Kinetic model for serum albumin adsorption : experimental verification

Kurrat, R.; Ramsden, Jeremy J.; Prenosil, J. E.

doi:10.1039/ft9949000587

Cited by 83 publications

(68 citation statements)

References 15 publications

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“…To see why this is so, we consider the picture of partially reversible protein adsorption in which molecules initially attach in a reversible manner (with a structure similar to that in solution) and subsequently undergo an irreversible transition to a conformationally or orientationally altered structure possessing a greater degree of surface contact (16,35). Within this picture, steric blocking of the transition prevents some of the molecules from becoming irreversibly bound; this explains observations of (i) a removal of only a certain fraction of adsorbed proteins during dilution of the bulk phase and (ii) an increase in maximal surface coverage with protein bulk concentration (36,37). Based on this picture, one expects that the kinetics of a second adsorption step would be slower because of transitions of some of the proteins during the rinse, leading to a more efficiently blocked surface and a diminishment of the area available for subsequent protein adsorption.…”

Section: Discussionmentioning

confidence: 89%

History dependence of protein adsorption kinetics

Calonder

Tie

Tassel

2001

Proc. Natl. Acad. Sci. U.S.A.

115

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The behavior of proteins at biological and synthetic interfaces is often characterized by a strong history dependence caused by long relaxation times or irreversible transitions. In this work, we introduce the rate of adsorption as a means to systematically quantify the extent, and identify the underlying causes, of history dependence. We use multistep kinetic experiments in which the ith step is an exposure of a Si(Ti)O2 surface to a flowing fibronectin or cytochrome c solution of concentration ci for a time ti (ci ‫؍‬ 0 corresponds to a rinse) and measure the protein adsorption by optical waveguide light mode spectroscopy. The rate of adsorption is sensitive to the structure of the adsorbed layer, and we observe it to greatly increase, for a given adsorbed density, when going from a first to a subsequent adsorption step. This increase is most pronounced when the duration of the initial adsorption step is long. We attribute these observations to the gradual and irreversible formation of protein clusters or locally ordered structures and use them to explain previous underestimates of kinetic data by mesoscopic model descriptions. A thorough understanding of these complex postadsorption events, and their impact on history dependence, is essential for many physiological and biotechnological processes. Optical waveguide lightmode spectroscopy is a promising technique for their macroscopic quantification.optical waveguide lightmode spectroscopy ͉ interfacial kinetics ͉ surface diffusion ͉ surface aggregation

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Section: Discussionmentioning

confidence: 89%

History dependence of protein adsorption kinetics

Calonder

Tie

Tassel

2001

Proc. Natl. Acad. Sci. U.S.A.

115

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“…One example is the so called 'catalysis of desorption' by adsorbed neighbors primarily observed by Kurrat et al which accounts for rising desorption rates at higher surface coverages [139]. Further, even though mechanistically somewhat different, it has been shown that proteins approaching the surface may hit other pre-adsorbed proteins which, as a result, are released from the surface [10,140].…”

Section: Lateral Interactionsmentioning

confidence: 99%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,354

1,289

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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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“…(Levich, 1962); under typical experimental conditions W d « 100 fim. k d may be more complicated than a simple first-order rate constant if lateral interactions are taken into account (Kurrat et al 1993). k a and k s depend on energy barriers impeding adsorption; k a refers to reversibly adsorbed molecules, and k s to irreversibly adsorbed ones.…”

Section: Evaluation Of Kinetic Parametersmentioning

confidence: 99%

Experimental methods for investigating protein adsorption kinetics at surfaces

Ramsden¹

1994

Quart. Rev. Biophys.

Self Cite

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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Kinetic model for serum albumin adsorption : experimental verification

Cited by 83 publications

References 15 publications

History dependence of protein adsorption kinetics

History dependence of protein adsorption kinetics

Understanding protein adsorption phenomena at solid surfaces

Experimental methods for investigating protein adsorption kinetics at surfaces

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