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| Content Provider | Springer Nature Link |
|---|---|
| Author | Ibrahim, Firas Guillaume, Yves Claude André, Claire |
| Copyright Year | 2008 |
| Abstract | In this work, the interaction of memantine with human serum albumin (HSA) immobilized on porous silica particles was studied using a biochromatographic approach. The determination of the enthalpy change at different pH values suggested that the protonated group in the memantine–HSA complex exhibits a heat protonation with a magnitude around 65 kJ mol−1. This value agrees with the protonation of a guanidinium group, and confirmed that an arginine group may become protonated in the memantine–HSA complex formation. The thermodynamic data showed that memantine–HSA binding, for low temperature (<293 K), is dominated by a positive entropy change. This result suggests that dehydration at the binding interface and charge–charge interactions contribute to the memantine–HSA complex formation. Above 293 K, the thermodynamic data ΔH and ΔS became negative due to van der Waals interactions and hydrogen bonding which are engaged at the complex interface. The temperature dependence of the free energy of binding is weak because of the enthalpy–entropy compensation caused by a large heat capacity change, ΔC p = − 3.79 kJ mol−1 K−1 at pH = 7. These results were used to determine the potential binding site of this drug on HSA. |
| Starting Page | 179 |
| Ending Page | 186 |
| Page Count | 8 |
| File Format | |
| ISSN | 00095893 |
| Journal | Chromatographia |
| Volume Number | 68 |
| Issue Number | 3-4 |
| e-ISSN | 16121112 |
| Language | English |
| Publisher | Vieweg Verlag |
| Publisher Date | 2008-06-03 |
| Publisher Place | Wiesbaden |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Column liquid chromatography Human serum albumin Memantine Measurement Science, Instrumentation Plant Sciences Biochemistry Pharmacy Organic Chemistry Analytical Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Analytical Chemistry Biochemistry Clinical Biochemistry |
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