Estimation of diffusion coefficients of proteins

Young, Margaret A.; Carroad, Paul A.; Bell, Richard L.

doi:10.1002/bit.260220504

Cited by 473 publications

(279 citation statements)

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“…Using D ~ 10 −6 cm 2 /sec appropriate for proteins [86], τ ≈ 1.6 msec, anticipating that equilibrium would be achieved within a few milliseconds.…”

Section: Appendix a Appendix A 1 Bond And Puls Analysismentioning

confidence: 99%

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Barnthip¹,

Noh²,

Leibner³

et al. 2008

Biomaterials

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Time-dependent energetics of blood-protein adsorption are interpreted in terms of a slowlyconcentrating three-dimensional interphase volume initially formed by rapid diffusion of protein molecules into an interfacial region spontaneously formed by bringing a protein solution into contact with a physical surface. This modification of standard adsorption theory is motivated by the experimental observation that interfacial tensions of protein-containing solutions decrease slowly over the first hour to a steady-state value while, over this same period, the total adsorbed-protein mass is constant (for lysozyme, 15 kDa; albumin, 66 kDa; prothrombin, 72 kDa; IgG, 160 kDa; fibrinogen, 341 kDa studied in this work). These seemingly divergent observations are rationalized by the fact that interfacial energetics (tensions) are explicit functions of solute chemical potential (concentration), not adsorbed mass. Hence, rates-of-interfacial-tension-change parallel a slow interphase concentration effect whereas solution depletion detects a constant interphase composition within the time frame of experiment. A straightforward mathematical model approximating the perceived physical situation leads to an analytic formulation that is used to compute time-varying interphase volume and protein concentration from experimentally-measured interfacial tensions. Derivation from the fundamental thermodynamic adsorption equation verifies that protein adsorption from dilute solution is controlled by a partition coefficient at equilibrium, as is observed experimentally at steady state. Implications of the alternative interpretation of adsorption kinetics on biomaterials and biocompatibility are discussed. KeywordsProtein adsorption; kinetics; interfacial energetics; interphase; surface; radiometry IntroductionProtein-adsorption kinetics are of practical importance in biomaterials because adsorption rates have been implicated as a cause of selective protein adsorption. For example, the so-called Vroman Effect is commonly thought to occur because low-molecular-weight proteins *Author to whom correspondence should be addressed EAV3@PSU.EDU. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Author ManuscriptBiomaterials. Author manuscript; available in PMC 2009 July 1. Published in final edited form as:Biomaterials. presumably arriving first at a surface immersed in a multi-component solution are displaced by higher-molecular-weight proteins arriving later (see refs. and citations therein). The final adsorbed-protein composition is thus purported to be achieved through a complex se...

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“…Using D ~ 10 −6 cm 2 /sec appropriate for proteins [86], τ ≈ 1.6 msec, anticipating that equilibrium would be achieved within a few milliseconds.…”

Section: Appendix a Appendix A 1 Bond And Puls Analysismentioning

confidence: 99%

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Barnthip¹,

Noh²,

Leibner³

et al. 2008

Biomaterials

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“…Keeping these observations in mind, we will obtain diffusion coefficients for low molecular weight proteins in plasma (1.2 cP) at 378C using a generalized form of the Stokes-Einstein equation, namely the correlation in Young et al (1980). This requires knowledge of the molecular weights and specific partial volumes for each protein.…”

Section: Treatment Of Diffusion Coefficientsmentioning

confidence: 99%

“…This requires knowledge of the molecular weights and specific partial volumes for each protein. Complete data was not found for the specific partial volumes, and hence a value of 0.73 cc/g was chosen where this data was unavailable (see Young et al (1980) for a rationale for this assumption). We will use the correlation in Young et al (1980) for high molecular weight proteins (.…”

Section: Treatment Of Diffusion Coefficientsmentioning

confidence: 99%

“…A slightly more sophisticated equation than the one in Young et al (1980) is proposed in Tyn and Gusek (1990) which includes the role of protein shape and sizes by means of the radius of gyration (R gyr ). Measurements of R gyr are not available for all the coagulation factors, and hence we have not used this correlation.…”

Section: Treatment Of Diffusion Coefficientsmentioning

confidence: 99%

“…A thr and AðtÞ . A damage ; ð67Þ Young et al (1980) and Lentner (1984) and Lijnen and Collen (2000) then…”

Section: Platelet Activation Due To Prolonged Exposure To Shear Stressesmentioning

confidence: 99%

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A Model Incorporating Some of the Mechanical and Biochemical Factors Underlying Clot Formation and Dissolution in Flowing Blood

Mohan

Rajagopal

2003

Computational and Mathematical Methods in Medicine

142

121

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Multiple interacting mechanisms control the formation and dissolution of clots to maintain blood in a state of delicate balance. In addition to a myriad of biochemical reactions, rheological factors also play a crucial role in modulating the response of blood to external stimuli. To date, a comprehensive model for clot formation and dissolution, that takes into account the biochemical, medical and rheological factors, has not been put into place, the existing models emphasizing either one or the other of the factors. In this paper, after discussing the various biochemical, physiologic and rheological factors at some length, we develop a model for clot formation and dissolution that incorporates many of the relevant crucial factors that have a bearing on the problem. The model, though just a first step towards understanding a complex phenomenon, goes further than previous models in integrating the biochemical, physiologic and rheological factors that come into play.

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Development of operating conditions for protein purification using expanded bed techniques: The effect of the degree of bed expansion on adsorption performance

Chang

Chase

2000

Biotechnol. Bioeng.

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A strategy for the optimization of an expanded bed adsorption process has been developed by studying a model system involving the adsorption of lysozyme onto the adsorbent STREAMLINE SP. The hydrodynamic and adsorption properties of this ion exchange adsorbent in a variety of viscosities of feedstocks have been compared by analyzing bed expansion characteristics, liquid phase dispersion characteristics, equilibrium adsorption isotherms, and mass transfer characteristics. Additionally, the influences of the degree of bed expansion on adsorption performance have been investigated by frontal analysis. In these experiments, viscous feedstocks were simulated by the inclusion of glycerol in the adsorption buffers. Breakthrough curves for lysozyme were characterized and compared in terms of overall purification processing time and productivity. On the basis of these results, the relative productivities of different operating modes with the same process liquid were found to be almost the same. However, the processing time for each purification cycle decreased with increasing velocity of process liquid. It is demonstrated that an adsorption process carried out at a constant degree of bed expansion (twice its settled bed height, corresponding to bed voidage of 0.7) is more efficient, when characterized by the apparent dynamic binding capacity, than operation at a constant liquid velocity of 300 cm/h. These results have significant implications on the design and operation of the expanded bed adsorption procedures. The advantages and problems encountered in the use of expanded bed techniques for the direct extraction of proteins from unclarified feedstocks are also discussed. © 1996 John Wiley & Sons, Inc.

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Estimation of diffusion coefficients of proteins

Cited by 473 publications

References 4 publications

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

A Model Incorporating Some of the Mechanical and Biochemical Factors Underlying Clot Formation and Dissolution in Flowing Blood

Development of operating conditions for protein purification using expanded bed techniques: The effect of the degree of bed expansion on adsorption performance

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