477-1480
    • Cutler, J.I.1    Zheng, D.2    Xu, X.Y.3    Giljohann, D.A.4    Mirkin, C.A.5
  • 102
    • 38349163224 scopus 로고    scopus 로고
    • One-step bioengineering of magnetic nanoparticles via a surface diazo transfer/azide-alkyne click reaction sequence
    • L. Polito, D. Monti, E. Caneva, E. Delnevo, G. Russo, D. Prosperi, One-step bioengineering of magnetic nanoparticles via a surface diazo transfer/azide-alkyne click reaction sequence, Chem. Commun. (2008) 621-623.
    • (2008) Chem. Commun. , pp. 621-623
    • Polito, L.1    Monti, D.2    Caneva, E.3    Delnevo, E.4    Russo, G.5    Prosperi, D.6
  • 104
    • 72149096051 scopus 로고    scopus 로고
    • Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates
    • Y.P. Kim, W.L. Daniel, Z.Y. Xia, H.X. Xie, C.A. Mirkin, J.H. Rao, Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates, Chem. Commun. 46 (2010) 76-78.
    • (2010) Chem. Commun. , vol.46 , pp. 76-78
    • Kim, Y.P.1    Daniel, W.L.2    Xia, Z.Y.3    Xie, H.X.4    Mirkin, C.A.5    Rao, J.H.6
  • 105
    • 70349316698 scopus 로고    scopus 로고
    • Comparative analysis of nanoparticle-antibody conjugations: Carbodiimide versus click chemistry
    • D.L.J. Thorek, D.R. Elias, A. Tsourkas, Comparative analysis of nanoparticle-antibody conjugations: carbodiimide versus click chemistry, Mol. Imaging 8 (2009) 221-229.
    • (2009) Mol. Imaging , vol.8 , pp. 221-229
    • Thorek, D.L.J.1    Elias, D.R.2    Tsourkas, A.3
  • 106
    • 24044486238 scopus 로고    scopus 로고
    • Highly chemoselective addition of amines to epoxides in water
    • N. Azizi, M.R. Saidi, Highly chemoselective addition of amines to epoxides in water, Org. Lett. 7 (2005) 3649-3651.
    • (2005) Org. Lett. , vol.7 , pp. 3649-3651
    • Azizi, N.1    Saidi, M.R.2
  • 107
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • H.C. Kolb, M.G. Finn, K.B. Sharpless, Click chemistry: diverse chemical function from a few good reactions, Angew. Chem. Int. Edit. 40 (2001) 2004-+.
    • (2001) Angew. Chem. Int. Edit. , vol.40 , pp. 2004
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 108
    • 70349412011 scopus 로고    scopus 로고
    • One-step and high-density protein immobilization on epoxysilane-modified silica nanoparticles
    • Q. Zhang, R.F. Huang, L.H. Guo, One-step and high-density protein immobilization on epoxysilane-modified silica nanoparticles, Chin. Sci. Bull. 54 (2009) 2620-2626.
    • (2009) Chin. Sci. Bull. , vol.54 , pp. 2620-2626
    • Zhang, Q.1    Huang, R.F.2    Guo, L.H.3
  • 109
    • 33645969562 scopus 로고    scopus 로고
    • Immobilization of Mucor javanicus lipase on effectively functionalized silica nanoparticles
    • M.I. Kim, H.O. Ham, S.D. Oh, H.G. Park, H.N. Chang, S.H. Choi, Immobilization of Mucor javanicus lipase on effectively functionalized silica nanoparticles, J. Mol. Catal. B: Enzym. 39 (2006) 62-68.
    • (2006) J. Mol. Catal. B: Enzym. , vol.39 , pp. 62-68
    • Kim, M.I.1    Ham, H.O.2    Oh, S.D.3    Park, H.G.4    Chang, H.N.5    Choi, S.H.6
  • 110
    • 79952583790 scopus 로고    scopus 로고
    • Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods
    • D.-H. Tsai, F.W. DelRio, A.M. Keene, K.M. Tyner, R.I. MacCuspie, T.J. Cho, M.R. Zachariah, V.A. Hackley, Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods, Langmuir 27 (2011) 2464-2477.
    • (2011) Langmuir , vol.27 , pp. 2464-2477
    • Tsai, D.-H.1    DelRio, F.W.2    Keene, A.M.3    Tyner, K.M.4    MacCuspie, R.I.5    Cho, T.J.6    Zachariah, M.R.7    Hackley, V.A.8
  • 112
    • 80054045806 scopus 로고    scopus 로고
    • Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism
    • S. Laera, G. Ceccone, F. Rossi, D. Gilliland, R. Hussain, G. Siligardi, L. Calzolai, Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism, Nano Lett. 11 (2011) 4480-4484.
    • (2011) Nano Lett. , vol.11 , pp. 4480-4484
    • Laera, S.1    Ceccone, G.2    Rossi, F.3    Gilliland, D.4    Hussain, R.5    Siligardi, G.6    Calzolai, L.7
  • 113
    • 78649569522 scopus 로고    scopus 로고
    • Conjugation of peptides to the passivation shell of gold nanoparticles for targeting of cell-surface receptors
    • L. Maus, O. Dick, H. Bading, J.P. Spatz, R. Fiammengo, Conjugation of peptides to the passivation shell of gold nanoparticles for targeting of cell-surface receptors, ACS Nano 4 (2010) 6617-6628.
    • (2010) ACS Nano , vol.4 , pp. 6617-6628
    • Maus, L.1    Dick, O.2    Bading, H.3    Spatz, J.P.4    Fiammengo, R.5
  • 114
    • 31544481163 scopus 로고    scopus 로고
    • Essentials of biorecognition: The (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction
    • M. Wilchek, E.A. Bayer, O. Livnah, Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction, Immunol. Lett. 103 (2006) 27-32.
    • (2006) Immunol. Lett. , vol.103 , pp. 27-32
    • Wilchek, M.1    Bayer, E.A.2    Livnah, O.3
  • 115
    • 34548591376 scopus 로고    scopus 로고
    • Self-directed and self-oriented immobilization of antibody by protein G-DNA conjugate
    • Y. Jung, J.M. Lee, H. Jung, B.H. Chung, Self-directed and self-oriented immobilization of antibody by protein G-DNA conjugate, Anal. Chem. 79 (2007) 6534-6541.
    • (2007) Anal. Chem. , vol.79 , pp. 6534-6541
    • Jung, Y.1    Lee, J.M.2    Jung, H.3    Chung, B.H.4
  • 117
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • K. Nakanishi, T. Sakiyama, K. Imamura, On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon, J. Biosci. Bioeng. 91 (2001) 233-244.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 118
    • 34547562693 scopus 로고    scopus 로고
    • Unfolding of ribonuclease A on silica nanoparticle surfaces
    • W. Shang, J.H. Nuffer, J.S. Dordick, R.W. Siegel, Unfolding of ribonuclease A on silica nanoparticle surfaces, Nano Lett. 7 (2007) 1991-1995.
    • (2007) Nano Lett. , vol.7 , pp. 1991-1995
    • Shang, W.1    Nuffer, J.H.2    Dordick, J.S.3    Siegel, R.W.4
  • 119
    • 34249048873 scopus 로고    scopus 로고
    • Effect of the surface curvature on the secondary structure of peptides adsorbed on nanoparticles
    • H.S. Mandal, H.B. Kraatz, Effect of the surface curvature on the secondary structure of peptides adsorbed on nanoparticles, J. Am. Chem. Soc. 129 (2007) 6356-+.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6356
    • Mandal, H.S.1    Kraatz, H.B.2
  • 120
    • 71649103479 scopus 로고    scopus 로고
    • Regulation of enzyme activity through interactions with nanoparticles
    • Z.C. Wu, B. Zhang, B. Yan, Regulation of enzyme activity through interactions with nanoparticles, Int. J. Mol. Sci. 10 (2009) 4198-4209.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 4198-4209
    • Wu, Z.C.1    Zhang, B.2    Yan, B.3
  • 121
    • 29844434629 scopus 로고    scopus 로고
    • Gold nanoparticle cytochrome c complexes: The effect of nanoparticle ligand charge on protein structure
    • M.E. Aubin-Tam, K. Hamad-Schifferli, Gold nanoparticle cytochrome c complexes: the effect of nanoparticle ligand charge on protein structure, Langmuir 21 (2005) 12080-12084.
    • (2005) Langmuir , vol.21 , pp. 12080-12084
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 122
    • 34249681351 scopus 로고    scopus 로고
    • Synthesis, patterning and applications of star-shaped poly(ethylene glycol) biofunctionalized surfaces
    • C.D. Heyes, J. Groll, M. Moller, G.U. Nienhaus, Synthesis, patterning and applications of star-shaped poly(ethylene glycol) biofunctionalized surfaces, Mol. Biosyst. 3 (2007) 419-430.
    • (2007) Mol. Biosyst. , vol.3 , pp. 419-430
    • Heyes, C.D.1    Groll, J.2    Moller, M.3    Nienhaus, G.U.4
  • 124
    • 1642535341 scopus 로고    scopus 로고
    • Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds
    • R. Hong, N.O. Fischer, A. Verma, C.M. Goodman, T. Emrick, V.M. Rotello, Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds, J. Am. Chem. Soc. 126 (2004) 739-743.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 739-743
    • Hong, R.1    Fischer, N.O.2    Verma, A.3    Goodman, C.M.4    Emrick, T.5    Rotello, V.M.6
  • 125
    • 4043075579 scopus 로고    scopus 로고
    • Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme
    • A.A. Vertegel, R.W. Siegel, J.S. Dordick, Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme, Langmuir 20 (2004) 6800-6807.
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 126
    • 10044277018 scopus 로고    scopus 로고
    • Protein adsorption onto silica nanoparticles: Conformational changes depend on the particles' curvature and the protein stability
    • M. Lundqvist, I. Sethson, B.H. Jonsson, Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability, Langmuir 20 (2004) 10639-10647.
    • (2004) Langmuir , vol.20 , pp. 10639-10647
    • Lundqvist, M.1    Sethson, I.2    Jonsson, B.H.3
  • 127
    • 27744442001 scopus 로고    scopus 로고
    • Mono layer-protected nanoparticle-protein interactions
    • C.C. You, M. De, V.M. Rotello, Mono layer-protected nanoparticle-protein interactions, Curr. Opin. Chem. Biol. 9 (2005) 639-646.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 639-646
    • You, C.C.1    De, M.2    Rotello, V.M.3
  • 131
    • 71249126549 scopus 로고    scopus 로고
    • Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1-1.5 nm Au nanoparticle bioconjugate
    • J.M. Kogot, A.M. Parker, J. Lee, M. Blaber, G.F. Strouse, T.M. Logan, Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1-1.5 nm Au nanoparticle bioconjugate, Bioconjug. Chem. 20 (2009) 2106-2113.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 2106-2113
    • Kogot, J.M.1    Parker, A.M.2    Lee, J.3    Blaber, M.4    Strouse, G.F.5    Logan, T.M.6
  • 132
    • 17644397303 scopus 로고    scopus 로고
    • Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins
    • J.M. Abad, S.F.L. Mertens, M. Pita, V.M. Fernandez, D.J. Schiffrin, Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins, J. Am. Chem. Soc. 127 (2005) 5689-5694.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5689-5694
    • Abad, J.M.1    Mertens, S.F.L.2    Pita, M.3    Fernandez, V.M.4    Schiffrin, D.J.5
  • 133
    • 73949087550 scopus 로고    scopus 로고
    • Effect of Surface Properties on Nanoparticle-Cell Interactions
    • A. Verma, F. Stellacci, Effect of Surface Properties on Nanoparticle-Cell Interactions, Small. 6 (2010) 12-21.
    • (2010) Small , vol.6 , pp. 12-21
    • Verma, A.1    Stellacci, F.2
  • 134
    • 80052870945 scopus 로고    scopus 로고
    • Effects of transport inhibitors on the cellular uptake of carboxylated polystyrene nanoparticles in different cell lines
    • T. dos Santos, J. Varela, I. Lynch, A. Salvati, K.A. Dawson, Effects of transport inhibitors on the cellular uptake of carboxylated polystyrene nanoparticles in different cell lines, PLoS One 6 (2011) e24438.
    • (2011) PLoS One , vol.6
    • Dos Santos, T.1    Varela, J.2    Lynch, I.3    Salvati, A.4    Dawson, K.A.5
  • 135
    • 47549093587 scopus 로고    scopus 로고
    • A multimodal targeting nanoparticle for selectively labeling T cells
    • J. Gunn, H. Wallen, O. Veiseh, C. Sun, C. Fang, J. Cao, C. Yee, M. Zhang, A multimodal targeting nanoparticle for selectively labeling T cells, Small 4 (2008) 712-715.
    • (2008) Small , vol.4 , pp. 712-715
    • Gunn, J.1    Wallen, H.2    Veiseh, O.3    Sun, C.4    Fang, C.5    Cao, J.6    Yee, C.7    Zhang, M.8
  • 136
    • 77954313055 scopus 로고    scopus 로고
    • Stealth nanoparticles: High density but sheddable PEG is a key for tumor targeting
    • S.-D. Li, L. Huang, Stealth nanoparticles: high density but sheddable PEG is a key for tumor targeting, J. Control. Release 145 (2010) 178-181.
    • (2010) J. Control. Release , vol.145 , pp. 178-181
    • Li, S.-D.1    Huang, L.2


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