메뉴 건너뛰기




Volumn 120, Issue 20, 2016, Pages 4591-4599

Light Scattering Analysis of Mono- and Multi-PEGylated Bovine Serum Albumin in Solution: Role of Composition on Structure and Interactions

Author keywords

[No Author keywords available]

Indexed keywords

BODY FLUIDS; CHAINS; FUNCTIONAL MATERIALS; MAMMALS; POLYETHYLENE GLYCOLS; POLYETHYLENE OXIDES; PROTEINS; SOLUBILITY; SURFACE PLASMON RESONANCE;

EID: 84973468673     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.6b03097     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 80054996604 scopus 로고    scopus 로고
    • Effects of PEG size on structure, function and stability of PEGylated BSA
    • Plesner, B.; Fee, C. J.; Westh, P.; Nielsen, A. D. Effects of PEG size on structure, function and stability of PEGylated BSA Eur. J. Pharm. Biopharm. 2011, 79, 399-405 10.1016/j.ejpb.2011.05.003
    • (2011) Eur. J. Pharm. Biopharm. , vol.79 , pp. 399-405
    • Plesner, B.1    Fee, C.J.2    Westh, P.3    Nielsen, A.D.4
  • 2
    • 0035086519 scopus 로고    scopus 로고
    • Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon alpha-2a for the treatment of hepatitis C
    • Bailon, P.; Palleroni, A.; Schaffer, C. A.; Spence, C. L.; Fung, W. J.; Porter, J. E.; Ehrlich, G. K.; Pan, W.; Xu, Z. X.; Modi, M. W. et al. Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon alpha-2a for the treatment of hepatitis C Bioconjugate Chem. 2001, 12, 195-202 10.1021/bc000082g
    • (2001) Bioconjugate Chem. , vol.12 , pp. 195-202
    • Bailon, P.1    Palleroni, A.2    Schaffer, C.A.3    Spence, C.L.4    Fung, W.J.5    Porter, J.E.6    Ehrlich, G.K.7    Pan, W.8    Xu, Z.X.9    Modi, M.W.10
  • 3
    • 81255189103 scopus 로고    scopus 로고
    • The Conformation of the Poly(ethylene glycol) chain in Mono-PEGylated lysozyme and mono-PEGylated human growth hormone
    • Pai, S. S.; Hammouda, B.; Hong, K.; Pozzo, D. C.; Przybycien, T. M.; Tilton, R. D. The Conformation of the Poly(ethylene glycol) chain in Mono-PEGylated lysozyme and mono-PEGylated human growth hormone Bioconjugate Chem. 2011, 22, 2317-2323 10.1021/bc2003583
    • (2011) Bioconjugate Chem. , vol.22 , pp. 2317-2323
    • Pai, S.S.1    Hammouda, B.2    Hong, K.3    Pozzo, D.C.4    Przybycien, T.M.5    Tilton, R.D.6
  • 4
    • 0242585450 scopus 로고    scopus 로고
    • NMR structure of two novel polyethylene glycol conjugates of the human growth hormone-releasing factor, hGRF(1-29)-NH2
    • Digilio, G.; Barbero, L.; Bracco, C.; Corpillo, D.; Esposito, P.; Piquet, G.; Traversa, S.; Aime, S. NMR structure of two novel polyethylene glycol conjugates of the human growth hormone-releasing factor, hGRF(1-29)-NH2 J. Am. Chem. Soc. 2003, 125, 3458-3470 10.1021/ja021264j
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3458-3470
    • Digilio, G.1    Barbero, L.2    Bracco, C.3    Corpillo, D.4    Esposito, P.5    Piquet, G.6    Traversa, S.7    Aime, S.8
  • 5
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski, A.; van Es, T.; Palczuk, N. C.; Davis, F. F. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol J. Biol. Chem. 1977, 252, 3578-3581
    • (1977) J. Biol. Chem. , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    Van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 6
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese, F. M. Peptide and protein PEGylation: A review of problems and solutions Biomaterials 2001, 22, 405-417 10.1016/S0142-9612(00)00193-9
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 7
    • 84876811891 scopus 로고    scopus 로고
    • Analysis of heterogeneity in nonspecific PEGylation reactions of biomolecules
    • Hakem, I. F.; Leech, A. M.; Bohn, J.; Walker, J. P.; Bockstaller, M. R. Analysis of heterogeneity in nonspecific PEGylation reactions of biomolecules Biopolymers 2013, 99, 427-435 10.1002/bip.22193
    • (2013) Biopolymers , vol.99 , pp. 427-435
    • Hakem, I.F.1    Leech, A.M.2    Bohn, J.3    Walker, J.P.4    Bockstaller, M.R.5
  • 8
    • 78650258243 scopus 로고    scopus 로고
    • Analysis of monoPEGylated human galectin-2 by small-angle X-ray and neutron scattering: Concentration dependence of PEG conformation in the conjugate
    • He, L.; Wang, H.; Garamus, V. M.; Hanley, T.; Lensch, M.; Gabius, H. J.; Fee, C. J.; Middelberg, A. Analysis of monoPEGylated human galectin-2 by small-angle X-ray and neutron scattering: concentration dependence of PEG conformation in the conjugate Biomacromolecules 2010, 11, 3504-3510 10.1021/bm100999a
    • (2010) Biomacromolecules , vol.11 , pp. 3504-3510
    • He, L.1    Wang, H.2    Garamus, V.M.3    Hanley, T.4    Lensch, M.5    Gabius, H.J.6    Fee, C.J.7    Middelberg, A.8
  • 9
    • 84876000039 scopus 로고    scopus 로고
    • Peptide-polymer conjugates: From fundamental science to application
    • Shu, J. Y.; Panganiban, B.; Xu, T. Peptide-polymer conjugates: from fundamental science to application Annu. Rev. Phys. Chem. 2013, 64, 631-657 10.1146/annurev-physchem-040412-110108
    • (2013) Annu. Rev. Phys. Chem. , vol.64 , pp. 631-657
    • Shu, J.Y.1    Panganiban, B.2    Xu, T.3
  • 11
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins
    • Fee, C. J.; Van Alstine, J. M. Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins Bioconjugate Chem. 2004, 15, 1304-1313 10.1021/bc049843w
    • (2004) Bioconjugate Chem. , vol.15 , pp. 1304-1313
    • Fee, C.J.1    Van Alstine, J.M.2
  • 12
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris, J. M.; Chess, R. B. Effect of pegylation on pharmaceuticals Nat. Rev. Drug Discovery 2003, 2, 214-221 10.1038/nrd1033
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 13
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • Roberts, M. J.; Bentley, M. D.; Harris, J. M. Chemistry for peptide and protein PEGylation Adv. Drug Delivery Rev. 2002, 54, 459-476 10.1016/S0169-409X(02)00022-4
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 459-476
    • Roberts, M.J.1    Bentley, M.D.2    Harris, J.M.3
  • 14
    • 0037343959 scopus 로고    scopus 로고
    • Site-specific PEGylation of hemoglobin at Cys-93(beta): Correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain
    • Manjula, B. N.; Tsai, A.; Upadhya, R.; Perumalsamy, K.; Smith, P. K.; Malavalli, A.; Vandegriff, K.; Winslow, R. M.; Intaglietta, M.; Prabhakaran, M. et al. Site-specific PEGylation of hemoglobin at Cys-93(beta): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain Bioconjugate Chem. 2003, 14, 464-472 10.1021/bc0200733
    • (2003) Bioconjugate Chem. , vol.14 , pp. 464-472
    • Manjula, B.N.1    Tsai, A.2    Upadhya, R.3    Perumalsamy, K.4    Smith, P.K.5    Malavalli, A.6    Vandegriff, K.7    Winslow, R.M.8    Intaglietta, M.9    Prabhakaran, M.10
  • 17
    • 33749234394 scopus 로고    scopus 로고
    • Extension arm facilitated PEGylation of hemoglobin: Correlation of the properties with the extent of PEGylation
    • Li, D.; Manjula, B. N.; Acharya, A. S. Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation Protein J. 2006, 25, 263-274 10.1007/s10930-006-9010-y
    • (2006) Protein J. , vol.25 , pp. 263-274
    • Li, D.1    Manjula, B.N.2    Acharya, A.S.3
  • 18
    • 84938629639 scopus 로고    scopus 로고
    • Conformation of the Poly(ethylene Glycol) chains in DiPEGylated hemoglobin specifically probed by SANS: Correlation with PEG length and in vivo efficiency
    • Le Cœur, C.; Combet, S.; Carrot, G.; Busch, P.; Teixeira, J.; Longeville, S. Conformation of the Poly(ethylene Glycol) chains in DiPEGylated hemoglobin specifically probed by SANS: correlation with PEG length and in vivo efficiency Langmuir 2015, 31, 8402-8410 10.1021/acs.langmuir.5b01121
    • (2015) Langmuir , vol.31 , pp. 8402-8410
    • Le Cœur, C.1    Combet, S.2    Carrot, G.3    Busch, P.4    Teixeira, J.5    Longeville, S.6
  • 19
    • 0001516764 scopus 로고    scopus 로고
    • Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution
    • Haas, C.; Drenth, J.; Wilson, W. W. Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution J. Phys. Chem. B 1999, 103, 2808-2811 10.1021/jp984035l
    • (1999) J. Phys. Chem. B , vol.103 , pp. 2808-2811
    • Haas, C.1    Drenth, J.2    Wilson, W.W.3
  • 20
    • 84905442057 scopus 로고    scopus 로고
    • Applications of the second virial coefficient: Protein crystallization and solubility
    • Wilson, W. W.; DeLucas, L. J. Applications of the second virial coefficient: Protein crystallization and solubility Acta Crystallogr., Sect. F: Struct. Biol. Commun. 2014, 70, 543-554 10.1107/S2053230X1400867X
    • (2014) Acta Crystallogr., Sect. F: Struct. Biol. Commun. , vol.70 , pp. 543-554
    • Wilson, W.W.1    DeLucas, L.J.2
  • 21
    • 33750343814 scopus 로고    scopus 로고
    • Supramolecular structures in aqueous solutions of rigid polyelectrolytes with monovalent and divalent counterions
    • Kroeger, A.; Belack, J.; Larsen, A.; Fytas, G.; Wegner, G. Supramolecular structures in aqueous solutions of rigid polyelectrolytes with monovalent and divalent counterions Macromolecules 2006, 39, 7098-7106 10.1021/ma061228v
    • (2006) Macromolecules , vol.39 , pp. 7098-7106
    • Kroeger, A.1    Belack, J.2    Larsen, A.3    Fytas, G.4    Wegner, G.5
  • 22
    • 32644472469 scopus 로고    scopus 로고
    • Characterizing the modification of surface proteins with poly(ethylene glycol) to interrupt platelet adhesion
    • Xu, H.; Kaar, J. L.; Russell, A. J.; Wagner, W. R. Characterizing the modification of surface proteins with poly(ethylene glycol) to interrupt platelet adhesion Biomaterials 2006, 27, 3125-3135 10.1016/j.biomaterials.2006.01.012
    • (2006) Biomaterials , vol.27 , pp. 3125-3135
    • Xu, H.1    Kaar, J.L.2    Russell, A.J.3    Wagner, W.R.4
  • 24
    • 77649110057 scopus 로고    scopus 로고
    • A Quantitative assessment of nanoparticle-ligand distributions: Implications for targeted drug and imaging delivery in dendrimer conjugates
    • Mullen, D. G.; Fang, M.; Desai, A.; Baker, J. R.; Orr, B. G.; Banaszak Holl, M. A Quantitative assessment of nanoparticle-ligand distributions: Implications for targeted drug and imaging delivery in dendrimer conjugates ACS Nano 2010, 4, 657-670 10.1021/nn900999c
    • (2010) ACS Nano , vol.4 , pp. 657-670
    • Mullen, D.G.1    Fang, M.2    Desai, A.3    Baker, J.R.4    Orr, B.G.5    Banaszak Holl, M.6
  • 25
    • 47349120456 scopus 로고    scopus 로고
    • Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements
    • Jachimska, B.; Wasilewska, M.; Adamczyk, Z. Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements Langmuir 2008, 24, 6866-6872 10.1021/la800548p
    • (2008) Langmuir , vol.24 , pp. 6866-6872
    • Jachimska, B.1    Wasilewska, M.2    Adamczyk, Z.3
  • 26
    • 0033891708 scopus 로고    scopus 로고
    • Attachment of functionalized Poly(ethylene glycol) films to gold surfaces
    • Lu, H.; Campbell, C. T.; Castner, D. G. Attachment of functionalized Poly(ethylene glycol) films to gold surfaces Langmuir 2000, 16, 1711 10.1021/la990221m
    • (2000) Langmuir , vol.16 , pp. 1711
    • Lu, H.1    Campbell, C.T.2    Castner, D.G.3
  • 28
    • 34250919425 scopus 로고
    • Die beugung von röntgenstrahlen in flüssigkeiten als effekt der molekülanordnung
    • Zernike, F.; Prins, J. A. Die beugung von röntgenstrahlen in flüssigkeiten als effekt der molekülanordnung Z. Phys. 1927, 41, 184-194 10.1007/BF01391926
    • (1927) Z. Phys. , vol.41 , pp. 184-194
    • Zernike, F.1    Prins, J.A.2
  • 29
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George, A.; Wilson, W. W. Predicting protein crystallization from a dilute solution property Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50, 361-365 10.1107/S0907444994001216
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 30
    • 0001167738 scopus 로고
    • Osmotic virial coefficients of aqueous Poly(ethylene glycol) from laser-light scattering and isopiestic measurements
    • Hasse, H.; Kany, H. P.; Tintinger, R.; Maurer, G. Osmotic virial coefficients of aqueous Poly(ethylene glycol) from laser-light scattering and isopiestic measurements Macromolecules 1995, 28, 3540-3552 10.1021/ma00114a007
    • (1995) Macromolecules , vol.28 , pp. 3540-3552
    • Hasse, H.1    Kany, H.P.2    Tintinger, R.3    Maurer, G.4
  • 31
    • 33644694594 scopus 로고    scopus 로고
    • Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures
    • Bloustine, J.; Virmani, T.; Thurston, G. M.; Fraden, S. Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures Phys. Rev. Lett. 2006, 96, 087803 10.1103/PhysRevLett.96.087803
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 087803
    • Bloustine, J.1    Virmani, T.2    Thurston, G.M.3    Fraden, S.4
  • 32
    • 0002232436 scopus 로고
    • Über das lösungsverhalten von nylon 6,6
    • von Elias, H.-G.; Schumacher, R. Über das lösungsverhalten von nylon 6,6 Makromol. Chem. 1964, 76, 23-53 10.1002/macp.1964.020760103
    • (1964) Makromol. Chem. , vol.76 , pp. 23-53
    • Von Elias, H.-G.1    Schumacher, R.2
  • 33
    • 84964355234 scopus 로고    scopus 로고
    • Structure and dynamics of dendronized polymer solutions: Gaussian coil or macromolecular rod?
    • Dutertre, F.; Bang, K. T.; Loppinet, B.; Choi, I.; Choi, T.; Fytas, G. Structure and dynamics of dendronized polymer solutions: gaussian coil or macromolecular rod? Macromolecules 2016, 49, 2731-2740 10.1021/acs.macromol.6b00420
    • (2016) Macromolecules , vol.49 , pp. 2731-2740
    • Dutertre, F.1    Bang, K.T.2    Loppinet, B.3    Choi, I.4    Choi, T.5    Fytas, G.6
  • 34
    • 0000856458 scopus 로고
    • Mouvement brownien d'un ellipsoïde, 1: Dispersion diélectrique pour des molécules ellipsoïde
    • Perrin, F. Mouvement brownien d'un ellipsoïde, 1: Dispersion diélectrique pour des molécules ellipsoïde J. Phys. Radium 1934, 5, 497-511 10.1051/jphysrad:01934005010049700
    • (1934) J. Phys. Radium , vol.5 , pp. 497-511
    • Perrin, F.1
  • 35
    • 0031193807 scopus 로고    scopus 로고
    • Branched and linear poly(ethylene glycol): Influence of the polymer structure on enzymological, pharmacokinetic and immunological properties of protein conjugates
    • Veronese, F.; Caliceti, P.; Schiavon, O. Branched and linear poly(ethylene glycol): influence of the polymer structure on enzymological, pharmacokinetic and immunological properties of protein conjugates J. Bioact. Compat. Polym. 1997, 12, 196-207
    • (1997) J. Bioact. Compat. Polym. , vol.12 , pp. 196-207
    • Veronese, F.1    Caliceti, P.2    Schiavon, O.3
  • 36
    • 84964649209 scopus 로고    scopus 로고
    • Processing fragile matter: Effect of polymer graft modification on the mechanical properties and processibility of (nano-) particulate solids
    • Schmitt, M.; Choi, J.; Hui, C. M.; Chen, B.; Korkmaz, E.; Yan, J.; Margel, S.; Ozdoganlar, O. B.; Matyjaszewski, K.; Bockstaller, M. R. Processing fragile matter: Effect of polymer graft modification on the mechanical properties and processibility of (nano-) particulate solids Soft Matter 2016, 12, 3527-3537 10.1039/C6SM00095A
    • (2016) Soft Matter , vol.12 , pp. 3527-3537
    • Schmitt, M.1    Choi, J.2    Hui, C.M.3    Chen, B.4    Korkmaz, E.5    Yan, J.6    Margel, S.7    Ozdoganlar, O.B.8    Matyjaszewski, K.9    Bockstaller, M.R.10
  • 37
    • 84858992651 scopus 로고    scopus 로고
    • Toughening fragile matter: Mechanical properties of particle solids assembled from polymer-grafted hybrid particles synthesized by ATRP
    • Choi, J.; Hui, C. M.; Pietrasik, J.; Dong, H.; Matyjaszewski, K.; Bockstaller, M. R. Toughening fragile matter: Mechanical properties of particle solids assembled from polymer-grafted hybrid particles synthesized by ATRP Soft Matter 2012, 8, 4072-4078 10.1039/c2sm06915f
    • (2012) Soft Matter , vol.8 , pp. 4072-4078
    • Choi, J.1    Hui, C.M.2    Pietrasik, J.3    Dong, H.4    Matyjaszewski, K.5    Bockstaller, M.R.6
  • 38
    • 84892576110 scopus 로고    scopus 로고
    • Surface-initiated polymerization as an enabling tool for multifunctional (nano-)engineered hybrid materials
    • Hui, C. M.; Pietrasik, J.; Schmitt, M.; Mahoney, C.; Choi, J.; Bockstaller, M. R.; Matyjaszewski, K. Surface-initiated polymerization as an enabling tool for multifunctional (nano-)engineered hybrid materials Chem. Mater. 2014, 26, 745-472 10.1021/cm4023634
    • (2014) Chem. Mater. , vol.26 , pp. 472-745
    • Hui, C.M.1    Pietrasik, J.2    Schmitt, M.3    Mahoney, C.4    Choi, J.5    Bockstaller, M.R.6    Matyjaszewski, K.7
  • 39
    • 84879107865 scopus 로고    scopus 로고
    • Fluctuation-driven anisotropic assembly in nanoscale systems
    • Bozorgui, B.; Meng, D.; Kumar, S. K.; Chakravarty, C.; Cacciouto, A. Fluctuation-driven anisotropic assembly in nanoscale systems Nano Lett. 2013, 13, 2732-2737 10.1021/nl401378r
    • (2013) Nano Lett. , vol.13 , pp. 2732-2737
    • Bozorgui, B.1    Meng, D.2    Kumar, S.K.3    Chakravarty, C.4    Cacciouto, A.5
  • 40
    • 84927608155 scopus 로고    scopus 로고
    • Effects of functional groups and ionization on the structure of alkanethiol-coated gold nanoparticles
    • Bolintineanu, D. S.; Lane, M. D.; Grest, G. S. Effects of functional groups and ionization on the structure of alkanethiol-coated gold nanoparticles Langmuir 2014, 30, 11075-11085 10.1021/la502795z
    • (2014) Langmuir , vol.30 , pp. 11075-11085
    • Bolintineanu, D.S.1    Lane, M.D.2    Grest, G.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.