Improving understanding of solvent effects on intermolecular interactions in reactive liquid–liquid extraction with Isothermal Titration Calorimetry and molecular modeling

2019 ◽  
Vol 72 ◽  
pp. 364-373 ◽  
Author(s):  
Lisette M.J. Sprakel ◽  
Boelo Schuur
Keyword(s):  
Molecular Modeling ◽  
Intermolecular Interactions ◽  
Isothermal Titration Calorimetry ◽  
Solvent Effects ◽  
Liquid Extraction ◽  
Titration Calorimetry ◽  
Liquid Liquid Extraction ◽  
Reactive Liquid

A microfluidic study of liquid–liquid extraction mediated by carbon dioxide

Lab on a Chip ◽  
2016 ◽  
Vol 16 (14) ◽  
pp. 2710-2718 ◽  
Author(s):  
Gabriella Lestari ◽  
Alinaghi Salari ◽  
Milad Abolhasani ◽  
Eugenia Kumacheva
Keyword(s):  
Carbon Dioxide ◽  
Energy Consumption ◽  
Environmental Impact ◽  
Liquid Extraction ◽  
Separation And Purification ◽  
Purification Method ◽  
Carbon Dioxide Gas ◽  
Liquid Liquid Extraction ◽  
Switchable Solvents ◽  
Reactive Liquid

Liquid–liquid extraction is an important separation and purification method; however, it faces a challenge in reducing the energy consumption and the environmental impact of solvent (extractant) recovery. An oscillatory microfluidic platform is proposed to study reactive liquid–liquid extraction involving switchable solvents and carbon dioxide gas.

scholarly journals Cyclodextrin Complex Formation with Water-Soluble Drugs: Conclusions from Isothermal Titration Calorimetry and Molecular Modeling

2021 ◽  
Vol 22 (7) ◽  
Author(s):  
Karim S. Shalaby ◽  
Muhammad I. Ismail ◽  
Alf Lamprecht
Keyword(s):  
Molecular Modeling ◽  
Complex Formation ◽  
Drug Release ◽  
Binding Affinity ◽  
Isothermal Titration Calorimetry ◽  
Water Soluble ◽  
Titration Calorimetry ◽  
Cyclodextrin Complex ◽  
Water Soluble Drugs

AbstractCyclodextrin (CD) complexes are frequently used for enhancing the solubility or absorption of poorly water-soluble drugs. On the contrary, little is known about their complex formation with water-soluble drugs. Here, we have studied the interaction between 2-hydroxypropyl β-CD (HPβCD) and three water-soluble drugs, namely naloxone (NX), oxycodone (OC), and tramadol (TR), by isothermal titration calorimetry (ITC) combined with molecular modeling in view of the potential impact on drug release. The results showed that the complex formation of HPβCD with all three drugs occurs spontaneously. The complexes formed with NX and OC were found to be 2NX:1HPβCD and 3OC:2HPβCD, respectively. TR was found to form 2 complexes with HPβCD; of 1:2 and 1:1 complexation ratios. The binding of HPβCD to NX was greater than to OC due to the higher hydrophobicity of the structure of the former. Moreover, the binding affinity of HPβCD to TR was higher than to OC, which indicated the effect of the higher flexibility of the guest in increasing the binding affinity. In vitro drug release experiments from the various complexes revealed a significant impact of the stoichiometry of the complex on the release profiles. Accordingly, the co-administration of cyclodextrins with water-soluble drugs should be closely monitored, as it may result in unintentional complex formation that can potentially impact the drugs’ gastrointestinal absorption.

scholarly journals Galectin-4 N-Terminal Domain: Binding Preferences Toward A and B Antigens With Different Peripheral Core Presentations

2021 ◽  
Vol 9 ◽  
Author(s):  
Jon I. Quintana ◽  
Sandra Delgado ◽  
Reyes Núñez-Franco ◽  
F. Javier Cañada ◽  
Gonzalo Jiménez-Osés ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Blood Group ◽  
Intermolecular Interactions ◽  
Tandem Repeat ◽  
Titration Calorimetry ◽  
Blood Group Antigens ◽  
Chemical Modifications ◽  
Terminal Domain ◽  
Specific Effects ◽  
Covalently Linked

The tandem-repeat Galectin-4 (Gal-4) contains two different domains covalently linked through a short flexible peptide. Both domains have been shown to bind preferentially to A and B histo blood group antigens with different affinities, although the binding details are not yet available. The biological relevance of these associations is unknown, although it could be related to its attributed role in pathogen recognition. The presentation of A and B histo blood group antigens in terms of peripheral core structures differs among tissues and from that of the antigen-mimicking structures produced by pathogens. Herein, the binding of the N-terminal domain of Gal-4 toward a group of differently presented A and B oligosaccharide antigens in solution has been studied through a combination of NMR, isothermal titration calorimetry (ITC), and molecular modeling. The data presented in this paper allow the identification of the specific effects that subtle chemical modifications within this antigenic family have in the binding to the N-terminal domain of Gal-4 in terms of affinity and intermolecular interactions, providing a structural-based rationale for the observed trend in the binding preferences.

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