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Molecularly imprinted polymers for protome analysis

By Francesca Bonini


Fast and efficient methods for the detection of insurgence and progression of diseases are at the basis of modern diagnostics and medicine. In this concern, biomarkers represent a powerful diagnostic tool, as their expression profiles well correlate with the pathology progression. Thus, the pathological state could be diagnosed by measuring the altered presence of a biomarker. In this direction, conspicuous help has been given by proteomics, intended as the study of the protein pattern of a sample and most frequently performed by two-dimensional electrophoresis. Although the proteome approach is a powerful analytical method, its application to biological samples for the detection and quantification of putative biomarkers is hampered by technical problems, in fact, the wide diversity in concentrations exhibited by the proteins present in the biological samples, with a concentration range spanning over nine orders of magnitude, and the relative abundance of each protein, are responsible of masking the less abundant species and of their loss in traceability. The aim of my PhD project is to apply Molecularly Imprinted Technology to the specific removal of a high abundance protein (Human Serum Albumin, HSA) frequently affecting proteomic analysis, in order to increase the detection of potential biomarkers. This technology allows the creation of artificial recognition sites in synthetic polymers for a specific protein. These sites are tailor-made in situ by co-polymerisation of functional monomers and cross-linkers around the template molecules. Two different approaches have been assayed in order to remove HSA: • Immobilisation of protein template on a rigid silica support (bead) and creation of polymer around beads. • Polymerisation in bulk of a polymer with protein template and application of this polymer to multicompartment electrolyser. In both of the cases, the chemical and structural features of the polymers have been analysed, after that they have been applied to complex proteome pre-treatment, obtaining encouraging results

Publisher: Cranfield University
Year: 2008
OAI identifier:
Provided by: Cranfield CERES

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  1. (2002). A colorimetric assay for the quantitation of free adenine applied to determine the enzymatic activity of ribosomeinactivating proteins. doi
  2. (1995). Alpha 2-macroglobulin receptor mediates binding and cytotoxicity of plant ribosome-inactivating proteins. doi
  3. (1993). Broadspectrum virus resistance in transgenic plants expressing pokeweed antiviral protein. doi
  4. (1997). Characterization of a saporin isoform with lower ribosome-inhibiting activity.
  5. (1994). Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. doi
  6. (2003). Cytotoxicity of ribosome-inactivating protein saporin is not mediated through alpha2-macroglobulin receptor. doi
  7. (1992). Determination by systematic deletion of the amino acids essential for catalysis by ricin A chain. doi
  8. (2005). Expression and characterisation in E. coli of mutant forms of saporin. doi
  9. GLQ223: An inhibitor of human immunodeficiency virus replication in acutely and chronically infected cells of lymphocyte and mononuclear phagocyte lineage. doi
  10. (1986). Membrane action of colicin E1: Detection by the release of carboxyfluorescein and calcein from liposomes. Biochim Biophys Acta 860:51–56. doi
  11. (1989). Molecular cloning. A laboratory manual. doi
  12. N-Terminal Deletion Affects Catalytic Activity 1139 doi
  13. (1986). Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. doi
  14. (1989). Ribosome inactivation by ricin A chain: A sensitive method to assess the activity of wild-type and mutant polypeptides.
  15. (1993). Ribosomeinactivating proteins from plants. doi
  16. (1999). Secondary structure of sea anemone cytolysins in soluble and membrane bound form by infrared spectroscopy. doi
  17. (1991). Small-volume extrusion apparatus for preparation of large, unilamellar vesicles. doi
  18. (1993). The 1138 Bonini et al.expression of saporin, a ribosome-inactivating protein from the plant Saponaria officinalis, in Escherichia coli.
  19. (2000). The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome. doi
  20. (2003). The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities. doi

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