Comparison of conjugating chondroitin sulfate A and B on amine-rich surface: For deeper understanding on directing cardiovascular cells fate

2021 ◽  
pp. 109430
Author(s):  
Jingan Li ◽  
Wei Li ◽  
Dan Zou ◽  
Fang Kou ◽  
Yachen Hou ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Cardiovascular Cells ◽  
Chondroitin Sulfate A

scholarly journals Immobilization of Chondroitin Sulfate A onto Monolithic Epoxy Silica Column as a New Chiral Stationary Phase for High-Performance Liquid Chromatographic Enantioseparation

2021 ◽  
Vol 14 (2) ◽  
pp. 98
Author(s):  
Ratih Ratih ◽  
Hermann Wätzig ◽  
Azminah Azminah ◽  
Mufarreh Asmari ◽  
Benjamin Peters ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Chondroitin Sulfate ◽  
High Performance ◽  
Chiral Stationary Phase ◽  
High Performance Liquid Chromatographic ◽  
Schiff Base Formation ◽  
The Individual ◽  
Liquid Chromatographic ◽  
Base Formation ◽  
Chondroitin Sulfate A

Chondroitin sulfate A was covalently immobilized onto a monolithic silica epoxy column involving a Schiff base formation in the presence of ethylenediamine as a spacer and evaluated in terms of its selectivity in enantioseparation. The obtained column was utilized as a chiral stationary phase in enantioseparation of amlodipine and verapamil using a mobile phase consisting of 50 mM phosphate buffer pH 3.5 and UV detection. Sample dilution by organic solvents (preferably 25% v/v acetonitrile-aqueous solution) was applied to achieve baseline enantioresolution (Rs > 3.0) of the individual drug models within 7 min, an excellent linearity (R2 = 0.999) and an interday repeatability of 1.1% to 1.8% RSD. The performance of the immobilized column for quantification of racemate in commercial tablets showed a recovery of 86–98% from tablet matrices. Computational modeling by molecular docking was employed to investigate the feasible complexes between enantiomers and the chiral selector.

scholarly journals Chondroitin Sulfate: A Critical Review of Generic and Specific Problems in Its Characterization and Determination—An Exemplar of a Material with an Unknown or Variable Composition (UVCB)

2018 ◽  
Vol 101 (1) ◽  
pp. 196-202 ◽  
Author(s):  
Duncan Thorburn Burns ◽  
Michael John Walker ◽  
Christopher Mussell
Keyword(s):  
Chondroitin Sulfate ◽  
Critical Review ◽  
Analytical Methods ◽  
Cetylpyridinium Chloride ◽  
Variable Composition ◽  
Reference Samples ◽  
Selection Of ◽  
Chondroitin Sulfate A

Abstract This review discusses the criteria for the selection of appropriate reference samples of chondroitin sulfate (CS) and the properties and specific problems of analytical methods for CS, namely titration with cetylpyridinium chloride; various separations; and UV-Vis, NMR, MS, and IR spectroscopies. Suggestions are put forward with regard to acceptable protocols for manufactures’ and for official/referee analysts for the analysis of CS in products.

scholarly journals The Chondroitin Sulfate A-binding Site of the VAR2CSA Protein Involves Multiple N-terminal Domains

2011 ◽  
Vol 286 (18) ◽  
pp. 15908-15917 ◽  
Author(s):  
Madeleine Dahlbäck ◽  
Lars M. Jørgensen ◽  
Morten A. Nielsen ◽  
Thomas M. Clausen ◽  
Sisse B. Ditlev ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Binding Site ◽  
Placental Malaria ◽  
African Women ◽  
Major Health Problem ◽  
Major Health ◽  
Malaria During Pregnancy ◽  
High Parasite ◽  
Similar Affinity ◽  
Chondroitin Sulfate A

Malaria during pregnancy is a major health problem for African women. The disease is caused by Plasmodium falciparum malaria parasites, which accumulate in the placenta by adhering to chondroitin sulfate A (CSA). The interaction between infected erythrocytes and the placental receptor is mediated by a parasite expressed protein named VAR2CSA. A vaccine protecting pregnant women against placental malaria should induce antibodies inhibiting the interaction between VAR2CSA and CSA. Much effort has been put into defining the part of the 350 kDa VAR2CSA protein that is responsible for binding. It has been shown that full-length recombinant VAR2CSA binds specifically to CSA with high affinity, however to date no sub-fragment of VAR2CSA has been shown to interact with CSA with similar affinity or specificity. In this study, we used a biosensor technology to examine the binding properties of a panel of truncated VAR2CSA proteins. The experiments indicate that the core of the CSA-binding site is situated in three domains, DBL2X-CIDRPAM and a flanking domain, located in the N-terminal part of VAR2CSA. Furthermore, recombinant VAR2CSA subfragments containing this region elicit antibodies with high parasite adhesion blocking activity in animal immunization experiments.

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