Affinity capillary electrophoresis for the determination of binding affinities for low molecular weight heparins and antithrombin‐III

@article{Dinges2014AffinityCE,
  title={Affinity capillary electrophoresis for the determination of binding affinities for low molecular weight heparins and antithrombin‐III},
  author={Meredith M Dinges and Kemal Solakyildirim and Cynthia K Larive},
  journal={ELECTROPHORESIS},
  year={2014},
  volume={35}
}
The anticoagulant properties of heparin stem in part from high‐affinity binding to antithrombin‐III (AT‐III) inducing a 300‐fold increase in its inhibitory activity against the coagulation protease factor Xa. The minimal structural requirements for AT‐III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6‐O‐sulfated N‐sulfoglucosamine residue. ACE is used in this work to measure the relative AT‐III binding affinities of the low molecular weight heparins (LWMHs… 

Using affinity capillary electrophoresis and computational models for binding studies of heparinoids with p‐selectin and other proteins

It was found that P‐selectin interacts more strongly with heparinoids in the presence of calcium ions, and docking models proved to be particularly well suited to investigate the interaction of charged compounds, and are therefore complementary to ACE experiments.

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.

Glycosaminoglycans: anticoagulant and nonanticoagulant actions: a short history of symposia held at villa vigoni.

The latest developments on the methods of analysis, the synthesis, the degradation by heparanases and the nonanticoagulant effects in tumor growth, in anti-inflammatory diseases, and in Alzheimer diseases as presented in the 21st symposium are summarized.

Evaluation of the interactions between oligonucleotides and small molecules by partial filling-nonequilibrium affinity capillary electrophoresis.

When interactions between drug candidates and disease-related RNAs were analyzed, one of the candidates showed remarkable variation in the peak parameters upon the addition of potassium ions, indicating the applicability of the proposed method for drug screening.

Capillary electrophoresis in the context of drug discovery

Polymer-Based MEMS Calorimetric Devices for Characterization of Biomolecular Interactions

Polymer-Based MEMS Calorimetric Devices for Characterization of Biomolecular Interactions Yuan Jia Biomolecular interactions are central to all biological functions as the execution of biological

Electrophorèse capillaire couplée ou non à la spectrométrie de masse pour l’évaluation ou le contrôle qualité de protéines à visée thérapeutique

Au cours de cette these, nous avons ete amenes a developper des methodes analytiques afin de controler la qualite de proteines therapeutiques en tant que produits finis ou d'evaluer le potentiel de

References

SHOWING 1-10 OF 45 REFERENCES

Structure of the antithrombin-binding site in heparin.

Compositional analysis based on separation and identification of deamination products reduced with sodium boro[3H]hydride showed that nonsulfated L-iduronic acid occurred in larger amounts in high-affinity heparin than in low-Affinity heParin; furthermore, this component was concentrated in the antithrombin-binding regions of the high- Affinity Heparin molecules.

The binding of low-affinity and high-affinity heparin to antithrombin. Fluorescence studies.

The fluorescence enhancement caused by high-affinity heparin is consistent with a conformational change of antithrombin related to its activation, suggesting a different mode of binding of the two fractions to the protein.

Structural features of low-molecular-weight heparins affecting their affinity to antithrombin.

Enoxaparin is consistently richer in shorter oligosaccharides than Tinzaparin and Dalteparin, and this study is critical for establishing correlations between structural features of LMWHs and their AT-mediated anticoagulant activity.

An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence.

The aim of the present study was the structural and biochemical characterization of a previously unreported AGA*IA*-containing octasaccharide isolated from the very-low-molecular-mass heparin semuloparin, in which both glucosamine residues of the pentasACcharide moiety located at the non-reducing end bear 3-O-sulfate groups.

Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding.

The proposed mechanism of heparin activation is correct with respect to loop expulsion and it may consequently be possible to create more highly activated antithrombin variants through suitable hinge region substitutions.

Characterization of currently marketed heparin products: analysis of molecular weight and heparinase-I digest patterns

It is found that the PAGE analysis of heparinase digested UFH and neat LMWH samples yield characteristic patterns that provide a facile approach for identification and assessment of drug quality and uniformity.