Interaction of proteins with linear polyelectrolytes and spherical polyelectrolyte brushes in aqueous solution

Wittemann, Alexander; Ballauff, Matthias

doi:10.1039/b609879g

Cited by 171 publications

(290 citation statements)

References 54 publications

(180 reference statements)

Supporting

Mentioning

277

Contrasting

Unclassified

Order By: Relevance

“…This is due to the intrinsic amphiphilic character of the protein that facilitated the adsorption of protein onto similarly charged surfaces. 36 Hence, although the net charge of a protein is negative, positively charged patches on the protein surface are also present due to the heterogeneous distribution on the protein surface. 37,38 Park et al demonstrated positive charge patches in bovine serum albumin (BSA) (that is otherwise negatively charged), 39 allowing BSA to bind with a strong polyanion, as also observed in this work and in a previous report.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…32,38 The protein could also carry multiple positive charges and therefore be able to replace the counterions on a polymer surface. 32,36 In addition, albumin can also bind to the hydrophobic site of polymethacrylic acid. The binding between albumin and a hydrophobic surface is often used as a protein carrier for hydrophobic molecules, such as drugs.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media

Wiogo¹,

Lim

Bulmuş³

et al. 2012

Langmuir

View full text Add to dashboard Cite

Surface modification with linear polymethacrylic acid (20 kDa), linear and branched polyethylenimine (25 kDa), and branched oligoethylenimine (800 Da) is commonly used to improve the function of magnetite nanoparticles (MNPs) in many biomedical applications. These polymers were shown herein to have different adsorption capacity and anticipated conformations on the surface of MNPs due to differences in their functional groups, architectures, and molecular weight. This in turn affects the interaction of MNPs surfaces with biological serum proteins (fetal bovine serum). MNPs coated with 25 kDa branched polyethylenimine were found to attract the highest amount of serum protein while MNPs coated with 20 kDa linear polymethacrylic acid adsorbed the least. The type and amount of protein adsorbed, and the surface conformation of the polymer was shown to affect the size stability of the MNPs in a model biological media (RPMI-1640). A moderate reduction in r 2 relaxivity was also observed for MNPs suspended in RPMI-1640 containing serum protein compared to the same particles suspended in water. However, the relaxivities following protein adsorption are still relatively high making the use of these polymer-coated MNPs as Magnetic Resonance Imaging (MRI) contrast agents feasible. This work shows that through judicious selection of functionalization polymers and elucidation of the factors governing the stabilization mechanism, the design of nanoparticles for applications in biologically relevant conditions can be improved.

show abstract

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media

Wiogo¹,

Lim

Bulmuş³

et al. 2012

Langmuir

View full text Add to dashboard Cite

show abstract

“…Because of their complex structure proteins typically exhibit different affinities in different regions of their surface depending on the local composition of amino acid residues. An often applied concept is to divide the protein's surface into different patches or domains that can be of hydrophobic, hydrophilic, positively, or negatively charged nature [84][85][86]. Thus, on hydrophilic interfaces proteins predominantly expose those patches toward the surface that are rich of hydrophilic residues and on hydrophobic surfaces proteins direct their hydrophobic patches to the surface.…”

Section: Side-on or End-on? The Protein's Orientationmentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,354

1,289

View full text Add to dashboard Cite

Protein adsorption at solid surfaces plays a key role in many natural processes and has therefore promoted a widespread interest in many research areas. Despite considerable progress in this field there are still widely differing and even contradictive opinions on how to explain the frequently observed phenomena such as structural rearrangements, cooperative adsorption, overshooting adsorption kinetics, or protein aggregation. In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed. The main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions. Relevant experimental and computational strategies to practically approach the field of protein adsorption mechanisms and their impact on current successes are outlined.

show abstract

“…Moreover, the biological activity of the bound and redesorbed proteins and enzymes is nearly the same as in the native state [12]. Hence, spherical polyelectrolyte brushes present a well-defined model system for the study of protein adsorption [12].BSA solutions (15 g=l; Sigma A6003; Lot. : 045K7422) were prepared in a MES-buffer (2-N-morpholinoethane sulfonic acid) containing 2 mM NaN 3 to avoid microbial growth.…”

mentioning

confidence: 99%

Directed Motion of Proteins along Tethered Polyelectrolytes

et al. 2008

View full text Add to dashboard Cite

We present the first time-resolved investigation of motions of proteins in densely grafted layers of spherical polyelectrolyte brushes. Using small-angle x-ray scattering combined with rapid stopped-flow mixing, we followed the uptake of bovine serum albumin by poly(acrylic acid) layer with high spatial and temporal resolution. We find that the total amount of adsorbed protein scales with time as t 1=4 . This subdiffusive behavior is explained on the basis of directed motion of the protein along the polyelectrolyte chains. DOI: 10.1103/PhysRevLett.100.158301 PACS numbers: 82.35.Rs, 87.15.Vv The adsorption and immobilization of proteins from aqueous solutions onto solid surfaces is among the most important problems in biochemical research. Many biotechnological processes require immobilization of enzymes with full retention of their biological activity [1][2][3][4]. Reversible adsorption of proteins onto charged surfaces is involved in protein purification by ion exchange chromatography [5] and in many natural processes such as cell adhesion [3]. On the other hand, unspecific adsorption of proteins must be suppressed in many practical applications in order to prevent biofouling [6]. Very often, charged and uncharged polymers attached to surfaces are used to tune the interaction with proteins. Tethered chains of poly(ethylene oxide) are now widely used to prevent protein adsorption [7] while polyelectrolyte multilayers [8,9] or dense layers of polyelectrolytes [9][10][11] are utilized to immobilize proteins on surfaces.Despite numerous studies, little is known about the kinetics of protein adsorption and the self-organization of biomolecules with tethered polymer chains on a molecular level. Evidently, the kinetics of protein adsorption plays a major role in these processes [4,5,8,10 -13] and it is necessary to determine the position of the protein molecules on a molecular scale as a function of time. In this letter, we demonstrate for the first time that protein adsorption can be monitored directly with high temporal and spatial resolution on surface-modified colloidal spheres. We present the first study of the motion of a protein in a layer of tethered polyelectrolyte chains of a spherical polyelectrolyte brush [14] using time-resolved small-angle x-ray scattering (TR-SAXS) [15].Figure 1 schematically displays a colloidal particle composed of poly(styrene) spheres with chemically grafted chains of poly(acrylic acid). The grafting of the polyelectrolyte chains is dense, with the average distance of the chains on the surface much smaller than their contour length L c resulting in a spherical polyelectrolyte brush (SPB) [14]. The radius R of the cores of the SPB is 46 nm ( R 4%) and the thickness of the shell L is 58 nm ( L 25%). Here we study the spontaneous adsorption of bovine serum albumin (BSA). Despite the fact that both the SPB as well as the protein carry an overall negative charge, proteins can spontaneously adsorb onto these SPBs [12] at low ionic strength without inducing denaturation. Moreover, the...

show abstract

Interaction of proteins with linear polyelectrolytes and spherical polyelectrolyte brushes in aqueous solution

Cited by 171 publications

References 54 publications

Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media

Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media

Understanding protein adsorption phenomena at solid surfaces

Directed Motion of Proteins along Tethered Polyelectrolytes

Contact Info

Product

Resources

About