Protein adsorption on and swelling of polyelectrolyte brushes: A simultaneous ellipsometry-quartz crystal microbalance study

Biointerphases - 2010
Eva Bittrich1, Keith B. Rodenhausen2, Klaus‐Jochen Eichhorn1, Tino Hofmann3, M. Schubert3, Manfred Stamm1, Petra Uhlmann1
1Leibniz Institute of Polymer Research Dresden 1 , Hohe Str. 6, Dresden, 1069, Germany
2University of Nebraska-Lincoln 2 Department of Chemical and Biomolecular Engineering, , 207 Othmer Hall, Lincoln, Nebraska 68588-0643, USA
3University of Nebraska-Lincoln 3 Department of Electrical Engineering, , 209N Scott Engineering Center, P.O. Box 880511, Lincoln, Nebraska 68588-0511, USA

Tóm tắt

With a coupled spectroscopic ellipsometry-quartz crystal microbalance with dissipation (QCM-D) experimental setup, quantitative information can be obtained about the amount of buffer components (water molecules and ions) coupled to a poly(acrylic acid) (PAA) brush surface in swelling and protein adsorption processes. PAA Guiselin brushes with more than one anchoring point per single polymer chain were prepared. For the swollen brushes a high amount of buffer was found to be coupled to the brush-solution interface in addition to the content of buffer inside the brush layer. Upon adsorption of bovine serum albumin the further incorporation of buffer molecules into the protein-brush layer was monitored at overall electrostatic attractive conditions [below the protein isolectric poimt (IEP)] and electrostatic repulsive conditions (above the protein IEP), and the shear viscosity of the combined polymer-protein layer was evaluated from QCM-D data. For adsorption at the “wrong side” of the IEP an incorporation of excess buffer molecules was observed, indicating an adjustment of charges in the combined polymer-protein layer. Desorption of protein at pH 7.6 led to a very high stretching of the polymer-protein layer with additional incorporation of high amounts of buffer, reflecting the increase of negative charges on the protein molecules at this elevated pH.

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Tài liệu tham khảo

2002, Science, 297, 964, 10.1126/science.1075997

2010, Nature Mater., 9, 101, 10.1038/nmat2614

2006, Prog. Org. Coat., 55, 168, 10.1016/j.porgcoat.2005.09.014

2008, Annu. Rev. Phys. Chem., 59, 493, 10.1146/annurev.physchem.59.032607.093623

2007, J. Polym. Sci., Part A: Polym. Chem., 45, 3505, 10.1002/pola.22180

2006, Phys. Chem. Chem. Phys., 8, 3815, 10.1039/b606415a

2003, Adv. Colloid Interface Sci., 100–102, 205, 10.1016/S0001-8686(02)00061-1

2000, Langmuir, 16, 8324, 10.1021/la991528o

2007, J. Phys. Chem. B, 111, 979, 10.1021/jp065585j

2001, Phys. Rev. E, 64, 051406, 10.1103/PhysRevE.64.051406

2010, Langmuir, 26, 12926, 10.1021/la101762f

2006, Curr. Opin. Colloid Interface Sci., 11, 316, 10.1016/j.cocis.2006.12.002

2005, Macromolecules, 38, 4855, 10.1021/ma047501f

2004, Phys. Rev. E, 70, 061403, 10.1103/PhysRevE.70.061403

2006, Phys. Rev. E, 73, 011802, 10.1103/PhysRevE.73.011802

2007, Langmuir, 23, 1347, 10.1021/la061881b

2008, Langmuir, 24, 6575, 10.1021/la8006469

2010, Langmuir, 26, 249, 10.1021/la902079u

2010, J. Am. Chem. Soc., 132, 3159, 10.1021/ja909938c

2010, J. Polym. Sci., Part B: Polym. Phys., 48, 1606, 10.1002/polb.22021

1999, Colloids Surf., A, 156, 3, 10.1016/S0927-7757(99)00007-2

2009, Colloids Surf., B, 69, 169, 10.1016/j.colsurfb.2008.11.025

1978, Biopolymers, 17, 1759, 10.1002/bip.1978.360170711

1959, Z. Phys., 155, 206, 10.1007/BF01337937

1995, Rev. Sci. Instrum., 66, 3924, 10.1063/1.1145396

1997, J. Phys.: Condens. Matter, 9, 7799, 10.1088/0953-8984/9/37/011

2002, Biosens. Bioelectron., 17, 835, 10.1016/S0956-5663(02)00050-7

2008, Macromolecules, 41, 8124, 10.1021/ma8009307

2010, Soft Matter, 6, 937, 10.1039/b918586k

2009, Langmuir, 25, 10014, 10.1021/la900751w

2001, Anal. Chem., 73, 5796, 10.1021/ac0106501

1997, Phys. Rev. E, 56, 680, 10.1103/PhysRevE.56.680

2004, Langmuir, 20, 1739, 10.1021/la035475t

1996, Macromolecules, 29, 7261, 10.1021/ma9604348

2009, Polym. Mater. Sci. Eng., 101, 930

1992, Chem. Rev. (Washington, D.C.), 92, 1355, 10.1021/cr00014a006

1972, J. Biochem. (Tokyo), 71, 705

1982, Thin Solid Films, 89, 249, 10.1016/0040-6090(82)90590-9

1986, Appl. Spectrosc., 40, 313, 10.1366/0003702864509204

2002, Langmuir, 18, 9924, 10.1021/la020473e

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