Affinity Interactions by Capillary Electrophoresis: Binding, Separation, and Detection.

  title={Affinity Interactions by Capillary Electrophoresis: Binding, Separation, and Detection.},
  author={Fangzhi Yu and Qiang Zhao and Dapeng Zhang and Zheng Yuan and Hailin Wang},
  journal={Analytical chemistry},
  volume={91 1},
Affinity interactions between molecules constitute this amazing and mysterious world of the human-living earth. At the level of individuals, affinity interactions are fundamental for the paramount functions and exquisite architectures of all organisms in life, for the occurrence and development of diseases, for the therapy-associated diagnosis, pharmaceutics and medicine (and cutting-edge regenerative medicine), and for the environment-life interplayed sphere. At the level of cells, affinity… 
19 Citations

An electroosmotic flow-free two-direction migration strategy enables fast affinity capillary electrophoresis to study the weak interactions between basic peptides and RNA.

A two-direction migration strategy is proposed that enables ACE to detect weak and unstable but important interactions by decreasing the migration distance of the binding complex and controlling the opposite migration direction of the free probe.

Affinity Capillary Electrophoresis–Mass Spectrometry as a Tool to Unravel Proteoform-Specific Antibody–Receptor Interactions

An approach based on mobility shift-affinity capillary electrophoresis–mass spectrometry (ACE–MS) permitted us to determine the binding of coexisting mAb proteoforms to Fc receptors (FcRs) and can be extended to other FcRs and protein interactions.

Quantitative characterization of human oncogene promoter G‐quadruplex DNA‐ligand interactions using a combination of mass spectrometry and capillary electrophoresis

The combination of electrospray ionization–mass spectrometry (ESI‐MS), capillary electrophoresis frontal analysis (CE‐FA), and Taylor dispersion analysis (TDA) is proposed to accurately investigate the G4/ligands binding properties of c‐KIT G4 to identify small molecule ligands which can specifically bind with the G‐quadruplex in the c-KIT promoter region as potential antitumor agents.

Label-free methods for optical in vitro characterization of protein–protein interactions

Recent advances in optical technologies providing label-free in vitro measurements of affinities and kinetics are reviewed, providing an overview and comparison of existing techniques and their principles, discussing advantages, limitations, and recent applications.

Capillary electrophoresis–based immunoassay and aptamer assay: A review

The aptamer‐based CE technique was in practice utilized for the determination of proteins in biological fluids and environmentally or clinically important small molecules and the techniques were also transferred to microchip.

Recent developments in capillary and microchip electroseparations of peptides (2017–mid 2019)

A comprehensive survey of recent developments and applications of high performance capillary and microchip electroseparation methods for analysis, micropreparation, and physicochemical and biochemical characterization of peptides since 2017 up to about the middle of 2019.



Protein Cross-Linking Capillary Electrophoresis for Protein-Protein Interaction Analysis.

PXCE allows rapid method development for quantitative analysis of PPIs and eliminates the need to maintain noncovalent interactions during electrophoresis and facilitates method development.

Separation of Methylated Histone Peptides via Host-Assisted Capillary Electrophoresis.

It is shown that supramolecular hosts such as calixarenes and cucurbiturils can be applied in the background electrolyte of capillary electrophoresis for highly effective separation of post-translationally methylated histone peptides and monitoring of the activity of the histone lysine demethylase JMJD2E.

Evoking picomolar binding in RNA by a single phosphorodithioate linkage

The use of the phosphorodithioate (PS2) substitution on a single nucleotide of RNA aptamers is reported to dramatically improve target binding affinity by ∼1000-fold (from nanomolar to picomolar).

Development of a capillary electrophoresis platform for identifying inhibitors of protein-protein interactions.

Capillary electrophoresis has been evaluated as a method to screen for PPI inhibitors using the challenging system of Hsp70 interacting with its co-chaperone Bag3, and it is attractive as a secondary screen to test hits found by higher-throughput methods.

Fluorescence anisotropy analysis for mapping aptamer-protein interaction at the single nucleotide level.

Simultaneous monitoring of both fluorescence anisotropy changes and electrophoretic mobility shifts upon binding of the fluorescently modified aptamer to the protein provides unique information on the specific nucleotide site of binding.

Affinity capillary electrophoresis for the assessment of binding affinity of carbohydrate‐based cholera toxin inhibitors

The developed method can be an important platform for preclinical development of drugs targeting pathogen‐induced secretory diarrhea and the selectivity of GM1os towards CTB was demonstrated using Influenza hemagglutinin (H5) as a binding competitor.

Specific Binding Constant and Stoichiometry Determination in Free Solution by Mass Spectrometry and Capillary Electrophoresis Frontal Analysis.

A nonlinear curve fitting equation capable of extracting specific binding constants in the presence of nonspecific binding without the need for reference compounds was proposed and tested and jatrorrhizine and palmatine were found to bind specifically to the Bcl-2 promoter G-quadruplex with stoichiometries of 4:1 and 3:1, respectively.

Development of Phosphorothioate DNA and DNA Thioaptamers

The development of phosphorothioate chemistry and thioaptamers are discussed, known to have increased binding affinity towards their target, as well as enhanced resistance to nuclease degradation.

Analysis of Proteins, Protein Complexes, and Organellar Proteomes Using Sheathless Capillary Zone Electrophoresis - Native Mass Spectrometry

Capillary zone electrophoresis (CZE) was coupled online to Orbitrap mass spectrometers using a commercial sheathless interface to enable high-performance separation, identification, and structural characterization of limited amounts of purified proteins and protein complexes, the latter with preserved non-covalent associations under native conditions.