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Volumn 6, Issue 6, 2012, Pages 4585-4602

Molecular interaction of proteins and peptides with nanoparticles

Author keywords

amyloidosis; colloidal nanocrystalls; protein aggregation; protein structure; protein nanoparticle interaction; proteome; quantum dots; self assembly; surface forces

Indexed keywords

AMYLOIDOSIS; COLLOIDAL NANOCRYSTALLS; PROTEIN AGGREGATION; PROTEIN STRUCTURES; PROTEIN-NANOPARTICLE INTERACTION; SURFACE FORCES;

EID: 84862867927     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn300415x     Document Type: Review
Times cited : (397)

References (167)
  • 2
    • 33646534455 scopus 로고    scopus 로고
    • Functionalized Carbon Nanotubes as Emerging Nanovectors for the Delivery of Therapeutics
    • Klumpp, C.; Kostarelos, K.; Prato, M.; Bianco, A. Functionalized Carbon Nanotubes as Emerging Nanovectors for the Delivery of Therapeutics Biochim. Biophys. Acta 2006, 1758, 404-412
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 404-412
    • Klumpp, C.1    Kostarelos, K.2    Prato, M.3    Bianco, A.4
  • 5
    • 20144379798 scopus 로고    scopus 로고
    • Quantum Dot Bioconjugates for Imaging, Labelling and Sensing
    • Medintz, I. L.; Uyeda, H. T.; Goldman, E. R.; Mattoussi, H. Quantum Dot Bioconjugates for Imaging, Labelling and Sensing Nat. Mater. 2005, 4, 435-446
    • (2005) Nat. Mater. , vol.4 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 7
    • 0346725932 scopus 로고    scopus 로고
    • The Use of Nanocrystals in Biological Detection
    • Alivisatos, P. The Use of Nanocrystals in Biological Detection Nat. Biotechnol. 2004, 22, 47-52
    • (2004) Nat. Biotechnol. , vol.22 , pp. 47-52
    • Alivisatos, P.1
  • 8
    • 37049000154 scopus 로고    scopus 로고
    • Nanosilver: A Nanoproduct in Medical Application
    • Chen, X.; Schluesener, H. J. Nanosilver: A Nanoproduct in Medical Application Toxicol. Lett. 2008, 176, 1-12
    • (2008) Toxicol. Lett. , vol.176 , pp. 1-12
    • Chen, X.1    Schluesener, H.J.2
  • 9
    • 67349191427 scopus 로고    scopus 로고
    • Interaction of Colloidal Gold Nanoparticles with Human Blood: Effects on Particle Size and Analysis of Plasma Protein Binding Profiles
    • Dobrovolskaia, M. A.; Patri, A. K.; Zheng, J.; Clogston, J. D.; Ayub, N.; Aggarwal, P.; Neun, B. W.; Hall, J. B.; McNeil, S. E. Interaction of Colloidal Gold Nanoparticles with Human Blood: Effects on Particle Size and Analysis of Plasma Protein Binding Profiles Nanomedicine 2009, 5, 106-117
    • (2009) Nanomedicine , vol.5 , pp. 106-117
    • Dobrovolskaia, M.A.1    Patri, A.K.2    Zheng, J.3    Clogston, J.D.4    Ayub, N.5    Aggarwal, P.6    Neun, B.W.7    Hall, J.B.8    McNeil, S.E.9
  • 10
    • 79952302512 scopus 로고    scopus 로고
    • Physical-Chemical Aspects of Protein Corona: Relevance to in Vitro and in Vivo Biological Impacts of Nanoparticles
    • Monopoli, M. P.; Walczyk, D.; Campbell, A.; Elia, G.; Lynch, I.; Bombelli, F. B.; Dawson, K. A. Physical-Chemical Aspects of Protein Corona: Relevance to in Vitro and in Vivo Biological Impacts of Nanoparticles J. Am. Chem. Soc. 2011, 133, 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    Bombelli, F.B.6    Dawson, K.A.7
  • 12
    • 0031216476 scopus 로고    scopus 로고
    • Surface Reactivity in the Pathogenic Response to Particulates
    • Fubini, B. Surface Reactivity in the Pathogenic Response to Particulates Environ. Health Perspect. 1997, 105 (Suppl 5) 1013-1020
    • (1997) Environ. Health Perspect. , vol.105 , Issue.SUPPL. 5 , pp. 1013-1020
    • Fubini, B.1
  • 13
    • 79959808397 scopus 로고    scopus 로고
    • Proteomic Characterization of Engineered Nanomaterial-Protein Interactions in Relation to Surface Reactivity
    • Sund, J.; Alenius, H.; Vippola, M.; Savolainen, K.; Puustinen, A. Proteomic Characterization of Engineered Nanomaterial-Protein Interactions in Relation to Surface Reactivity ACS Nano 2011, 5, 4300-4309
    • (2011) ACS Nano , vol.5 , pp. 4300-4309
    • Sund, J.1    Alenius, H.2    Vippola, M.3    Savolainen, K.4    Puustinen, A.5
  • 14
    • 0026761918 scopus 로고
    • Mechanisms, Measurement, and Significance of Lung Macrophage Function
    • Brain, J. D. Mechanisms, Measurement, and Significance of Lung Macrophage Function Environ. Health Perspect. 1992, 97, 5-10
    • (1992) Environ. Health Perspect. , vol.97 , pp. 5-10
    • Brain, J.D.1
  • 15
    • 33845189668 scopus 로고    scopus 로고
    • Carbon Black Nanoparticles Induce Type II Epithelial Cells to Release Chemotaxins for Alveolar Macrophages
    • Barlow, P. G.; Clouter-Baker, A.; Donaldson, K.; Maccallum, J.; Stone, V. Carbon Black Nanoparticles Induce Type II Epithelial Cells to Release Chemotaxins for Alveolar Macrophages Part. Fibre Toxicol. 2005, 2, 11
    • (2005) Part. Fibre Toxicol. , vol.2 , pp. 11
    • Barlow, P.G.1    Clouter-Baker, A.2    Donaldson, K.3    MacCallum, J.4    Stone, V.5
  • 16
    • 2442498325 scopus 로고    scopus 로고
    • Increased Inflammation and Altered Macrophage Chemotactic Responses Caused by Two Ultrafine Particle Types
    • Renwick, L. C.; Brown, D.; Clouter, A.; Donaldson, K. Increased Inflammation and Altered Macrophage Chemotactic Responses Caused by Two Ultrafine Particle Types Occup. Environ. Med. 2004, 61, 442-447
    • (2004) Occup. Environ. Med. , vol.61 , pp. 442-447
    • Renwick, L.C.1    Brown, D.2    Clouter, A.3    Donaldson, K.4
  • 17
    • 33746770098 scopus 로고    scopus 로고
    • Ultrafine Particles Cause Cytoskeletal Dysfunctions in Macrophages: Role of Intracellular Calcium
    • Moller, W.; Brown, D. M.; Kreyling, W. G.; Stone, V. Ultrafine Particles Cause Cytoskeletal Dysfunctions in Macrophages: Role of Intracellular Calcium Part. Fibre Toxicol. 2005, 2, 7
    • (2005) Part. Fibre Toxicol. , vol.2 , pp. 7
    • Moller, W.1    Brown, D.M.2    Kreyling, W.G.3    Stone, V.4
  • 20
    • 33748310797 scopus 로고    scopus 로고
    • Comparison of the Abilities of Ambient and Manufactured Nanoparticles to Induce Cellular Toxicity According to an Oxidative Stress Paradigm
    • Xia, T.; Kovochich, M.; Brant, J.; Hotze, M.; Sempf, J.; Oberley, T.; Sioutas, C.; Yeh, J. I.; Wiesner, M. R.; Nel, A. E. Comparison of the Abilities of Ambient and Manufactured Nanoparticles to Induce Cellular Toxicity According to an Oxidative Stress Paradigm Nano Lett. 2006, 6, 1794-1807
    • (2006) Nano Lett. , vol.6 , pp. 1794-1807
    • Xia, T.1    Kovochich, M.2    Brant, J.3    Hotze, M.4    Sempf, J.5    Oberley, T.6    Sioutas, C.7    Yeh, J.I.8    Wiesner, M.R.9    Nel, A.E.10
  • 23
    • 83355166280 scopus 로고    scopus 로고
    • Induction of ROS, Mitochondrial Damage and Autophagy in Lung Epithelial Cancer Cells by Iron Oxide Nanoparticles
    • Khan, M. I.; Mohammad, A.; Patil, G.; Naqvi, S. A.; Chauhan, L. K.; Ahmad, I. Induction of ROS, Mitochondrial Damage and Autophagy in Lung Epithelial Cancer Cells by Iron Oxide Nanoparticles Biomaterials 2012, 33, 1477-1488
    • (2012) Biomaterials , vol.33 , pp. 1477-1488
    • Khan, M.I.1    Mohammad, A.2    Patil, G.3    Naqvi, S.A.4    Chauhan, L.K.5    Ahmad, I.6
  • 24
    • 80455129723 scopus 로고    scopus 로고
    • EGFR-Targeted Hybrid Plasmonic Magnetic Nanoparticles Synergistically Induce Autophagy and Apoptosis in Non-small Cell Lung Cancer Cells
    • Yokoyama, T.; Tam, J.; Kuroda, S.; Scott, A. W.; Aaron, J.; Larson, T.; Shanker, M.; Correa, A. M.; Kondo, S.; Roth, J. A. et al. EGFR-Targeted Hybrid Plasmonic Magnetic Nanoparticles Synergistically Induce Autophagy and Apoptosis in Non-small Cell Lung Cancer Cells PLoS One 2011, 6, e25507
    • (2011) PLoS One , vol.6 , pp. 25507
    • Yokoyama, T.1    Tam, J.2    Kuroda, S.3    Scott, A.W.4    Aaron, J.5    Larson, T.6    Shanker, M.7    Correa, A.M.8    Kondo, S.9    Roth, J.A.10
  • 25
    • 79956216582 scopus 로고    scopus 로고
    • 4 Nanoparticles Induce Human Lung Cancer Cell Apoptosis through Caspase-8 Pathway Activation and Disrupt Tight Junctions
    • 4 Nanoparticles Induce Human Lung Cancer Cell Apoptosis through Caspase-8 Pathway Activation and Disrupt Tight Junctions Cancer Sci. 2011, 102, 1216-1222
    • (2011) Cancer Sci. , vol.102 , pp. 1216-1222
    • Zhang, G.1    Ding, L.2    Renegar, R.3    Wang, X.4    Lu, Q.5    Huo, S.6    Chen, Y.H.7
  • 26
    • 0037235805 scopus 로고    scopus 로고
    • The Role of Free Radicals in the Toxic and Inflammatory Effects of Four Different Ultrafine Particle Types
    • Dick, C. A.; Brown, D. M.; Donaldson, K.; Stone, V. The Role of Free Radicals in the Toxic and Inflammatory Effects of Four Different Ultrafine Particle Types Inhal. Toxicol. 2003, 15, 39-52
    • (2003) Inhal. Toxicol. , vol.15 , pp. 39-52
    • Dick, C.A.1    Brown, D.M.2    Donaldson, K.3    Stone, V.4
  • 29
    • 0033870253 scopus 로고    scopus 로고
    • Skin Penetration and Stabilization of Formulations Containing Microfine Titanium Dioxide as Physical UV Filter
    • Bennat, C.; Muller-Goymann, C. C. Skin Penetration and Stabilization of Formulations Containing Microfine Titanium Dioxide as Physical UV Filter Int. J. Cosmet. Sci. 2000, 22, 271-283
    • (2000) Int. J. Cosmet. Sci. , vol.22 , pp. 271-283
    • Bennat, C.1    Muller-Goymann, C.C.2
  • 30
    • 33645800783 scopus 로고    scopus 로고
    • Penetration of Intact Skin by Quantum Dots with Diverse Physicochemical Properties
    • Ryman-Rasmussen, J. P.; Riviere, J. E.; Monteiro-Riviere, N. A. Penetration of Intact Skin by Quantum Dots with Diverse Physicochemical Properties Toxicol. Sci. 2006, 91, 159-165
    • (2006) Toxicol. Sci. , vol.91 , pp. 159-165
    • Ryman-Rasmussen, J.P.1    Riviere, J.E.2    Monteiro-Riviere, N.A.3
  • 31
    • 33846883504 scopus 로고    scopus 로고
    • Effects of Mechanical Flexion on the Penetration of Fullerene Amino Acid-Derivatized Peptide Nanoparticles through Skin
    • Rouse, J. G.; Yang, J.; Ryman-Rasmussen, J. P.; Barron, A. R.; Monteiro-Riviere, N. A. Effects of Mechanical Flexion on the Penetration of Fullerene Amino Acid-Derivatized Peptide Nanoparticles through Skin Nano Lett. 2007, 7, 155-160
    • (2007) Nano Lett. , vol.7 , pp. 155-160
    • Rouse, J.G.1    Yang, J.2    Ryman-Rasmussen, J.P.3    Barron, A.R.4    Monteiro-Riviere, N.A.5
  • 32
    • 0037902540 scopus 로고    scopus 로고
    • Activation of Mast Cells by Silver Particles in a Patient with Localized Argyria Due to Implantation of Acupuncture Needles
    • Kakurai, M.; Demitsu, T.; Umemoto, N.; Ohtsuki, M.; Nakagawa, H. Activation of Mast Cells by Silver Particles in a Patient with Localized Argyria Due to Implantation of Acupuncture Needles Br. J. Dermatol. 2003, 148, 822
    • (2003) Br. J. Dermatol. , vol.148 , pp. 822
    • Kakurai, M.1    Demitsu, T.2    Umemoto, N.3    Ohtsuki, M.4    Nakagawa, H.5
  • 37
    • 33845750500 scopus 로고    scopus 로고
    • Surface Coatings Determine Cytotoxicity and Irritation Potential of Quantum Dot Nanoparticles in Epidermal Keratinocytes
    • Ryman-Rasmussen, J. P.; Riviere, J. E.; Monteiro-Riviere, N. A. Surface Coatings Determine Cytotoxicity and Irritation Potential of Quantum Dot Nanoparticles in Epidermal Keratinocytes J. Invest. Dermatol. 2007, 127, 143-153
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 143-153
    • Ryman-Rasmussen, J.P.1    Riviere, J.E.2    Monteiro-Riviere, N.A.3
  • 39
    • 33748746916 scopus 로고    scopus 로고
    • Multi-walled Carbon Nanotube Exposure Alters Protein Expression in Human Keratinocytes
    • Witzmann, F. A.; Monteiro-Riviere, N. A. Multi-walled Carbon Nanotube Exposure Alters Protein Expression in Human Keratinocytes Nanomedicine 2006, 2, 158-168
    • (2006) Nanomedicine , vol.2 , pp. 158-168
    • Witzmann, F.A.1    Monteiro-Riviere, N.A.2
  • 42
    • 77649180085 scopus 로고    scopus 로고
    • PEG-PLA-PEG Block Copolymeric Nanoparticles for Oral Immunization against Hepatitis B
    • Jain, A. K.; Goyal, A. K.; Mishra, N.; Vaidya, B.; Mangal, S.; Vyas, S. P. PEG-PLA-PEG Block Copolymeric Nanoparticles for Oral Immunization against Hepatitis B Int. J. Pharm. 2010, 387, 253-262
    • (2010) Int. J. Pharm. , vol.387 , pp. 253-262
    • Jain, A.K.1    Goyal, A.K.2    Mishra, N.3    Vaidya, B.4    Mangal, S.5    Vyas, S.P.6
  • 44
    • 0036127360 scopus 로고    scopus 로고
    • Biocompatibility of Micro- and Nanoparticles. Part I: In Liver and Kidney
    • Gatti, A. M.; Rivasi, F. Biocompatibility of Micro- and Nanoparticles. Part I: in Liver and Kidney Biomaterials 2002, 23, 2381-2387
    • (2002) Biomaterials , vol.23 , pp. 2381-2387
    • Gatti, A.M.1    Rivasi, F.2
  • 45
    • 0142227102 scopus 로고    scopus 로고
    • Biocompatibility of Micro- and Nano-particles in the Colon. Part II
    • Gatti, A. M. Biocompatibility of Micro- and Nano-particles in the Colon. Part II Biomaterials 2004, 25, 385-392
    • (2004) Biomaterials , vol.25 , pp. 385-392
    • Gatti, A.M.1
  • 46
    • 79955801224 scopus 로고    scopus 로고
    • Efficient Chemotherapy of Rat Glioblastoma Using Doxorubicin-Loaded PLGA Nanoparticles with Different Stabilizers
    • Wohlfart, S.; Khalansky, A. S.; Gelperina, S.; Maksimenko, O.; Bernreuther, C.; Glatzel, M.; Kreuter, J. Efficient Chemotherapy of Rat Glioblastoma Using Doxorubicin-Loaded PLGA Nanoparticles with Different Stabilizers PLoS One 2011, 6, e19121
    • (2011) PLoS One , vol.6 , pp. 19121
    • Wohlfart, S.1    Khalansky, A.S.2    Gelperina, S.3    Maksimenko, O.4    Bernreuther, C.5    Glatzel, M.6    Kreuter, J.7
  • 48
    • 28844488494 scopus 로고    scopus 로고
    • Opsonization, Biodistribution, and Pharmacokinetics of Polymeric Nanoparticles
    • Owens, D. E., 3rd; Peppas, N. A. Opsonization, Biodistribution, and Pharmacokinetics of Polymeric Nanoparticles Int. J. Pharm. 2006, 307, 93-102
    • (2006) Int. J. Pharm. , vol.307 , pp. 93-102
    • Owens Iii, D.E.1    Peppas, N.A.2
  • 49
    • 78651457743 scopus 로고    scopus 로고
    • Polyethylene Glycol Modified, Cross-Linked Starch-Coated Iron Oxide Nanoparticles for Enhanced Magnetic Tumor Targeting
    • Cole, A. J.; David, A. E.; Wang, J.; Galban, C. J.; Hill, H. L.; Yang, V. C. Polyethylene Glycol Modified, Cross-Linked Starch-Coated Iron Oxide Nanoparticles for Enhanced Magnetic Tumor Targeting Biomaterials 2011, 32, 2183-2193
    • (2011) Biomaterials , vol.32 , pp. 2183-2193
    • Cole, A.J.1    David, A.E.2    Wang, J.3    Galban, C.J.4    Hill, H.L.5    Yang, V.C.6
  • 53
    • 79959574752 scopus 로고    scopus 로고
    • Toxicity of Nanocrystal Quantum Dots: The Relevance of Surface Modifications
    • Hoshino, A.; Hanada, S.; Yamamoto, K. Toxicity of Nanocrystal Quantum Dots: The Relevance of Surface Modifications Arch. Toxicol. 2011, 85, 707-720
    • (2011) Arch. Toxicol. , vol.85 , pp. 707-720
    • Hoshino, A.1    Hanada, S.2    Yamamoto, K.3
  • 58
    • 77950140732 scopus 로고    scopus 로고
    • Quantitative Analysis of the Protein Corona on FePt Nanoparticles Formed by Transferrin Binding
    • Jiang, X.; Weise, S.; Hafner, M.; Rocker, C.; Zhang, F.; Parak, W. J.; Nienhaus, G. U. Quantitative Analysis of the Protein Corona on FePt Nanoparticles Formed by Transferrin Binding J. R. Soc. Interface 2010, 7 (Suppl 1) S5-S13
    • (2010) J. R. Soc. Interface , vol.7 , Issue.SUPPL. 1
    • Jiang, X.1    Weise, S.2    Hafner, M.3    Rocker, C.4    Zhang, F.5    Parak, W.J.6    Nienhaus, G.U.7
  • 59
    • 39749107963 scopus 로고    scopus 로고
    • Protein-Nanoparticle Interactions
    • Lynch, I.; Dawson, K. A. Protein-Nanoparticle Interactions Nano Today 2008, 3, 40-47
    • (2008) Nano Today , vol.3 , pp. 40-47
    • Lynch, I.1    Dawson, K.A.2
  • 61
    • 70349466557 scopus 로고    scopus 로고
    • Effect of Maghemite Nanoparticles on Insulin Amyloid Fibril Formation: Selective Labeling, Kinetics, and Fibril Removal by a Magnetic Field
    • Skaat, H.; Sorci, M.; Belfort, G.; Margel, S. Effect of Maghemite Nanoparticles on Insulin Amyloid Fibril Formation: Selective Labeling, Kinetics, and Fibril Removal by a Magnetic Field J. Biomed. Mater. Res. A 2009, 91, 342-351
    • (2009) J. Biomed. Mater. Res. A , vol.91 , pp. 342-351
    • Skaat, H.1    Sorci, M.2    Belfort, G.3    Margel, S.4
  • 62
    • 80054738299 scopus 로고    scopus 로고
    • Supramolecular Nanodevices: From Design Validation to Theranostic Nanomedicine
    • Cabral, H.; Nishiyama, N.; Kataoka, K. Supramolecular Nanodevices: From Design Validation to Theranostic Nanomedicine Acc. Chem. Res. 2011, 44, 999-1008
    • (2011) Acc. Chem. Res. , vol.44 , pp. 999-1008
    • Cabral, H.1    Nishiyama, N.2    Kataoka, K.3
  • 64
    • 79955580331 scopus 로고    scopus 로고
    • Intrinsically Disordered Proteins May Escape Unwanted Interactions via Functional Misfolding
    • Uversky, V. N. Intrinsically Disordered Proteins May Escape Unwanted Interactions via Functional Misfolding Biochim. Biophys. Acta 2011, 1814, 693-712
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 693-712
    • Uversky, V.N.1
  • 65
    • 37549018134 scopus 로고    scopus 로고
    • My Voyage of Discovery to Proteins in Flatland.and beyond
    • Norde, W. My Voyage of Discovery to Proteins in Flatland...and Beyond Colloids Surf. B Biointerfaces 2008, 61, 1-9
    • (2008) Colloids Surf. B Biointerfaces , vol.61 , pp. 1-9
    • Norde, W.1
  • 66
    • 77954293169 scopus 로고    scopus 로고
    • Conformational Transitions of Adsorbed Proteins on Surfaces of Varying Polarity
    • Anand, G.; Sharma, S.; Dutta, A. K.; Kumar, S. K.; Belfort, G. Conformational Transitions of Adsorbed Proteins on Surfaces of Varying Polarity Langmuir 2010, 26, 10803-10811
    • (2010) Langmuir , vol.26 , pp. 10803-10811
    • Anand, G.1    Sharma, S.2    Dutta, A.K.3    Kumar, S.K.4    Belfort, G.5
  • 67
    • 68949119488 scopus 로고    scopus 로고
    • Monoclonal Antibody Interactions with Micro- and Nanoparticles: Adsorption, Aggregation, and Accelerated Stress Studies
    • Bee, J. S.; Chiu, D.; Sawicki, S.; Stevenson, J. L.; Chatterjee, K.; Freund, E.; Carpenter, J. F.; Randolph, T. W. Monoclonal Antibody Interactions with Micro- and Nanoparticles: Adsorption, Aggregation, and Accelerated Stress Studies J. Pharm. Sci. 2009, 98, 3218-3238
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3218-3238
    • Bee, J.S.1    Chiu, D.2    Sawicki, S.3    Stevenson, J.L.4    Chatterjee, K.5    Freund, E.6    Carpenter, J.F.7    Randolph, T.W.8
  • 68
    • 73949093277 scopus 로고    scopus 로고
    • Aggregation of a Monoclonal Antibody Induced by Adsorption to Stainless Steel
    • Bee, J. S.; Davis, M.; Freund, E.; Carpenter, J. F.; Randolph, T. W. Aggregation of a Monoclonal Antibody Induced by Adsorption to Stainless Steel Biotechnol. Bioeng. 2010, 105, 121-129
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 121-129
    • Bee, J.S.1    Davis, M.2    Freund, E.3    Carpenter, J.F.4    Randolph, T.W.5
  • 70
    • 0034657198 scopus 로고    scopus 로고
    • CD Spectroscopy of Proteins Adsorbed at Flat Hydrophilic Quartz and Hydrophobic Teflon Surfaces
    • Vermeer, A. W.; Norde, W. CD Spectroscopy of Proteins Adsorbed at Flat Hydrophilic Quartz and Hydrophobic Teflon Surfaces J. Colloid Interface Sci. 2000, 225, 394-397
    • (2000) J. Colloid Interface Sci. , vol.225 , pp. 394-397
    • Vermeer, A.W.1    Norde, W.2
  • 71
    • 79958162258 scopus 로고    scopus 로고
    • Interaction of Beta-Sheet Folds with a Gold Surface
    • Hoefling, M.; Monti, S.; Corni, S.; Gottschalk, K. E. Interaction of Beta-Sheet Folds with a Gold Surface PLoS One 2011, 6, e20925
    • (2011) PLoS One , vol.6 , pp. 20925
    • Hoefling, M.1    Monti, S.2    Corni, S.3    Gottschalk, K.E.4
  • 72
    • 71749085441 scopus 로고    scopus 로고
    • Water Structuring and Collagen Adsorption at Hydrophilic and Hydrophobic Silicon Surfaces
    • Cole, D. J.; Payne, M. C.; Ciacchi, L. C. Water Structuring and Collagen Adsorption at Hydrophilic and Hydrophobic Silicon Surfaces Phys. Chem. Chem. Phys. 2009, 11, 11395-11399
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 11395-11399
    • Cole, D.J.1    Payne, M.C.2    Ciacchi, L.C.3
  • 74
    • 54049144209 scopus 로고    scopus 로고
    • Effect of Surface Concentration on Secondary and Tertiary Conformational Changes of Lysozyme Adsorbed on Silica Nanoparticles
    • Wu, X.; Narsimhan, G. Effect of Surface Concentration on Secondary and Tertiary Conformational Changes of Lysozyme Adsorbed on Silica Nanoparticles Biochim. Biophys. Acta 2008, 1784, 1694-1701
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1694-1701
    • Wu, X.1    Narsimhan, G.2
  • 75
    • 79952607947 scopus 로고    scopus 로고
    • Protein Adsorption at Charged Surfaces: The Role of Electrostatic Interactions and Interfacial Charge Regulation
    • 10.1021/la104720n
    • Hartvig, R. A.; van de Weert, M.; Ostergaard, J.; Jorgensen, L.; Jensen, H. Protein Adsorption at Charged Surfaces: The Role of Electrostatic Interactions and Interfacial Charge Regulation Langmuir 2011, 10.1021/la104720n
    • (2011) Langmuir
    • Hartvig, R.A.1    Van De Weert, M.2    Ostergaard, J.3    Jorgensen, L.4    Jensen, H.5
  • 76
    • 69949139818 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Hen Egg White Lysozyme Adsorption at a Charged Solid Surface
    • Kubiak, K.; Mulheran, P. A. Molecular Dynamics Simulations of Hen Egg White Lysozyme Adsorption at a Charged Solid Surface J. Phys. Chem. B 2009, 113, 12189-12200
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12189-12200
    • Kubiak, K.1    Mulheran, P.A.2
  • 77
    • 23844548026 scopus 로고    scopus 로고
    • Change of Zeta Potential of Biocompatible Colloidal Oxide Particles Upon Adsorption of Bovine Serum Albumin and Lysozyme
    • Rezwan, K.; Studart, A. R.; Voros, J.; Gauckler, L. J. Change of Zeta Potential of Biocompatible Colloidal Oxide Particles Upon Adsorption of Bovine Serum Albumin and Lysozyme J. Phys. Chem. B 2005, 109, 14469-14474
    • (2005) J. Phys. Chem. B , vol.109 , pp. 14469-14474
    • Rezwan, K.1    Studart, A.R.2    Voros, J.3    Gauckler, L.J.4
  • 78
    • 67651002623 scopus 로고    scopus 로고
    • PH-Dependent Surface Charging and Points of Zero Charge. IV. Update and New Approach
    • Kosmulski, M. pH-Dependent Surface Charging and Points of Zero Charge. IV. Update and New Approach J. Colloid Interface Sci. 2009, 337, 439-448
    • (2009) J. Colloid Interface Sci. , vol.337 , pp. 439-448
    • Kosmulski, M.1
  • 79
    • 17844400953 scopus 로고    scopus 로고
    • Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles
    • Karlsson, M.; Carlsson, U. Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles Biophys. J. 2005, 88, 3536-3544
    • (2005) Biophys. J. , vol.88 , pp. 3536-3544
    • Karlsson, M.1    Carlsson, U.2
  • 80
    • 79957991651 scopus 로고    scopus 로고
    • Mechanisms of Fibrinogen Adsorption at Solid Substrates
    • Adamczyk, Z.; Barbasz, J.; Ciesla, M. Mechanisms of Fibrinogen Adsorption at Solid Substrates Langmuir 2011, 27, 6868-6878
    • (2011) Langmuir , vol.27 , pp. 6868-6878
    • Adamczyk, Z.1    Barbasz, J.2    Ciesla, M.3
  • 81
    • 0032188786 scopus 로고    scopus 로고
    • The Denaturation of Lysozyme Layers Adsorbed at the Hydrophobic Solid/Liquid Surface Studied by Neutron Reflection
    • Lu, J. R.; Su, T. J.; Thirtle, P. N.; Thomas, R. K.; Rennie, A. R.; Cubitt, R. The Denaturation of Lysozyme Layers Adsorbed at the Hydrophobic Solid/Liquid Surface Studied by Neutron Reflection J. Colloid Interface Sci. 1998, 206, 212-223
    • (1998) J. Colloid Interface Sci. , vol.206 , pp. 212-223
    • Lu, J.R.1    Su, T.J.2    Thirtle, P.N.3    Thomas, R.K.4    Rennie, A.R.5    Cubitt, R.6
  • 83
    • 0001431603 scopus 로고    scopus 로고
    • Effect of pH on the Adsorption of Bovine Serum Albumin at the Silica/Water Interface Studied by Neutron Reflection
    • Su, T. J.; Lu, J. R.; Thomas, R. K.; Cui, Z. F. Effect of pH on the Adsorption of Bovine Serum Albumin at the Silica/Water Interface Studied by Neutron Reflection J. Phys. Chem. B 1999, 103, 3727-3736
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3727-3736
    • Su, T.J.1    Lu, J.R.2    Thomas, R.K.3    Cui, Z.F.4
  • 85
    • 77956423135 scopus 로고    scopus 로고
    • An Index for Characterization of Nanomaterials in Biological Systems
    • Xia, X. R.; Monteiro-Riviere, N. A.; Riviere, J. E. An Index for Characterization of Nanomaterials in Biological Systems Nat. Nanotechnol. 2010, 5, 671-675
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 671-675
    • Xia, X.R.1    Monteiro-Riviere, N.A.2    Riviere, J.E.3
  • 87
    • 36749055209 scopus 로고    scopus 로고
    • Nonfunctionalized Nanocrystals Can Exploit a Cell's Active Transport Machinery Delivering Them to Specific Nuclear and Cytoplasmic Compartments
    • Nabiev, I.; Mitchell, S.; Davies, A.; Williams, Y.; Kelleher, D.; Moore, R.; Gun'ko, Y. K.; Byrne, S.; Rakovich, Y. P.; Donegan, J. F. et al. Nonfunctionalized Nanocrystals Can Exploit a Cell's Active Transport Machinery Delivering Them to Specific Nuclear and Cytoplasmic Compartments Nano Lett. 2007, 7, 3452-3461
    • (2007) Nano Lett. , vol.7 , pp. 3452-3461
    • Nabiev, I.1    Mitchell, S.2    Davies, A.3    Williams, Y.4    Kelleher, D.5    Moore, R.6    Gun'Ko, Y.K.7    Byrne, S.8    Rakovich, Y.P.9    Donegan, J.F.10
  • 89
    • 73649109910 scopus 로고    scopus 로고
    • Size-Dependent Hydrophobic to Hydrophilic Transition for Nanoparticles: A Molecular Dynamics Study
    • Chiu, C. C.; Moore, P. B.; Shinoda, W.; Nielsen, S. O. Size-Dependent Hydrophobic to Hydrophilic Transition for Nanoparticles: A Molecular Dynamics Study J. Chem. Phys. 2009, 131, 244706
    • (2009) J. Chem. Phys. , vol.131 , pp. 244706
    • Chiu, C.C.1    Moore, P.B.2    Shinoda, W.3    Nielsen, S.O.4
  • 90
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle Size and Surface Properties Determine the Protein Corona with Possible Implications for Biological Impacts
    • Lundqvist, M.; Stigler, J.; Elia, G.; Lynch, I.; Cedervall, T.; Dawson, K. A. Nanoparticle Size and Surface Properties Determine the Protein Corona with Possible Implications for Biological Impacts Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 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
  • 91
    • 79960846411 scopus 로고    scopus 로고
    • Effect of Gold Nanoparticle Morphology on Adsorbed Protein Structure and Function
    • Gagner, J. E.; Lopez, M. D.; Dordick, J. S.; Siegel, R. W. Effect of Gold Nanoparticle Morphology on Adsorbed Protein Structure and Function Biomaterials 2011, 32, 7241-7252
    • (2011) Biomaterials , vol.32 , pp. 7241-7252
    • Gagner, J.E.1    Lopez, M.D.2    Dordick, J.S.3    Siegel, R.W.4
  • 92
    • 4043075579 scopus 로고    scopus 로고
    • Silica Nanoparticle Size Influences the Structure and Enzymatic Activity of Adsorbed Lysozyme
    • Vertegel, A. A.; Siegel, R. W.; Dordick, J. S. Silica Nanoparticle Size Influences the Structure and Enzymatic Activity of Adsorbed Lysozyme Langmuir 2004, 20, 6800-6807
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 93
    • 33645459798 scopus 로고    scopus 로고
    • Surface Tailoring for Controlled Protein Adsorption: Effect of Topography at the Nanometer Scale and Chemistry
    • Roach, P.; Farrar, D.; Perry, C. C. Surface Tailoring for Controlled Protein Adsorption: Effect of Topography at the Nanometer Scale and Chemistry J. Am. Chem. Soc. 2006, 128, 3939-3945
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 95
    • 77955562565 scopus 로고    scopus 로고
    • Protein-Nanoparticle Interaction: Identification of the Ubiquitin-Gold Nanoparticle Interaction Site
    • Calzolai, L.; Franchini, F.; Gilliland, D.; Rossi, F. Protein-Nanoparticle Interaction: Identification of the Ubiquitin-Gold Nanoparticle Interaction Site Nano Lett. 2010, 10, 3101-3105
    • (2010) Nano Lett. , vol.10 , pp. 3101-3105
    • Calzolai, L.1    Franchini, F.2    Gilliland, D.3    Rossi, F.4
  • 96
    • 10044277018 scopus 로고    scopus 로고
    • Protein Adsorption onto Silica Nanoparticles: Conformational Changes Depend on the Particles' Curvature and the Protein Stability
    • Lundqvist, M.; Sethson, I.; Jonsson, B. H. Protein Adsorption onto Silica Nanoparticles: Conformational Changes Depend on the Particles' Curvature and the Protein Stability Langmuir 2004, 20, 10639-10647
    • (2004) Langmuir , vol.20 , pp. 10639-10647
    • Lundqvist, M.1    Sethson, I.2    Jonsson, B.H.3
  • 97
    • 62749100589 scopus 로고    scopus 로고
    • Cytochrome C on Silica Nanoparticles: Influence of Nanoparticle Size on Protein Structure, Stability, and Activity
    • Shang, W.; Nuffer, J. H.; Muniz-Papandrea, V. A.; Colon, W.; Siegel, R. W.; Dordick, J. S. Cytochrome C on Silica Nanoparticles: Influence of Nanoparticle Size on Protein Structure, Stability, and Activity Small 2009, 5, 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
  • 98
    • 34547562693 scopus 로고    scopus 로고
    • Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces
    • Shang, W.; Nuffer, J. H.; Dordick, J. S.; Siegel, R. W. Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces Nano Lett. 2007, 7, 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
  • 99
    • 34249048873 scopus 로고    scopus 로고
    • Effect of the Surface Curvature on the Secondary Structure of Peptides Adsorbed on Nanoparticles
    • Mandal, H. S.; Kraatz, H. B. Effect of the Surface Curvature on the Secondary Structure of Peptides Adsorbed on Nanoparticles J. Am. Chem. Soc. 2007, 129, 6356-6357
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6356-6357
    • Mandal, H.S.1    Kraatz, H.B.2
  • 100
    • 82455167818 scopus 로고    scopus 로고
    • Protein Structural Changes Induced by Glutathione-Coated CdS Quantum Dots as Revealed by Trp Phosphorescence
    • Gabellieri, E.; Cioni, P.; Balestreri, E.; Morelli, E. Protein Structural Changes Induced by Glutathione-Coated CdS Quantum Dots as Revealed by Trp Phosphorescence Eur. Biophys. J. 2011, 40, 1237-1245
    • (2011) Eur. Biophys. J. , vol.40 , pp. 1237-1245
    • Gabellieri, E.1    Cioni, P.2    Balestreri, E.3    Morelli, E.4
  • 101
    • 33745748175 scopus 로고    scopus 로고
    • Increasing Protein Stability through Control of the Nanoscale Environment
    • Asuri, P.; Karajanagi, S. S.; Yang, H.; Yim, T. J.; Kane, R. S.; Dordick, J. S. Increasing Protein Stability through Control of the Nanoscale Environment Langmuir 2006, 22, 5833-5836
    • (2006) Langmuir , vol.22 , pp. 5833-5836
    • Asuri, P.1    Karajanagi, S.S.2    Yang, H.3    Yim, T.J.4    Kane, R.S.5    Dordick, J.S.6
  • 103
    • 38049172612 scopus 로고    scopus 로고
    • Structure, Stability, and Activity of Myoglobin Adsorbed onto Phosphate-Grafted Zirconia Nanoparticles
    • Bellezza, F.; Cipiciani, A.; Quotadamo, M. A.; Cinelli, S.; Onori, G.; Tacchi, S. Structure, Stability, and Activity of Myoglobin Adsorbed onto Phosphate-Grafted Zirconia Nanoparticles Langmuir 2007, 23, 13007-13012
    • (2007) Langmuir , vol.23 , pp. 13007-13012
    • Bellezza, F.1    Cipiciani, A.2    Quotadamo, M.A.3    Cinelli, S.4    Onori, G.5    Tacchi, S.6
  • 105
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the Nanoparticle-Protein Corona Using Methods to Quantify Exchange Rates and Affinities of Proteins for Nanoparticles
    • Cedervall, T.; Lynch, I.; Lindman, S.; Berggard, T.; Thulin, E.; Nilsson, H.; Dawson, K. A.; Linse, S. Understanding the Nanoparticle-Protein Corona Using Methods to Quantify Exchange Rates and Affinities of Proteins for Nanoparticles Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 2050-2055
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggard, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 106
    • 35349010059 scopus 로고    scopus 로고
    • The Nanoparticle-Protein Complex as a Biological Entity; A Complex Fluids and Surface Science Challenge for the 21st Century
    • Lynch, I.; Cedervall, T.; Lundqvist, M.; Cabaleiro-Lago, C.; Linse, S.; Dawson, K. A. The Nanoparticle-Protein Complex as a Biological Entity; A Complex Fluids and Surface Science Challenge for the 21st Century Adv. Colloid Interface Sci. 2007, 134-135, 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
  • 107
    • 79952694623 scopus 로고    scopus 로고
    • Role of Surface Area, Primary Particle Size, and Crystal Phase on Titanium Dioxide Nanoparticle Dispersion Properties
    • Suttiponparnit, K.; Jiang, J.; Sahu, M.; Suvachittanont, S.; Charinpanitkul, T.; Biswas, P. Role of Surface Area, Primary Particle Size, and Crystal Phase on Titanium Dioxide Nanoparticle Dispersion Properties Nanoscale Res. Lett. 2011, 6, 1-8
    • (2011) Nanoscale Res. Lett. , vol.6 , pp. 1-8
    • Suttiponparnit, K.1    Jiang, J.2    Sahu, M.3    Suvachittanont, S.4    Charinpanitkul, T.5    Biswas, P.6
  • 108
    • 34248155667 scopus 로고    scopus 로고
    • Systematic Investigation of the Thermodynamics of HSA Adsorption to N - Iso -Propylacrylamide/ N - Tert -Butylacrylamide Copolymer Nanoparticles. Effects of Particle Size and Hydrophobicity
    • Lindman, S.; Lynch, I.; Thulin, E.; Nilsson, H.; Dawson, K. A.; Linse, S. Systematic Investigation of the Thermodynamics of HSA Adsorption to N-iso -Propylacrylamide/ N-tert -Butylacrylamide Copolymer Nanoparticles. Effects of Particle Size and Hydrophobicity Nano Lett. 2007, 7, 914-920
    • (2007) Nano Lett. , vol.7 , pp. 914-920
    • Lindman, S.1    Lynch, I.2    Thulin, E.3    Nilsson, H.4    Dawson, K.A.5    Linse, S.6
  • 109
    • 33750440502 scopus 로고    scopus 로고
    • Are There Generic Mechanisms Governing Interactions between Nanoparticles and Cells? Epitope Mapping the Outer Layer of the Protein-Material Interface
    • Lynch, I. Are There Generic Mechanisms Governing Interactions between Nanoparticles and Cells? Epitope Mapping the Outer Layer of the Protein-Material Interface Phys. A 2007, 373, 511-520
    • (2007) Phys. A , vol.373 , pp. 511-520
    • Lynch, I.1
  • 110
    • 33646183969 scopus 로고    scopus 로고
    • Detecting Cryptic Epitopes Created by Nanoparticles
    • Lynch, I.; Dawson, K. A.; Linse, S. Detecting Cryptic Epitopes Created by Nanoparticles Sci. STKE 2006, 2006, pe14
    • (2006) Sci. STKE , vol.2006 , pp. 14
    • Lynch, I.1    Dawson, K.A.2    Linse, S.3
  • 111
    • 0037666430 scopus 로고    scopus 로고
    • Coverage-Dependent Orientation of Lysozyme Adsorbed on Silica
    • Daly, S. M.; Przybycien, T. M.; Tilton, R. D. Coverage-Dependent Orientation of Lysozyme Adsorbed on Silica Langmuir 2003, 19, 3848-3857
    • (2003) Langmuir , vol.19 , pp. 3848-3857
    • Daly, S.M.1    Przybycien, T.M.2    Tilton, R.D.3
  • 113
    • 77956224283 scopus 로고    scopus 로고
    • Effects of Nano-sized Silicon Dioxide on the Structures and Activities of Three Functional Proteins
    • Xu, Z.; Wang, S. L.; Gao, H. W. Effects of Nano-sized Silicon Dioxide on the Structures and Activities of Three Functional Proteins J. Hazard. Mater. 2010, 180, 375-383
    • (2010) J. Hazard. Mater. , vol.180 , pp. 375-383
    • Xu, Z.1    Wang, S.L.2    Gao, H.W.3
  • 114
  • 115
    • 46749087806 scopus 로고    scopus 로고
    • Characterization of a Targeted Nanoparticle Functionalized with a Urea-Based Inhibitor of Prostate-Specific Membrane Antigen (PSMA)
    • Chandran, S. S.; Banerjee, S. R.; Mease, R. C.; Pomper, M. G.; Denmeade, S. R. Characterization of a Targeted Nanoparticle Functionalized with a Urea-Based Inhibitor of Prostate-Specific Membrane Antigen (PSMA) Cancer Biol. Ther. 2008, 7, 974-982
    • (2008) Cancer Biol. Ther. , vol.7 , pp. 974-982
    • Chandran, S.S.1    Banerjee, S.R.2    Mease, R.C.3    Pomper, M.G.4    Denmeade, S.R.5
  • 117
  • 118
    • 67649386624 scopus 로고    scopus 로고
    • In Pursuit of Zero: Polymer Brushes that Resist the Adsorption of Proteins
    • Hucknall, A.; Rangarajan, S.; Chilkoti, A. In Pursuit of Zero: Polymer Brushes that Resist the Adsorption of Proteins Adv. Mater. 2009, 21, 2441-2446
    • (2009) Adv. Mater. , vol.21 , pp. 2441-2446
    • Hucknall, A.1    Rangarajan, S.2    Chilkoti, A.3
  • 119
    • 77952107337 scopus 로고    scopus 로고
    • A Comparison of Mono and Multivalent Linkers and Their Effect on the Colloidal Stability of Nanoparticle and Immunoassays Performance
    • Gubala, V.; Le Guevel, X.; Nooney, R.; Williams, D. E.; MacCraith, B. A Comparison of Mono and Multivalent Linkers and Their Effect on the Colloidal Stability of Nanoparticle and Immunoassays Performance Talanta 2010, 81, 1833-1839
    • (2010) Talanta , vol.81 , pp. 1833-1839
    • Gubala, V.1    Le Guevel, X.2    Nooney, R.3    Williams, D.E.4    MacCraith, B.5
  • 120
    • 77951723418 scopus 로고    scopus 로고
    • Morphing Low-Affinity Ligands into High-Avidity Nanoparticles by Thermally Triggered Self-Assembly of a Genetically Encoded Polymer
    • Simnick, A. J.; Valencia, C. A.; Liu, R.; Chilkoti, A. Morphing Low-Affinity Ligands into High-Avidity Nanoparticles by Thermally Triggered Self-Assembly of a Genetically Encoded Polymer ACS Nano 2010, 4, 2217-2227
    • (2010) ACS Nano , vol.4 , pp. 2217-2227
    • Simnick, A.J.1    Valencia, C.A.2    Liu, R.3    Chilkoti, A.4
  • 122
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of Globular Proteins on Locally Planar Surfaces: Models for the Effect of Excluded Surface Area and Aggregation of Adsorbed Protein on Adsorption Equilibria
    • Chatelier, R. C.; Minton, A. P. Adsorption of Globular Proteins on Locally Planar Surfaces: Models for the Effect of Excluded Surface Area and Aggregation of Adsorbed Protein on Adsorption Equilibria Biophys. J. 1996, 71, 2367-2374
    • (1996) Biophys. J. , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 123
    • 0032905175 scopus 로고    scopus 로고
    • Adsorption of Globular Proteins on Locally Planar Surfaces. II. Models for the Effect of Multiple Adsorbate Conformations on Adsorption Equilibria and Kinetics
    • Minton, A. P. Adsorption of Globular Proteins on Locally Planar Surfaces. II. Models for the Effect of Multiple Adsorbate Conformations on Adsorption Equilibria and Kinetics Biophys. J. 1999, 76, 176-187
    • (1999) Biophys. J. , vol.76 , pp. 176-187
    • Minton, A.P.1
  • 124
    • 0034734291 scopus 로고    scopus 로고
    • Effects of Excluded Surface Area and Adsorbate Clustering on Surface Adsorption of Proteins. I. Equilibrium Models
    • Minton, A. P. Effects of Excluded Surface Area and Adsorbate Clustering on Surface Adsorption of Proteins. I. Equilibrium Models Biophys. Chem. 2000, 86, 239-247
    • (2000) Biophys. Chem. , vol.86 , pp. 239-247
    • Minton, A.P.1
  • 125
    • 0035073816 scopus 로고    scopus 로고
    • Effects of Excluded Surface Area and Adsorbate Clustering on Surface Adsorption of Proteins. II. Kinetic Models
    • Minton, A. P. Effects of Excluded Surface Area and Adsorbate Clustering on Surface Adsorption of Proteins. II. Kinetic Models Biophys. J. 2001, 80, 1641-1648
    • (2001) Biophys. J. , vol.80 , pp. 1641-1648
    • Minton, A.P.1
  • 126
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 2006, 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 127
    • 77955898208 scopus 로고    scopus 로고
    • Effects of DHLA-Capped CdSe/ZnS Quantum Dots on the Fibrillation of Human Serum Albumin
    • Vannoy, C. H.; Leblanc, R. M. Effects of DHLA-Capped CdSe/ZnS Quantum Dots on the Fibrillation of Human Serum Albumin J. Phys. Chem. B 2010, 114, 10881-10888
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10881-10888
    • Vannoy, C.H.1    Leblanc, R.M.2
  • 128
    • 77749320957 scopus 로고    scopus 로고
    • Inhibition of IAPP and IAPP(20-29) Fibrillation by Polymeric Nanoparticles
    • Cabaleiro-Lago, C.; Lynch, I.; Dawson, K. A.; Linse, S. Inhibition of IAPP and IAPP(20-29) Fibrillation by Polymeric Nanoparticles Langmuir 2010, 26, 3453-3461
    • (2010) Langmuir , vol.26 , pp. 3453-3461
    • Cabaleiro-Lago, C.1    Lynch, I.2    Dawson, K.A.3    Linse, S.4
  • 129
    • 70350348150 scopus 로고    scopus 로고
    • Inhibition of Beta 1-40 Amyloid Fibrillation with N -Acetyl- l -cysteine Capped Quantum Dots
    • Xiao, L.; Zhao, D.; Chan, W. H.; Choi, M. M.; Li, H. W. Inhibition of Beta 1-40 Amyloid Fibrillation with N -Acetyl- l -cysteine Capped Quantum Dots Biomaterials 2010, 31, 91-98
    • (2010) Biomaterials , vol.31 , pp. 91-98
    • Xiao, L.1    Zhao, D.2    Chan, W.H.3    Choi, M.M.4    Li, H.W.5
  • 130
    • 37849186419 scopus 로고    scopus 로고
    • Inhibition of the Formation of Amyloid β-Protein Fibrils Using Biocompatible Nanogels as Artificial Chaperones
    • Ikeda, K.; Okada, T.; Sawada, S.; Akiyoshi, K.; Matsuzaki, K. Inhibition of the Formation of Amyloid β-Protein Fibrils Using Biocompatible Nanogels as Artificial Chaperones FEBS Lett. 2006, 580, 6587-6595
    • (2006) FEBS Lett. , vol.580 , pp. 6587-6595
    • Ikeda, K.1    Okada, T.2    Sawada, S.3    Akiyoshi, K.4    Matsuzaki, K.5
  • 135
    • 80051521864 scopus 로고    scopus 로고
    • Aggregation of Silica Nanoparticles Directed by Adsorption of Lysozyme
    • Bharti, B.; Meissner, J.; Findenegg, G. H. Aggregation of Silica Nanoparticles Directed by Adsorption of Lysozyme Langmuir 2011, 27, 9823-9833
    • (2011) Langmuir , vol.27 , pp. 9823-9833
    • Bharti, B.1    Meissner, J.2    Findenegg, G.H.3
  • 136
    • 79952851709 scopus 로고    scopus 로고
    • Particle and Nanoparticle Interactions with Fibrinogen: The Importance of Aggregation in Nanotoxicology
    • Kendall, M.; Ding, P.; Kendall, K. Particle and Nanoparticle Interactions with Fibrinogen: The Importance of Aggregation in Nanotoxicology Nanotoxicology 2011, 5, 55-65
    • (2011) Nanotoxicology , vol.5 , pp. 55-65
    • Kendall, M.1    Ding, P.2    Kendall, K.3
  • 137
    • 78650606928 scopus 로고    scopus 로고
    • Nanoparticle-Induced Unfolding of Fibrinogen Promotes Mac-1 Receptor Activation and Inflammation
    • Deng, Z. J.; Liang, M.; Monteiro, M.; Toth, I.; Minchin, R. F. Nanoparticle-Induced Unfolding of Fibrinogen Promotes Mac-1 Receptor Activation and Inflammation Nat. Nanotechnol. 2011, 6, 39-44
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 39-44
    • Deng, Z.J.1    Liang, M.2    Monteiro, M.3    Toth, I.4    Minchin, R.F.5
  • 138
    • 0038359740 scopus 로고    scopus 로고
    • Reactive Oxygen Species (ROS) and Reactive Nitrogen Species (RNS) Generation by Silica in Inflammation and Fibrosis
    • Fubini, B.; Hubbard, A. Reactive Oxygen Species (ROS) and Reactive Nitrogen Species (RNS) Generation by Silica in Inflammation and Fibrosis Free Radical Biol. Med. 2003, 34, 1507-1516
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 1507-1516
    • Fubini, B.1    Hubbard, A.2
  • 139
    • 41549129392 scopus 로고    scopus 로고
    • The Role of Oxidative Stress in Ambient Particulate Matter-Induced Lung Diseases and Its Implications in the Toxicity of Engineered Nanoparticles
    • Li, N.; Xia, T.; Nel, A. E. The Role of Oxidative Stress in Ambient Particulate Matter-Induced Lung Diseases and Its Implications in the Toxicity of Engineered Nanoparticles Free Radic. Biol. Med. 2008, 44, 1689-1699
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1689-1699
    • Li, N.1    Xia, T.2    Nel, A.E.3
  • 143
    • 84855573512 scopus 로고    scopus 로고
    • Theranostic Nanoplatforms for Simultaneous Cancer Imaging and Therapy: Current Approaches and Future Perspectives
    • Choi, K. Y.; Liu, G.; Lee, S.; Chen, X. Theranostic Nanoplatforms for Simultaneous Cancer Imaging and Therapy: Current Approaches and Future Perspectives Nanoscale 2011, 4, 330-342
    • (2011) Nanoscale , vol.4 , pp. 330-342
    • Choi, K.Y.1    Liu, G.2    Lee, S.3    Chen, X.4
  • 144
    • 84856642971 scopus 로고    scopus 로고
    • Chemical Nature and Structure of Organic Coating of Quantum Dots Is Crucial for Their Application in Imaging Diagnostics
    • Bakalova, R.; Zhelev, Z.; Kokuryo, D.; Spasov, L.; Aoki, I.; Saga, T. Chemical Nature and Structure of Organic Coating of Quantum Dots Is Crucial for Their Application in Imaging Diagnostics Int. J. Nanomed. 2011, 6, 1719-1732
    • (2011) Int. J. Nanomed. , vol.6 , pp. 1719-1732
    • Bakalova, R.1    Zhelev, Z.2    Kokuryo, D.3    Spasov, L.4    Aoki, I.5    Saga, T.6
  • 147
    • 2142821377 scopus 로고    scopus 로고
    • Electrostatic Interactions in Protein Adsorption Probed by Comparing Lysozyme and Succinylated Lysozyme
    • van der Veen, M.; Norde, W.; Stuart, M. C. Electrostatic Interactions in Protein Adsorption Probed by Comparing Lysozyme and Succinylated Lysozyme Colloids Surf. B 2004, 35, 33-40
    • (2004) Colloids Surf. B , vol.35 , pp. 33-40
    • Van Der Veen, M.1    Norde, W.2    Stuart, M.C.3
  • 148
    • 78650677105 scopus 로고    scopus 로고
    • Adsorption of Low-Density Lipoprotein, Its Oxidation, and Subsequent Binding of Specific Recombinant Antibodies: An in Situ Ellipsometric Study
    • Stollenwerk, M. M.; Svensson, O.; Schiopu, A.; Jansson, B.; Arnebrant, T.; Fredrikson, G. N. Adsorption of Low-Density Lipoprotein, Its Oxidation, and Subsequent Binding of Specific Recombinant Antibodies: An in Situ Ellipsometric Study Biochim. Biophys. Acta 2011, 1810, 211-217
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 211-217
    • Stollenwerk, M.M.1    Svensson, O.2    Schiopu, A.3    Jansson, B.4    Arnebrant, T.5    Fredrikson, G.N.6
  • 149
    • 34248342939 scopus 로고    scopus 로고
    • Spectroscopic Studies on the Interaction between Human Hemoglobin and CdS Quantum Dots
    • Shen, X. C.; Liou, X. Y.; Ye, L. P.; Liang, H.; Wang, Z. Y. Spectroscopic Studies on the Interaction between Human Hemoglobin and CdS Quantum Dots J. Colloid Interface Sci. 2007, 311, 400-406
    • (2007) J. Colloid Interface Sci. , vol.311 , pp. 400-406
    • Shen, X.C.1    Liou, X.Y.2    Ye, L.P.3    Liang, H.4    Wang, Z.Y.5
  • 150
    • 33745430441 scopus 로고    scopus 로고
    • An Alternative Approach to Amyloid Fibrils Morphology: CdSe/ZnS Quantum Dots Labelled β-Amyloid Peptide Fragments Abeta (31-35), Abeta (1-40) and Abeta (1-42)
    • Ji, X.; Naistat, D.; Li, C.; Orbulesco, J.; Leblanc, R. M. An Alternative Approach to Amyloid Fibrils Morphology: CdSe/ZnS Quantum Dots Labelled β-Amyloid Peptide Fragments Abeta (31-35), Abeta (1-40) and Abeta (1-42) Colloids Surf. B 2006, 50, 104-111
    • (2006) Colloids Surf. B , vol.50 , pp. 104-111
    • Ji, X.1    Naistat, D.2    Li, C.3    Orbulesco, J.4    Leblanc, R.M.5
  • 151
    • 70249141572 scopus 로고    scopus 로고
    • A Quantitative Fluorescence Study of Protein Monolayer Formation on Colloidal Nanoparticles
    • Rocker, C.; Potzl, M.; Zhang, F.; Parak, W. J.; Nienhaus, G. U. A Quantitative Fluorescence Study of Protein Monolayer Formation on Colloidal Nanoparticles Nat. Nanotechnol. 2009, 4, 577-580
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 577-580
    • Rocker, C.1    Potzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 153
    • 79959697473 scopus 로고    scopus 로고
    • Interaction of Silver Nanoparticles (SNPs) with Bacterial Extracellular Proteins (ECPs) and Its Adsorption Isotherms and Kinetics
    • Khan, S. S.; Srivatsan, P.; Vaishnavi, N.; Mukherjee, A.; Chandrasekaran, N. Interaction of Silver Nanoparticles (SNPs) with Bacterial Extracellular Proteins (ECPs) and Its Adsorption Isotherms and Kinetics J. Hazard. Mater. 2011, 192, 299-306
    • (2011) J. Hazard. Mater. , vol.192 , pp. 299-306
    • Khan, S.S.1    Srivatsan, P.2    Vaishnavi, N.3    Mukherjee, A.4    Chandrasekaran, N.5
  • 154
    • 80054045806 scopus 로고    scopus 로고
    • Measuring Protein Structure and Stability of Protein-Nanoparticle Systems with Synchrotron Radiation Circular Dichroism
    • Laera, S.; Ceccone, G.; Rossi, F.; Gilliland, D.; Hussain, R.; Siligardi, G.; Calzolai, L. Measuring Protein Structure and Stability of Protein-Nanoparticle Systems with Synchrotron Radiation Circular Dichroism Nano Lett. 2011, 11, 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
  • 155
    • 83455164598 scopus 로고    scopus 로고
    • Hardening of the Nanoparticle-Protein Corona in Metal (Au, Ag) and Oxide (Fe(3) O(4), CoO, and CeO(2)) Nanoparticles
    • Casals, E.; Pfaller, T.; Duschl, A.; Oostingh, G. J.; Puntes, V. F. Hardening of the Nanoparticle-Protein Corona in Metal (Au, Ag) and Oxide (Fe(3) O(4), CoO, and CeO(2)) Nanoparticles Small 2011, 7, 3479-3486
    • (2011) Small , vol.7 , pp. 3479-3486
    • Casals, E.1    Pfaller, T.2    Duschl, A.3    Oostingh, G.J.4    Puntes, V.F.5
  • 156
    • 84855815823 scopus 로고    scopus 로고
    • Study of Serum Interaction with a Cationic Nanoparticle: Implications for in Vitro Endocytosis, Cytotoxicity and Genotoxicity
    • Merhi, M.; Dombu, C. Y.; Brient, A.; Chang, J.; Platel, A.; Le Curieux, F.; Marzin, D.; Nesslany, F.; Betbeder, D. Study of Serum Interaction with a Cationic Nanoparticle: Implications for in Vitro Endocytosis, Cytotoxicity and Genotoxicity Int. J. Pharm. 2012, 423, 37-44
    • (2012) Int. J. Pharm. , vol.423 , pp. 37-44
    • Merhi, M.1    Dombu, C.Y.2    Brient, A.3    Chang, J.4    Platel, A.5    Le Curieux, F.6    Marzin, D.7    Nesslany, F.8    Betbeder, D.9
  • 157
    • 79952583790 scopus 로고    scopus 로고
    • Adsorption and Conformation of Serum Albumin Protein on Gold Nanoparticles Investigated Using Dimensional Measurements and in Situ Spectroscopic Methods
    • 10.1021/la104124d
    • Tsai, D. H.; Delrio, F. W.; Keene, A. M.; Tyner, K. M.; Maccuspie, R. I.; Cho, T. J.; Zachariah, M. R.; Hackley, V. A. Adsorption and Conformation of Serum Albumin Protein on Gold Nanoparticles Investigated Using Dimensional Measurements and in Situ Spectroscopic Methods Langmuir 2011, 10.1021/la104124d
    • (2011) Langmuir
    • 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
  • 158
    • 79959243546 scopus 로고    scopus 로고
    • Contrasting Effect of Gold Nanoparticles and Nanorods with Different Surface Modifications on the Structure and Activity of Bovine Serum Albumin
    • Chakraborty, S.; Joshi, P.; Shanker, V.; Ansari, Z. A.; Singh, S. P.; Chakrabarti, P. Contrasting Effect of Gold Nanoparticles and Nanorods with Different Surface Modifications on the Structure and Activity of Bovine Serum Albumin Langmuir 2011, 27, 7722-7731
    • (2011) Langmuir , vol.27 , pp. 7722-7731
    • Chakraborty, S.1    Joshi, P.2    Shanker, V.3    Ansari, Z.A.4    Singh, S.P.5    Chakrabarti, P.6
  • 159
    • 29844434629 scopus 로고    scopus 로고
    • Gold Nanoparticle-Cytochrome C Complexes: The Effect of Nanoparticle Ligand Charge on Protein Structure
    • Aubin-Tam, M. E.; Hamad-Schifferli, K. Gold Nanoparticle-Cytochrome C Complexes: The Effect of Nanoparticle Ligand Charge on Protein Structure Langmuir 2005, 21, 12080-12084
    • (2005) Langmuir , vol.21 , pp. 12080-12084
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 160
    • 34249899906 scopus 로고    scopus 로고
    • Probing Protein Adsorption onto Mercaptoundecanoic Acid Stabilized Gold Nanoparticles and Surfaces by Quartz Crystal Microbalance and Zeta-Potential Measurements
    • Kaufman, E. D.; Belyea, J.; Johnson, M. C.; Nicholson, Z. M.; Ricks, J. L.; Shah, P. K.; Bayless, M.; Pettersson, T.; Feldoto, Z.; Blomberg, E. et al. Probing Protein Adsorption onto Mercaptoundecanoic Acid Stabilized Gold Nanoparticles and Surfaces by Quartz Crystal Microbalance and Zeta-Potential Measurements Langmuir 2007, 23, 6053-6062
    • (2007) Langmuir , vol.23 , pp. 6053-6062
    • Kaufman, E.D.1    Belyea, J.2    Johnson, M.C.3    Nicholson, Z.M.4    Ricks, J.L.5    Shah, P.K.6    Bayless, M.7    Pettersson, T.8    Feldoto, Z.9    Blomberg, E.10
  • 162
    • 79952668032 scopus 로고    scopus 로고
    • Irreversible Changes in Protein Conformation Due to Interaction with Superparamagnetic Iron Oxide Nanoparticles
    • Mahmoudi, M.; Shokrgozar, M. A.; Sardari, S.; Moghadam, M. K.; Vali, H.; Laurent, S.; Stroeve, P. Irreversible Changes in Protein Conformation Due to Interaction with Superparamagnetic Iron Oxide Nanoparticles Nanoscale 2011, 3, 1127-1138
    • (2011) Nanoscale , vol.3 , pp. 1127-1138
    • Mahmoudi, M.1    Shokrgozar, M.A.2    Sardari, S.3    Moghadam, M.K.4    Vali, H.5    Laurent, S.6    Stroeve, P.7
  • 164
    • 78149366902 scopus 로고    scopus 로고
    • Serum Heat Inactivation Affects Protein Corona Composition and Nanoparticle Uptake
    • Lesniak, A.; Campbell, A.; Monopoli, M. P.; Lynch, I.; Salvati, A.; Dawson, K. A. Serum Heat Inactivation Affects Protein Corona Composition and Nanoparticle Uptake Biomaterials 2010, 31, 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
  • 165
    • 3843093727 scopus 로고    scopus 로고
    • Conformation and Orientation of a Protein Folding Intermediate Trapped by Adsorption
    • Engel, M. F.; Visser, A. J.; van Mierlo, C. P. Conformation and Orientation of a Protein Folding Intermediate Trapped by Adsorption Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 11316-11321
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11316-11321
    • Engel, M.F.1    Visser, A.J.2    Van Mierlo, C.P.3


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