Artificial receptors: New opportunities for the exploitation of molecularly imprinted polymers
Author
Summary, in English
Molecular imprinting, method for creating artificial receptors that are mimics of biological antibodies and receptors, is based on the concept of creating substrate-specific recognition sites in polymeric matrices by means of template polymerisation. The polymeric receptors produced display favourable binding characteristics, such as high affinity and specificity towards the substrate molecules. Compared to natural antibodies and receptors, imprinted polymers are much more stable and can therefore be utilised under considerably harsher conditions.
In the researches described in this thesis, non-covalent interactions are the major force driving the assembly of imprinted receptors. Given that non-covalent molecular interactions dominate in all biological recognition processes, their application in molecular imprinting is in principle unlimited. The general applicability of the non-covalent approach for the imprinting of various substrate molecules is reflected in the increasing number of publications in recent years. Non-covalent molecularly imprinted polymers have been applied in many areas, for example as stationary phases in chiral separation, as affinity adsorbents for sample pre-treatment using solid-phase extraction, as antibody mimics for drug determination, etc.
Summarised in this thesis are novel applications for molecularly imprinted polymers prepared via the non-covalent approach. Artificial antibodies against corticosteroids have been prepared that exhibit binding behaviour similar to their natural counterparts. The utility of imprinted polymers for the screening of combinatorial chemical libraries is demonstrated, where the compounds of interest can be specifically isolated from libraries composed of many similar structures. As specific adsorbents, molecularly imprinted polymers are used for product purification following chemical synthesis and for in situ product removal during a biotransformation process to enhance product yield. Finally, a new imprinting methodology is developed for the production of affinity microspheres that have various applications in analytical and medical sciences.
In the researches described in this thesis, non-covalent interactions are the major force driving the assembly of imprinted receptors. Given that non-covalent molecular interactions dominate in all biological recognition processes, their application in molecular imprinting is in principle unlimited. The general applicability of the non-covalent approach for the imprinting of various substrate molecules is reflected in the increasing number of publications in recent years. Non-covalent molecularly imprinted polymers have been applied in many areas, for example as stationary phases in chiral separation, as affinity adsorbents for sample pre-treatment using solid-phase extraction, as antibody mimics for drug determination, etc.
Summarised in this thesis are novel applications for molecularly imprinted polymers prepared via the non-covalent approach. Artificial antibodies against corticosteroids have been prepared that exhibit binding behaviour similar to their natural counterparts. The utility of imprinted polymers for the screening of combinatorial chemical libraries is demonstrated, where the compounds of interest can be specifically isolated from libraries composed of many similar structures. As specific adsorbents, molecularly imprinted polymers are used for product purification following chemical synthesis and for in situ product removal during a biotransformation process to enhance product yield. Finally, a new imprinting methodology is developed for the production of affinity microspheres that have various applications in analytical and medical sciences.
Department/s
Publishing year
1999
Language
English
Document type
Dissertation
Publisher
Pure and Applied Biochemistry, Lund University
Topic
- Biochemistry and Molecular Biology
Keywords
- Radioimmunoassay
- Microsphere
- Molecular imprinting
- Drug determination
- Cross-linking polymerisation
- Combinatorial library
- Chromatography
- Chiral separation
- Affinity adsorbent
- Biosensor
- Receptor
- Biochemistry
- Metabolism
- Biokemi
- metabolism
- Biotechnology
- Bioteknik
Status
Published
Supervisor
- [unknown] [unknown]
ISBN/ISSN/Other
- ISBN: 91-628-3713-3
- LUTKDH/TKBK-1049/1-119/1999
Defence date
28 October 1999
Defence time
10:15
Defence place
Lecture Hall C, Chemical Center, Lund University
Opponent
- David C Sherrington (Professor)