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| Content Provider | Springer Nature Link |
|---|---|
| Author | Peyrin, E. Ravel, A. Grosset, C. Villet, A. Ravelet, C. Nicolle, E. Alary, J. |
| Copyright Year | 2001 |
| Abstract | The binding of a series of D,L dansyl amino acids (used as test solutes) to immobilized teicoplanin has been investigated over a wide range of sodium citrate buffer concentrations,c (2.5×10−3 to 10−1 M). An approach based on the use of both the Gibbs adsorption isotherm and a solute displacement model was used to describe solute behavior in this chromatographic system. Variation of thermodynamic quantities was calculated from Van't Hoff plots to enable understanding of the forces driving solute association with the teicoplanin phase. An enthalpyentropy compensation study was also performed for further exploration of the interaction mechanisms. The results suggested that variations of solute retention whenc changed were governed by both (i) the salting-out effect of the salt and (ii) competitive displacement of the dansyl amino acids from their teicoplanin binding site by the citrate anion. The study also shows that hydrophobic interactions and hydrogen-bond formation are important to chiral discrimination in this chromatographic system. |
| Starting Page | 645 |
| Ending Page | 650 |
| Page Count | 6 |
| File Format | |
| ISSN | 00095893 |
| Journal | Chromatographia |
| Volume Number | 53 |
| Issue Number | 11-12 |
| e-ISSN | 16121112 |
| Language | English |
| Publisher | Vieweg Verlag |
| Publisher Date | 2001-01-01 |
| Publisher Place | Wiesbaden |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Column liquid chromatography Immobilized teicoplanin Dansyl amino acids Hydrophobic effect Hydrogen bonds Analytical Chemistry Organic Chemistry Pharmacy Biochemistry Plant Sciences Measurement Science, Instrumentation |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Analytical Chemistry Biochemistry Clinical Biochemistry |
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