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Evaluation of solid-phase microextraction for the study of protein binding in human plasma samples
M Abdel-Rehim1, G Carlsson, M Bielenstein
1AstraZeneca R&D Södertälje, Sweden. mohamed.abdel-rehim@astrazeneca.com
Journal of Chromatographic Science
|October 26, 2000
Summary
Solid-phase microextraction (SPME) offers a reliable method for analyzing protein binding of local anesthetics in plasma. This technique provides accurate results comparable to traditional methods.
Area of Science:
- Analytical Chemistry
- Pharmacology
- Biochemistry
Background:
- Protein binding influences drug efficacy and distribution.
- Accurate measurement of protein binding is crucial for pharmacokinetic studies.
- Traditional methods for assessing protein binding can be complex and time-consuming.
Purpose of the Study:
- To evaluate Solid-phase microextraction (SPME) as a sample preparation technique for studying protein binding of amide-type local anesthetics.
- To compare the performance of different SPME fibers (CW/DVB, polyacrylate, PDMS) for this application.
- To investigate the influence of concentration, pH, and temperature on the protein binding of these anesthetics.
Main Methods:
- Solid-phase microextraction (SPME) coupled with gas chromatography-nitrogen-phosphorous detection.
- Testing of Carbowax/divinylbenzene (CW/DVB), polyacrylate, and polydimethylsiloxane fibers.
- Analysis of ropivacaine, bupivacaine, mepivacaine, prilocaine, and lidocaine in human plasma samples.
Main Results:
- CW/DVB fibers demonstrated the highest recovery rates in plasma samples.
- Protein binding increased with decreasing solute concentration and increasing pH.
- Protein binding decreased with increasing temperature.
- The SPME method showed good correlation, precision, and accuracy within 20% of theoretical values.
Conclusions:
- SPME is a validated and effective sample preparation method for determining protein binding of local anesthetics.
- The developed SPME method yields comparable results to established techniques.
- This approach simplifies the analysis of drug-protein interactions in biological matrices.