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The use of chitin binding proteins for glycoprotein analysis

Larragy, Ruth, Thompson, Roisin and O'Connor, Brendan (2009) The use of chitin binding proteins for glycoprotein analysis. In: Glycosciences Ireland, 18 Jun 2009, NUIG, Galway, Ireland.

Abstract
The focus of the pharmaceutical industry has dramatically shifted in the past number of years. Traditional drugs were synthesised using chemical reactions have been replaced by recombinant glycoprotein molecules. These potential recombinant glycoprotein therapeutics display oligosaccharide structures on their surfaces that are recognised by their target host. The specific glycan moieties on the surface of the molecules vary dramatically and have a large impact on the efficacy of the drug. The development of bioanalytical tools to identify and separate the species of glyco-forms present in a preparation of the glycoprotein therapeutic will significantly help to advance the quality and effectiveness of recombinant glycoprotein molecules. Traditionally lectins, isolated from plants, had been used to profile sugar species displayed on glycoproteins. I have explored the use of prokaryotic chitin binding proteins (CBPs) to investigate structures on glycoproteins.
Metadata
Item Type:Conference or Workshop Item (Poster)
Event Type:Conference
Refereed:Yes
Uncontrolled Keywords:pharmaceuticals; recombinant glycoprotein therapeutics
Subjects:Biological Sciences > Biotechnology
Biological Sciences > Biochemistry
Biological Sciences > Enzymology
Biological Sciences > Molecular biology
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > Centre for Bioanalytical Science (CBAS)
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
Funders:Science Foundation Ireland, Irish Research Council for Science Engineering and Technology
ID Code:17782
Deposited On:13 Feb 2013 13:49 by Brendan O'connor . Last Modified 19 Jul 2018 14:58
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