Thermodynamic model for nonlinear electrostatic adsorption equilibrium of protein

Su, Xueli; Sun, Yan

doi:10.1002/aic.10900

Cited by 17 publications

(15 citation statements)

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“…620 To explain the data, they invoked the concept of lateral steric effects [622][623][624][625][626][627] -an unfavorable steric repulsion between BCA II that is bound at the surface and BCA II that is free in solution ( Figure 10C; section 8.4.3). Decreasing the fractional coverage of arylsulfonamide ligands on the surface should reduce the possibility of these unfavorable interactions between bound BCA II molecules and increase the observed value of k on to its solution-phase value.…”

Section: Lateral Steric Effectsmentioning

confidence: 99%

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

et al. 2008

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I. Introduction to Carbonic Anhydrase (CA) and to the Review 948 1. Introduction: Overview of CA as a Model 948 1.1. Value of Models 950 1.2. Objectives and Scope of the Review 950 2. Overview of Enzymatic Activity 950 3. Medical Relevance 951 II. Structure and Structure−Function Relationships of CA 953 4. Global and Active-Site Structure 953 4.1. Structure of Isoforms 953 4.2. Isolation and Purification 954 4.3. Crystallization 954 4.4. Structures Determined by X-ray Crystallography and NMR 955 4.4.1. Structures Determined by X-ray Crystallography 955 4.4.2. Structure Determined by NMR 955 4.5. Global Structural Features 963 4.6. Structure of the Binding Cavity 964 4.7. Zn II -Bound Water 965 5. Metalloenzyme Variants 966 6. Structure−Function Relationships in the Catalytic Active Site of CA 968 6.1. Effects of Ligands Directly Bound to Zn II 968 6.2. Effects of Indirect Ligands 969 7. Physical-Organic Models of the Active Site of CA 969 III. Using CA as a Model to Study Protein−Ligand Binding 970 8. Assays for Measuring Thermodynamic and Kinetic Parameters for Binding of Substrates and Inhibitors 970 8.1. Overview 970 8.

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Section: Lateral Steric Effectsmentioning

confidence: 99%

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

et al. 2008

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“…Of them, a 1 , a 2 , k 11 , and k 22 are singlecomponent adsorption parameters that can be determined by single protein adsorption equilibrium experiments. kp 12 or kp 21 can be determined by binary protein adsorption equilibrium experiments.…”

Section: Theorymentioning

confidence: 99%

“…Based on hypotheses (i) to (vii), the ST model for multicomponent adsorption equilibria has been derived as Su and Sun [21] …”

Section: Theorymentioning

confidence: 99%

“…The ST model developed by Su and Sun [21] is used herein to study the nonlinear binary protein adsorption equilibria. The theory is derived on the basis of statistical thermodynamics and the following fundamental hypotheses:…”

Section: Theorymentioning

confidence: 99%

“…Recently, a statistical thermodynamic (ST) model has been developed by Su and Sun [21] for nonlinear multi-component protein adsorption equilibria on ion exchangers. This model takes into account the electrostatic interactions between the adsorbent surface and protein molecules as well as the lateral interactions between adsorbed protein molecules.…”

Section: Introductionmentioning

confidence: 99%

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Analysis of statistical thermodynamic model for binary protein adsorption equilibria on cation exchange adsorbent

Xiaopeng

Sun

2007

Front. Chem. Eng. China

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knowledge of mass transfer kinetics is required to optimize the chromatographic purification process, as the process performance is mass-transfer-limited in many applications. Liquid chromatography models on the basis of continuity equations are useless unless they are fed with appropriate adsorption isotherm equations, describing the basic thermodynamic equilibria between biomolecules in the mobile phase and the stationary phase. Therefore the study of adsorption equilibrium is of major importance for liquid chromatography [1][2][3].Currently, many mathematical models have been proposed for describing the adsorption equilibrium of biomolecules. Among these models, the Langmuir-type isotherms are the most famous models and are widely used to describe the nonlinear adsorption behavior in preparative ion-exchange chromatography [4]. Expressed in the simple and explicit form, Langmuir isotherms can represent the singlecomponent adsorption equilibrium data very well. However, the Langmuir isotherms are recognized to be thermodynamically inconsistent for multi-component ion-exchange systems, and the effect of ionic strength on protein adsorption is not explicitly expressed in these models [5,6]. Based on the mass action law, the stoichiometric displacement (SD) model was proposed to study protein adsorption in ion exchange systems [1][2][3][4][5][6][7]. However, it is a non-mechanistic model on the basis of oversimplified hypotheses which restrict it to rather ideal cases. Brooks and Cramer [8] combined the SD model and the concept of macromolecule steric shielding effect together to bring forward the steric mass-action (SMA) model for ion exchange adsorption. This model is considered to be one of the best models so far for protein ion exchange adsorption equilibrium and has found many applications in multi-component ion exchange chromatography [9,10]. The SMA model has also been extended to describe the dyeligand affinity adsorption equilibrium of proteins [11]. Recently, Shen and Frey [12] further investigated the SMA model by incorporating the effects of charge regulation on the ion-exchange adsorption of proteins. Abstract A study of nonlinear competitive adsorption equilibria of proteins is of fundamental importance in understanding the behavior of preparative chromatographic separation. This work describes the nonlinear binary protein adsorption equilibria on ion exchangers by the statistical thermodynamic (ST) model. The single-component and binary protein adsorption isotherms of bovine hemoglobin (Hb) and bovine serum albumin (BSA) on SP Sepharose FF were determined by batch adsorption experiments in 0.05 mol/L sodium acetate buffer at three pH values (4.5, 5.0 and 5.5) and three NaCl concentrations (0.05, 0.10 and 0.15 mol/L) at pH 5.0. The ST model was found to depict the effects of pH and ionic strength on the single-component equilibria well, with model parameters depending on the pH and ionic strength. Moreover, the ST model gave acceptable fitting to the binary adsorption data with the fitted singlecompo...

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Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

Creasy

Barker

Yan

et al. 2015

Biotechnology Journal

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A method is developed to predict protein chromatographic behavior from batch isotherm using a a systematic empirical interpolation (EI) scheme and without relying on a mechanistic description of the dependence of protein binding on protein and salt concentration. Coupled with a lumped kinetic model with rate parameters determined from HETP measurements for non-binding conditions, the EI scheme is used to numerically predict the column behavior. For two experimental cation exchange systems considered in this work, lysozyme on SP-Sepharose-FF and a monoclonal antibody on POROS XS, predictions based on the EI scheme are in excellent agreement with experimental elution profiles under highly overloaded conditions without using any adjustable parameters. A qualitative study of the sensitivity of predicting protein elution profiles to the precision, granularity, and extent of the batch adsorption data is conducted. Based on the results for a hypothetical system, whose properties are comparable to those found in practice for protein cation exchange chromatography the results of this show that the interpolation scheme is relatively insensitive, requiring only that the ranges of protein and salt concentrations in the experimental dataset overlap those under which the protein actually elutes from the column and along with a 10% measurement precision.

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Thermodynamic model for nonlinear electrostatic adsorption equilibrium of protein

Cited by 17 publications

References 30 publications

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

Analysis of statistical thermodynamic model for binary protein adsorption equilibria on cation exchange adsorbent

Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

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