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GALAB is expanding the business area BioPharma - and develops specific separation techniques for glycoconjugates
GALAB Technologies, celebrating its 11th anniversary this year, is mainly known for their work in the fields of environmental, product and food analyses. Since the beginning of 2002, the Spin-off Company of the GKSS National Research Centre (Geesthacht, Germany) is expanding their activities in the market field BioPharma. GALAB develops bio specific separation techniques for glycoconjugates.
Glycoproteins carry information
Glycoconjugates as glycoproteins and glycolipids are present in every cell and play an important role in many physiological processes like immune response, cell differentiation and signalling. Consequently, they are potential candidates for the development of new therapeutics and for disease diagnostics. The glycan structure carries encoded information that can be recognized by other molecules. Carbohydrate structures stick out of the cell membrane and thus create the specific surface of the cell. Pathogenic agents approaching the cell surface recognize certain glycans and bind to them. This mechanism for example can cause an infection.
Precise diagnostics and disease control
If one can isolate and characterise glycoconjugates of a diseased cell type, it is possible to address new pharmaceutics towards a specific cell to provide protection. By this means, inflammation and bacteriologic infections can be antagonized.
This biotechnology can also be used as an early diagnostic against cancer. As cancer cells show different glycan surfaces compared to sound body cells, they can be detected via specific glycoconjugates.
Difficult analytical technology
Because of the enormous variety of glycoconjugates, it is difficult to find a standard method for their analysis. A highly specific separation technique is necessary to isolate the glycan molecules.
The analysis and purification of glycoproteins is performed using the technique of lectin affinity separation. Lectins are immobilised onto porous polymer particles.
Glycoproteins bind to the lectins and thereby are selectively isolated from a multi-compound mixture. Although this method has been known for some time it remains complex because each target molecule requires its own optimised separation parameters to achieve the desired results. Even the buffer conditions used in affinity separation must be adapted for each target glycoprotein and lectin ligand.
Optimal separation process
Since the beginning of 2002 the analytical chemist Dr. Simone Cartellieri is manager of the new biotechnology laboratory at GALAB. At the GKSS National Research Centre she has already worked on this promising technology: «For the research on glycoconjugates it is necessary to separate them in a natural form out of an unknown multi-compound mixture, to keep thei original structure and activity. Common physical and chemical separation techniques often result in a poor yield and product purity.» Affinity separation on the other hand yields an excellent purity and preserved biological activity of the target compounds.
To develop and optimise the affinity method a screening of the samples against different lectins is required. This approach confirms the binding behaviour and provides first knowledge about the structure of the glycoprotein. With this information, the parameters for the specific methods can be set.
Tailor-made solutions
GALAB Laboratories -excellently equipped for this task- offer tailor-made solutions in the field of affinity separation of glycoconjugates. Services reach from customized method development to the development and preparation of affinity columns, kits and adsorbents. GALAB provides an invaluable support for customers working in the field of glycobiology / glycoproteomics concerning the purification and characterization of glycoconjugates. |
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