Surface exclusion effects in adsorption processes

Schaaf, Pierre; Talbot, J.

doi:10.1063/1.456768

Cited by 336 publications

(320 citation statements)

References 31 publications

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“…An important result of this theory is that a so-called jamming limit of surface coverage is reached, beyond which no additional molecules can be accommodated in the layer. For circular discs the jamming limit of surface coverage is 0.547 (2). The fact that coverage in protein adsorption is known to reach higher values (close to 1.0) suggests immediately that some desorption and/or surface diffusion can occur as has in fact been demonstrated by experimental means (3,4).…”

Section: Theory and Molecular Mechanisms Of Protein Adsorptionmentioning

confidence: 75%

“…The fact that coverage in protein adsorption is known to reach higher values (close to 1.0) suggests immediately that some desorption and/or surface diffusion can occur as has in fact been demonstrated by experimental means (3,4). These authors have also drawn attention to a perceived weakness of the Langmuir model which gives the available surface function (related to the rate of adsorption) as (1)(2)(3)(4)(5)(6), where 0 is the fractional surface site coverage. This is a consequence of the Langmuirian specification that one molecule occupies only one site.…”

Section: Theory and Molecular Mechanisms Of Protein Adsorptionmentioning

confidence: 99%

“…An important approach to the modeling of protein adsorption has come from the studies of Schaaf and Talbot (2). These groups have investigated the random sequential adsorption (RSA) model in relation to proteins.…”

Section: Theory and Molecular Mechanisms Of Protein Adsorptionmentioning

confidence: 99%

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Proteins at Interfaces

Brash

Horbett

1995

ACS Symposium Series

203

119

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Proteins at interfaces are involved in a wide variety of phenomena, including mammalian cell growth in culture, reactions to implanted biomaterials, growth of soil bacteria, and formation of organized layers of proteins at the oil/water and air/water interfaces.This broad range of phenomena has attracted the interest of a correspondingly broad range of scientists and engineers, many with different backgrounds and different perspectives. As a result, the field of proteins at interfaces displays as much breadth as depth, and many of the investigators in this field of research conduct investigations that are unique with respect both to the particular protein/surface system studied and to the methods used. The many different approaches and systems under investigation, and in particular the wide variety of applications towards which the research is directed, means that an overview such as this one which is limited in length, must be selective. In selecting subtopics for discussion we had to be somewhat arbitrary, and therefore tried to focus on broad aspects which are common to most application areas.The contributions to the San Diego Symposium and to this volume represent a significant fraction of the workers who are actively involved in studying the behavior of proteins at interfaces. We have therefore chosen to organize our overview around six major aspects of protein behavior at interfaces which emerged from the Symposium. These aspects are: (1) theory, including molecular mechanisms; (2) competitive adsorption; (3) conformation and orientation of proteins at interfaces; (4) surface chemistry effects on adsorption; (5) the behavior of proteins at fluid interfaces; and (6) effects of proteins on cell interactions with surfaces.For each topic, current understanding is briefly summarized, and the contributions of the articles in this volume are then discussed. Inevitably this type of subdivision is to some extent arbitrary and artificial, so there is some overlap of material from one section to another. We trust, however, that on balance our approach will facilitate the readers' (as well as the authors') task of understanding the state of the art in this field.0097-6156/95/0602-0001$12.75/0

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Section: Theory and Molecular Mechanisms Of Protein Adsorptionmentioning

confidence: 75%

Section: Theory and Molecular Mechanisms Of Protein Adsorptionmentioning

confidence: 99%

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Proteins at Interfaces

Brash

Horbett

1995

ACS Symposium Series

203

119

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“…It does not give the correct form of protein adsorption kinetics where the adsorbing surface is a continuum, such as a bilayer lipid membrane (Ramsden, 1993 b;. In this case an expression involving successive powers of 0 must be used (Schaaf & Talbot, 1989;Dickman et al 1991 In order to evaluate the kinetic parameters, the experimental data is fitted to the expression for F or dF/dt constructed according to a scheme like that in Fig. 21 with more or less terms depending on the particular problem.…”

Section: Evaluation Of Kinetic Parametersmentioning

confidence: 99%

Experimental methods for investigating protein adsorption kinetics at surfaces

Ramsden¹

1994

Quart. Rev. Biophys.

177

131

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The adsorption of proteins at the solid-liquid interface is a process of fundamental importance in nature. Extensive reviews (MacRitchie, 1978; Andrade & Hlady, 1986; Norde, 1986) testify to the strong interest which has been shown in the problem during the past few decades. Norde & Lyklema (1978) have rightly pointed out that protein adsorption is scientifically intriguing; the phenomenology is complicated and includes many presently apparently irreconcilable observations.

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“…The form of  appropriate to RSA of disks and spheres was used (equation 42 in ref. [51]). The parameters a * and ⁄ , where m is the mass of an adsorbing objects (for a mucin molecule, m  900 zg), were obtained by numerically fitting the integrated form of equation (2) to the data and they are gathered in Table 2.…”

Section: Corroboration Of the Adsorption Mechanismmentioning

confidence: 99%

Surface rearrangement of adsorbed EGCG–mucin complexes on hydrophilic surfaces

Horváth

Yakubov

Ramsden

2017

International Journal of Biological Macromolecules

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The kinetic adsorption-desorption behaviour of porcine gastric mucin in the presence of physiologically relevant concentrations of the polyphenol epigallocatechin gallate (EGCG) was investigated using high-resolution kinetic optical waveguide lightmode spectroscopy (OWLS) and atomic force microscopy (AFM). Comparison with dynamic light scattering results from EGCGmucin mixtures indicates that discrete particles are formed whose size increases with increasing EGCG:mucin ratio. These particles are deduced to be the adsorbing entities, which fuse on the surface to form complex surface layers. At low molar EGCG:mucin ratios (< 1000), aggregates fuse on the surface to form a monolayer similar to one of pure mucin. With increasing EGCG concentration, the surface assembly of aggregates becomes consistent with their rearrangement and spreading in the shape of a spherical segment. At the highest molar ratios investigated (> 12 000) the particles begin to destabilize. The presence of EGCG leads to birefringence hysteresis during adsorption-desorption, indicating structural rearrangement, even at molar ratios 1000. The intensification of the phenomenon with increasing EGCG:mucin ratio mimics what was previously observed with the increase of mucin concentration in an EGCG-free system.

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Surface exclusion effects in adsorption processes

Cited by 336 publications

References 31 publications

Proteins at Interfaces

Proteins at Interfaces

Experimental methods for investigating protein adsorption kinetics at surfaces

Surface rearrangement of adsorbed EGCG–mucin complexes on hydrophilic surfaces

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