self-assembly in solution; micelle; stimuli responsive micelle
Abstract :
[en] We have studied the formation and the stability of grafted block complex coacervate core micelles (C3Ms) in solution and the influence of grafted block C3M coatings on the adsorption of the proteins beta-lactoglobulin, bovine serum albumin, and lysozyme. The C3Ms consist of a grafted block copolymer PAA(21)-b-PAPEO(14) (poly(acrylic acid)-b-poly(acrylate methoxy poly(ethylene oxide)), with a negatively charged PAA block and a neutral PAPEO block and a positively charged homopolymer P2MVPI (poly(N-methyl 2-vinyl pyridinium iodide). In solution, these C3Ms partly disintegrate at salt concentrations between 50 and 100 mM NaCl. Adsorption of C3Ms and proteins has been studied with fixed-angle optical reflectometry, at salt concentrations ranging from 1 to 100 mM NaCl. In comparison with the adsorption of PAA(21)-b-PAPEO(14) alone adsorption of C3Ms significantly increases the amount of PAA(21)-b-PAPEO(14) on the surface. This results in a higher surface density of PEO chains. The stability of the C3M coatings and their influence on protein adsorption are determined by the composition and the stability of the C3Ms in solution. A C3M-PAPEO(14)/P2MVPI(43) coating strongly suppresses the adsorption of all proteins on silica and polystyrene. The reduction of protein adsorption is the highest at 100 mM NaCl (> 90%). The adsorbed C3M-PAPEO(14)/P2MVPI(43) layer is partly removed from the surface upon exposure to an excess of beta-lactoglobulin solution, due to formation of soluble aggregates consisting of beta-lactoglobulin and P2MVPI(43). In contrast, C3M-PAPEO(14)/P2MVPI(228) which has a fivefold longer cationic block enhances adsorption of the negatively charged proteins on both surfaces at salt concentrations above 1 mM NaCl. A single PAA(21)-b-PAPEO(14) layer causes only a moderate reduction of protein adsorption.
Research Center/Unit :
Center for Education and Research on Macromolecules (CERM)
Disciplines :
Materials science & engineering Chemistry
Author, co-author :
Brzozowska, Agata M.; Wetsus, Centre of Excellence for Sustainable Water Technology, Leeuwarden, The Netherlands
de Keizer, Arie; Wageningen University, The Netherlands > Laboratory of Physical Chemistry and Colloid Science,
Norde, Willem; University Medical Center Groningen and University of Groningen, The Netherlands
Detrembleur, Christophe ; Université de Liège - ULiège > Department of Chemistry > Center for Education and Research on Macromolecules (CERM)
Cohen Stuart, Martien A.; Wageningen University, The Netherlands > Laboratory of Physical Chemistry and Colloid Science
Language :
English
Title :
Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene
Halperin A (1999) Polymer brushes that resist adsorption of model proteins: design parameters. Langmuir 15 (7):2525-2533
Brzozowska AM, Hofs B, de Keizer A, Fokkink R, Cohen Stuart MA, Norde W (2009) Reduction of protein adsorption on silica and polystyrene surfaces due to coating with complex coacervate core micelles. Colloids Surf A Physicochem Eng Asp 347:146-155
Hofs B, Brzozowska A, de Keizer A, Norde W, Cohen Stuart MA (2008) Reduction of protein adsorption to a solid surface by a coating composed of polymeric micelles with a glass-like core. J Colloid Interface Sci 325 (2):309-315
van der Burgh S, Fokkink R, de Keizer A, Cohen Stuart MA (2004) Complex coacervation core micelles as anti-fouling agents on silica and polystyrene surfaces. Colloids Surf A Physicochem Eng Asp 242 (1-3): 167-174
Cohen Stuart MA, Besseling N A M, Fokkink RG (1998) Formation of micelles with complex coacervate cores. Langmuir 14:6846-6849
Kabanov AV, Bronich TK, Kabanov VA, Yu K, Eisenberg A (1996) Soluble stoichiometric complexes from poly (N-ethyl-4-vinylpyridinium) cations and poly (ethylene oxide)-block-polymethacrylate anions. Macromolecules 29 (21):6797-6802
Kataoka K, Togawa H, Harada A, Yasugi K, Matsumoto T, Katayose S (1996) Spontaneous formation of polyion complex micelles with narrow distribution from antisense oligonucleotide and cationic block copolymer in physiological saline. Macromolecules 29 (26):8556-8557
Borisov OV, Zhulina EB (2002) Effect of salt on self-assembly in charged block copolymer micelles. Macromolecules 35 (11):4472-4480
van der Burgh S, de Keizer A, Cohen Stuart MA (2004) Complex coacervation core micelles. Colloidal stability and aggregation mechanism. Langmuir 20 (4):1073-1084
Voets IK, de Vos WA, Hofs B, de Keizer A, Cohen Stuart MA, Steitz R, Lott D (2008) Internal structure of a thin film of mixed polymeric micelles on a solid/liquid interface. J Phys Chem B 112 (23):6937-6945
Pasche S, De Paul SM, Voros J, Spencer ND, Textor M (2003) Poly (L-lysine)-graft-poly (ethylene glycol) assembled monolayers on niobium oxide surfaces: a quantitative study of the influence of polymer interfacial architecture on resistance to protein adsorption by ToF-SIMS and in situ OWLS. Langmuir 19 (22):9216-9225
Vande Vondele S, Voros J, Hubbell JA (2003) RGD-Grafted polyl-lysine-graft-(polyethylene glycol) copolymers block non-specific protein adsorption while promoting cell adhesion. Biotechnol Bioeng 82 (7):784-790
Zhang ZP, Ma HW, Hausner DB, Chilkoti A, Beebe TP (2005) Pretreatment of amphiphilic comb polymer surfaces dramatically affects protein adsorption. Biomacromolecules 6 (6):3388-3396
Aquil A, Vasseur S, Duguet E, Passirani C, Benoît JP, Roch A R M, Jérôme R, Jérôme C (2008) PEO coated magnetic nanoparticles for biomedical application. Eur Polym J 44:3191-3199
Burton WG, Nugent KD, Slattery TK, Summers BR, Snyder LR (1988) Separation of proteins by reversed-phase high-performance liquid-chromatography. 1. Optimizing the column. J Chromatogr 443:363-379
Wong D W S, Camirand WM, Pavlath AE (1996) Structures and functionalities of milk proteins. Crit Rev Food Sci Nutr 36 (8):807-844
Bosma JC, Wesselingh JA (1998) pH dependence of ion-exchange equilibrium of proteins. AIChE J 44 (11):2399-2409
Marsh RJ, Jones R A L, Sferrazza M (2002) Adsorption and displacement of a globular protein on hydrophilic and hydrophobic surfaces. Colloids Surf B Biointerfaces 23 (1):31-42
Tarasevich YI, Monakhova LI (2002) Interaction between globular proteins and silica surfaces. Colloid J 64 (4):482-487
Bachmann L, Schmittfumian WW, Hammel R, Lederer K (1975) Size and shape of fibrinogen. 1. Electron-microscopy of hydrated molecule. Makromol Chem-Macromol Chem Phys 176 (9):2603-2618
Hirayama K, Akashi S, Furuya M, Fukuhara K (1990) Rapid confirmation and revision of the primary structure of bovine serum-albumin by esims and Frit-Fab Lc Ms. Biochem Biophys Res Commun 173 (2):639-646
Voets IK, de Vries R, Fokkink R, Sprakel J, May RP, de Keizer A, Cohen Stuart MA (2009) Towards a structural characterization of charge-driven polymer micelles. Eur Phys J E 30 (4):351-359
Currie E P K, Sieval AB, Avena M, Zuilhof H, Sudholter E J R, Cohen Stuart MA (1999) Weak polyacid brushes: preparation by LB deposition and optically detected titrations. Langmuir 15 (21):7116-7118
Sieval AB, Demirel AL, Nissink J W M, Linford MR, van der Maas JH, de Jeu WH, Zuilhof H, Sudholter E J R (1998) Highly stable Si-C linked functionalized monolayers on the silicon (100) surface. Langmuir 14 (7):1759-1768
Dijt JC, Cohen Stuart MA, Hofman JE, Fleer GJ (1990) Kinetics of polymer adsorption in stagnation point flow. Colloids Surf 51:141-158
Cooper CL, Goulding A, Kayitmazer AB, Ulrich S, Stoll S, Turksen S, Yusa S, Kumar A, Dubin PL (2006) Effects of polyelectrolyte chain stiffness, charge mobility, and charge sequences on binding to proteins and micelles. Biomacromolecules 7 (4):1025-1035
Kabanov VA, Evdakov VP, Mustafaev MI, Antipina AD (1977) Cooperative bonding of serum-albumin by quaternized poly-4-vinylpyridines and structure of complexes formed. Mol Biol 11 (3):443-454
Kayitmazer AB, Seyrek E, Dubin PL, Staggemeier BA (2003) Influence of chain stiffness on the interaction of polyelectrolytes with oppositely charged micelles and proteins. J Phys Chem B 107 (32):8158-8165
Morawetz H, Hughes WL (1952) The interaction of proteins with synthetic polyelectrolytes. 1. Complexing of bovine serum albumin. J Phys Chem 56 (1):64-69
Matsunami H, Kikuchi R, Ogawa K, Kokufuta E (2007) Light scattering study of complex formation between protein and polyelectrolyte at various ionic strengths. Colloids Surf B Biointerfaces 56:142-148 (Pubitemid 46467303)
Seyrek E, Dubin PL, Tribet C, Gamble EA (2003) Ionic strength dependence of protein-polyelectrolyte interactions. Biomacromolecules 4 (2):273-282
Hallberg RK, Dubin PL (1998) Effect of pH on the binding of beta-lactoglobulin to sodium polystyrenesulfonate. J Phys Chem B 102 (43):8629-8633
de Vos WM, Biesheuvel PM, de Keizer A, Kleijn JM, Cohen Stuart MA (2008) Adsorption of the protein bovine serum albumin in a planar poly (acrylic acid) brush layer as measured by optical reflectometry. Langmuir 24 (13):6575-6584
Xia JL, Dubin PL, Kim Y, Muhoberac BB, Klimkowski VJ (1993) Electrophoretic and quasi-elastic light-scattering of solubleprotein polyelectrolyte complexes. J Phys Chem 97 (17):4528-4534
Menon MK, Zydney AL (1998) Measurement of protein charge and ion binding using capillary electrophoresis. Anal Chem 70 (8):1581-1584
Kovacevic D, van der Burgh S, de Keizer A, Cohen Stuart MA (2002) Kinetics of formation and dissolution of weak polyelectrolyte multilayers: role of salt and free polyions. Langmuir 18 (14):5607-5612
Norde W, Favier JP (1992) Structure of adsorbed and desorbed proteins. Colloids Surf 64 (1):87-93
Norde W, Gonzalez FG, Haynes CA (1995) Protein adsorption on polystyrene latex-particles. Polym Adv Technol 6 (7):518-525