Binding of proteins to copolymers of varying hydrophobicity

Gao, Jeff Y.; Dubin, Paul L.

doi:10.1002/(sici)1097-0282(199902)49:2<185::aid-bip6>3.0.co;2-6

Cited by 68 publications

(49 citation statements)

References 41 publications

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“…on April 30, 2019 by guest http://mmbr.asm.org/ 239); another example is the phenomenon of weak association of proteins via their hydrophobic patches, for example, the dimerization of GFP (68,164). Also, as discussed earlier in relation to biomacromolecular crowding, recent experiments on stabilization (folding) of proteins under crowded conditions (104,141,186,240) show attractive interactions in addition to the repulsive effect of excluded volume.…”

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confidence: 89%

From Water and Ions to Crowded Biomacromolecules:In VivoStructuring of a Prokaryotic Cell

Spitzer¹

2011

Microbiol Mol Biol Rev

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SUMMARY The interactions and processes which structure prokaryotic cytoplasm (water, ions, metabolites, and biomacromolecules) and ensure the fidelity of the cell cycle are reviewed from a physicochemical perspective. Recent spectroscopic and biological evidence shows that water has no active structuring role in the cytoplasm, an unnecessary notion still entertained in the literature; water acts only as a normal solvent and biochemical reactant. Subcellular structuring arises from localizations and interactions of biomacromolecules and from the growth and modifications of their surfaces by catalytic reactions. Biomacromolecular crowding is a fundamental physicochemical characteristic of cells in vivo . Though some biochemical and physiological effects of crowding (excluded volume effect) have been documented, crowding assays with polyglycols, dextrans, etc., do not properly mimic the compositional variety of biomacromolecules in vivo . In vitro crowding assays are now being designed with proteins, which better reflect biomacromolecular environments in vivo , allowing for hydrophobic bonding and screened electrostatic interactions. I elaborate further the concept of complex vectorial biochemistry, where crowded biomacromolecules structure the cytosol into electrolyte pathways and nanopools that electrochemically “wire” the cell. Noncovalent attractions between biomacromolecules transiently supercrowd biomacromolecules into vectorial, semiconducting multiplexes with a high (35 to 95%)-volume fraction of biomacromolecules; consequently, reservoirs of less crowded cytosol appear in order to maintain the experimental average crowding of ∼25% volume fraction. This nonuniform crowding model allows for fast diffusion of biomacromolecules in the uncrowded cytosolic reservoirs, while the supercrowded vectorial multiplexes conserve the remarkable repeatability of the cell cycle by preventing confusing cross talk of concurrent biochemical reactions.

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confidence: 89%

From Water and Ions to Crowded Biomacromolecules:In VivoStructuring of a Prokaryotic Cell

Spitzer¹

2011

Microbiol Mol Biol Rev

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“…CE-FA has been used to measure binding of copper(II) to 1,10-phenanthroline and 2,2'-bipyridyl [52], drugs to cyclodextrins [43], and haptens to antibodies [53]. Furthermore, polymerprotein systems have been investigated by FACCE [47,[54][55][56][57][58][59][60]. It seems unlikely that similar size/charge ratios [41] HSA (rat plasma) Phenytoin, sulfathiazole, phenylbutazone, warfarin, diclofenac, ketoprofen…”

Section: Requirements For Using Ce-famentioning

confidence: 99%

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

2003

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Capillary electrophoresis frontal analysis: Principles and applications for the study of drug-plasma protein bindingCapillary electrophoresis is a well-established technique for the study of noncovalent interactions. Various approaches exist and capillary electrophoresis-frontal analysis provides an interesting alternative to the migration shift affinity capillary electrophoresis methods and conventional methods. The present work reviews the principles on which the frontal analysis method is founded. Advantages and limitations of capillary electrophoresis frontal analysis in comparison with both conventional and other capillary electrophoresis based methods for quantification of binding interactions are discussed. Investigations utilizing capillary electrophoresis-frontal analysis have focused on the interaction of drugs with plasma proteins. These studies, primarily addressing the binding of drugs to human serum albumin, a 1 -acid glycoprotein, and lipoproteins are reviewed together with some recent developments in capillary electrophoresisfrontal analysis methodology.

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“…FACCE was used to study the binding of proteins to polyelectrolytes [35]. FACCE offers enhanced detection limits and is free from effects due to slow binding kinetics, thus making it suitable for studying equilibrium systems.…”

Section: Faccementioning

confidence: 99%

Recent advances in affinity capillary electrophoresis

Guijt¹,

Frank²,

Dedem³

et al. 2000

Electrophoresis

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Use of the specificity of (bio)interactions can effectively overcome the selectivity limitation faced in capillary electrophoresis (CE), and the resulting technique usually is referred to as affinity capillary electrophoresis (ACE). Despite the high selectivity of ACE, several important problems still need to be addressed. A major issue in all CE separations, including ACE, is the concentration detection limit. Using UV detection, this is usually in the order of 10(-6) M whereas laser-induced fluorescence (LIF) detection can provide detection limits down to the sub-10(-10) M range. However, a marked disadvantage of LIF is that labeling of the analytes is usually required, which might change the interaction behavior of the solutes under investigation. Additionally, labeling reactions at sub-10(-10) M concentration levels are certainly not trivial and often difficult to perform quantitatively. Alternative and universal detection approaches, particularly mass spectrometric (MS) detection, look very promising but (A) CE-MS techniques are still far from routine application. Important future progress in sensitive detection strategies is likely to increase the use of ACE in the future.

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Binding of proteins to copolymers of varying hydrophobicity

Cited by 68 publications

References 41 publications

From Water and Ions to Crowded Biomacromolecules:In VivoStructuring of a Prokaryotic Cell

From Water and Ions to Crowded Biomacromolecules:In VivoStructuring of a Prokaryotic Cell

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

Recent advances in affinity capillary electrophoresis

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