A molecular approach to bioseparations: protein-protein and protein-salt interactions

R.A. Curtis, L. Lue

Research output: Contribution to journalArticle

107 Citations (Scopus)

Abstract

Many bioprocess separations involve manipulating the solution conditions to selectively remove or concentrate a target protein. The selectivity is determined by the thermodynamics of the protein solution, which are governed, at the molecular level, by protein-protein interactions. Thus, to optimise these processes, one must understand the precise nature of these interactions, how they are affected by the control parameters (e.g., temperature, ionic strength, pH), and how they relate to the solution properties of interest (e.g., protein solubility, protein stability, crystal nucleation rates). Recently, studies of protein-protein interactions have been motivated by the discovery of a crystallisation window, which places bounds on the protein-protein attraction that is required for crystallisation to be possible. This review focuses on experimental and theoretical studies of protein-protein interactions and discusses the current caps in understanding these forces. The first models for these interactions had been based on DLVO theory, which has proven useful for understanding protein-protein interactions in dilute electrolyte solutions. However, DLVO theory does not include such important effects as anisotropic interactions, solvation forces, and specific ion effects. Various approaches have been developed to include these phenomena although they are still not well understood. One outstanding issue concerns specific ion effects, which play a crucial role in biological systems. An initial step in understanding these effects might be to first rationalize protein-salt interactions. (c) 2005 Elsevier Ltd. All fights reserved.
LanguageEnglish
Pages907-923
Number of pages17
JournalChemical Engineering Science
Volume61
Issue number3
DOIs
Publication statusPublished - Feb 2006

Fingerprint

Salt
Salts
Proteins
Protein
Protein-protein Interaction
Interaction
Crystallization
Solubility
Electrolyte
Selectivity
Nucleation
Biological Systems
Control Parameter
Thermodynamics
Crystal
Optimise
Ions
Target
Solvation
Biological systems

Keywords

  • proteins
  • phase equilibria
  • crystallisation
  • colloidal phenomena
  • intermolecular interactions
  • molecular thermodynamics

Cite this

@article{eee90a0c5cc84a7e90da9b91268f7edc,
title = "A molecular approach to bioseparations: protein-protein and protein-salt interactions",
abstract = "Many bioprocess separations involve manipulating the solution conditions to selectively remove or concentrate a target protein. The selectivity is determined by the thermodynamics of the protein solution, which are governed, at the molecular level, by protein-protein interactions. Thus, to optimise these processes, one must understand the precise nature of these interactions, how they are affected by the control parameters (e.g., temperature, ionic strength, pH), and how they relate to the solution properties of interest (e.g., protein solubility, protein stability, crystal nucleation rates). Recently, studies of protein-protein interactions have been motivated by the discovery of a crystallisation window, which places bounds on the protein-protein attraction that is required for crystallisation to be possible. This review focuses on experimental and theoretical studies of protein-protein interactions and discusses the current caps in understanding these forces. The first models for these interactions had been based on DLVO theory, which has proven useful for understanding protein-protein interactions in dilute electrolyte solutions. However, DLVO theory does not include such important effects as anisotropic interactions, solvation forces, and specific ion effects. Various approaches have been developed to include these phenomena although they are still not well understood. One outstanding issue concerns specific ion effects, which play a crucial role in biological systems. An initial step in understanding these effects might be to first rationalize protein-salt interactions. (c) 2005 Elsevier Ltd. All fights reserved.",
keywords = "proteins, phase equilibria, crystallisation, colloidal phenomena, intermolecular interactions, molecular thermodynamics",
author = "R.A. Curtis and L. Lue",
year = "2006",
month = "2",
doi = "10.1016/j.ces.2005.04.007",
language = "English",
volume = "61",
pages = "907--923",
journal = "Chemical Engineering Science",
issn = "0009-2509",
number = "3",

}

A molecular approach to bioseparations : protein-protein and protein-salt interactions. / Curtis, R.A.; Lue, L.

In: Chemical Engineering Science, Vol. 61, No. 3, 02.2006, p. 907-923.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A molecular approach to bioseparations

T2 - Chemical Engineering Science

AU - Curtis, R.A.

AU - Lue, L.

PY - 2006/2

Y1 - 2006/2

N2 - Many bioprocess separations involve manipulating the solution conditions to selectively remove or concentrate a target protein. The selectivity is determined by the thermodynamics of the protein solution, which are governed, at the molecular level, by protein-protein interactions. Thus, to optimise these processes, one must understand the precise nature of these interactions, how they are affected by the control parameters (e.g., temperature, ionic strength, pH), and how they relate to the solution properties of interest (e.g., protein solubility, protein stability, crystal nucleation rates). Recently, studies of protein-protein interactions have been motivated by the discovery of a crystallisation window, which places bounds on the protein-protein attraction that is required for crystallisation to be possible. This review focuses on experimental and theoretical studies of protein-protein interactions and discusses the current caps in understanding these forces. The first models for these interactions had been based on DLVO theory, which has proven useful for understanding protein-protein interactions in dilute electrolyte solutions. However, DLVO theory does not include such important effects as anisotropic interactions, solvation forces, and specific ion effects. Various approaches have been developed to include these phenomena although they are still not well understood. One outstanding issue concerns specific ion effects, which play a crucial role in biological systems. An initial step in understanding these effects might be to first rationalize protein-salt interactions. (c) 2005 Elsevier Ltd. All fights reserved.

AB - Many bioprocess separations involve manipulating the solution conditions to selectively remove or concentrate a target protein. The selectivity is determined by the thermodynamics of the protein solution, which are governed, at the molecular level, by protein-protein interactions. Thus, to optimise these processes, one must understand the precise nature of these interactions, how they are affected by the control parameters (e.g., temperature, ionic strength, pH), and how they relate to the solution properties of interest (e.g., protein solubility, protein stability, crystal nucleation rates). Recently, studies of protein-protein interactions have been motivated by the discovery of a crystallisation window, which places bounds on the protein-protein attraction that is required for crystallisation to be possible. This review focuses on experimental and theoretical studies of protein-protein interactions and discusses the current caps in understanding these forces. The first models for these interactions had been based on DLVO theory, which has proven useful for understanding protein-protein interactions in dilute electrolyte solutions. However, DLVO theory does not include such important effects as anisotropic interactions, solvation forces, and specific ion effects. Various approaches have been developed to include these phenomena although they are still not well understood. One outstanding issue concerns specific ion effects, which play a crucial role in biological systems. An initial step in understanding these effects might be to first rationalize protein-salt interactions. (c) 2005 Elsevier Ltd. All fights reserved.

KW - proteins

KW - phase equilibria

KW - crystallisation

KW - colloidal phenomena

KW - intermolecular interactions

KW - molecular thermodynamics

U2 - 10.1016/j.ces.2005.04.007

DO - 10.1016/j.ces.2005.04.007

M3 - Article

VL - 61

SP - 907

EP - 923

JO - Chemical Engineering Science

JF - Chemical Engineering Science

SN - 0009-2509

IS - 3

ER -