History dependence of protein adsorption kinetics

Calonder, Claudio; Tie, Yanrong; Tassel, Paul R. Van

doi:10.1073/pnas.181337298

Cited by 115 publications

(109 citation statements)

References 41 publications

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“…OWLS requires planar, optically transparent substrates such as quartz or Si(Ti)O 2 but no metal layer coating. Probably due to its high sensitivity and easy handling this technique has been used for numerous studies of protein adsorption kinetics [103,142,151,152,218,219].…”

Section: Optical Waveguide Lightmode Spectroscopy (Owls) Is Based On mentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,385

1,239

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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.

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Section: Optical Waveguide Lightmode Spectroscopy (Owls) Is Based On mentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,385

1,239

View full text Add to dashboard Cite

show abstract

“…carry both hydrophilic and hydrophobic parts) and these features make the thermodynamics of their interactions with a surface particularly rich and extensively studied [2]. Studies of the dynamics of adsorbed proteins mainly focus on adsorption kinetics that may take place in a few tens of minutes[3] but sometime is much slower, history dependent and displays some irreversible features [4,5]. In these latter cases, the slow dynamics is viewed as inherent to the random addition of new molecules onto the surface and described in terms of the Random Sequential Adsorption (RSA) model[6] that displays slow dynamics typical of glass or jamming transition.…”

Section: Pacs Numbersmentioning

confidence: 99%

Slow and remanent electric polarization of adsorbed BSA layer evidenced by neutron reflection

et al. 2012

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Using neutron reflectivity together with an appropriate electrochemical cell, we have studied the effects of transverse electric field on the Bovine Serum Albumin (BSA) monolayer initially adsorbed at the interface of the aqueous solution and a conductive doped-silicon wafer. Depending on the sign of the initial potential, a second layer is adsorbed or not on top of the first whereas a subsequent reversal of potential has no effect. We show that this behaviour reveals the slow and remanent electric polarization of the first BSA layer. Based on the permanent dipolar structure of BSA, we suggest an analogy with dipolar glasses that may account for the slowness and memory of the process. PACS numbers:Protein adsorption on solid surfaces is a fundamental phenomenon that plays a central role in biotechnology; e.g.for biomaterials and biocompatibility improvement [1]. Proteins are polyampholytes (i.e. carry both positive and negative charges) and amphiphiles (i.e. carry both hydrophilic and hydrophobic parts) and these features make the thermodynamics of their interactions with a surface particularly rich and extensively studied [2]. Studies of the dynamics of adsorbed proteins mainly focus on adsorption kinetics that may take place in a few tens of minutes[3] but sometime is much slower, history dependent and displays some irreversible features [4,5]. In these latter cases, the slow dynamics is viewed as inherent to the random addition of new molecules onto the surface and described in terms of the Random Sequential Adsorption (RSA) model[6] that displays slow dynamics typical of glass or jamming transition. The counterpart of this jammed behaviour is the slow relaxation of the in-plane density of the adsorbed layer after an external perturbation or spontaneous fluctuations [7]. Much less studied and also presumably quite different are external perturbations that retain the density constant but should in principle operate on the orientation of adsorbed molecules, although this handling of adsorbed layer has many practical significances, e.g. for immobilized enzymes, immunoassays and biosensors. Due to the electrical charges of proteins, electrical stimuli are the most obvious with respect to this orientation. But studies in this direction are still sparse [8][9][10][11] and only concerned up to now with ellipsometry or electrochemical measurements, which produce ambiguous results due to technical limitations [12].In this paper, we report a neutron reflectivity study on the effects of transverse electric field on a Bovine Serum Albumin (BSA) monolayer initially adsorbed at silicon/water interface. Our results show a slow and remanent polarization of this layer revealed by the formation of a second layer on top of the first. Based on the BSA structure that displays a permanent electric dipole [13], these features suggest an analogy with spin glasses that has not been considered until now. SAMPLES AND EXPERIMENTAL DEVICEBSA (Sigma-Aldrich) was diluted at a concentration of 1 mg/ml in heavy water (99.90 % 2 H, Euriso-top...

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“…That is, the kinetic behavior for a particular surface depends on "where that surface has been," and specifically whether any irreversible adsorption transitions have occurred on the surface. Multistep kinetic experiments, in which a Si(Ti)O 2 surface was exposed to a series of cytochrome c solutions of different concentrations, including rinse steps, show that the rate of adsorption is sensitive to the structure of any existing adsorbed layer on the protein surface [29]. This behavior seems to be consistent with a recent kinetic model proposed by Minton [28], which accounts for two pathways for protein adsorption: either directly onto the surface, or onto the upper surface of a pre-existing cluster followed be rearrangement of the cluster.…”

Section: Mechanism and Physics Of Protein Adsorptionmentioning

confidence: 99%

Microchannel wall coatings for protein separations by capillary and chip electrophoresis

et al. 2003

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The necessity for microchannel wall coatings in capillary and chip-based electrophoretic analysis of biomolecules is well understood. The regulation or elimination of EOF and the prevention of analyte adsorption is essential for the rapid, efficient separation of proteins and DNA within microchannels. Microchannel wall coatings and other wall modifications are especially critical for protein separations, both in fused-silica capillaries, and in glass or polymeric microfluidic devices. In this review, we present a discussion of recent advances in microchannel wall coatings of three major classes--covalently linked polymeric coatings, physically adsorbed polymeric coatings, and small molecule additives. We also briefly review modifications useful for polymeric microfluidic devices. Within each category of wall coatings, we discuss those used to eliminate EOF, to tune EOF, to prevent analyte adsorption, or to perform multiple functions. The knowledgeable application of the most promising recent developments in this area will allow for the separation of complex protein mixtures and for the development of novel microchannel wall modifications.

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History dependence of protein adsorption kinetics

Cited by 115 publications

References 41 publications

Understanding protein adsorption phenomena at solid surfaces

Understanding protein adsorption phenomena at solid surfaces

Slow and remanent electric polarization of adsorbed BSA layer evidenced by neutron reflection

Microchannel wall coatings for protein separations by capillary and chip electrophoresis

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