Main content

Engineering single-domain antibodies for bioactive paper applications

Show simple item record Wood, Sarah 2011-03-29T13:37:29Z 2011-03-29T13:37:29Z 2011-03 2010-09-14 2011-03-29
dc.description.abstract This thesis is an investigation of the fusion of a carbohydrate-binding module (CBM) to a high-affinity single-domain antibody (sdAb) which binds to bacteriophage M13. This fusion protein was applied to paper filters for detection of M13 phage. A CBM-sdAb fusion protein with nanomolar affinity for immobilized M13 phage was successfully expressed in E. coli. The CBM-sdAb fusion protein was effective in binding M13 phage in water to a cellulose filter paper. However, the sdAb and the CBM-sdAb fusion protein were ineffective in enhancing filter capture of M13 phage particles from water or air, respectively. This research demonstrates that a CBM-sdAb fusion protein will bind simultaneously to cellulose and a model virus. In the future, CBM-sdAb fusion proteins may be useful in the development of ‘bioactive’ paper products capable of detecting and/or inactivating pathogens which are a threat to public health. en_US
dc.description.sponsorship NRC Graduate Student Scholarship Supplement Program, NSERC Canada Graduate Scholarship, SENTINEL (Canadian Network for the Development and Use of Bioactive Paper) en_US
dc.language.iso en en_US
dc.title Engineering single-domain antibodies for bioactive paper applications en_US
dc.type Thesis en_US Environmental Biology en_US Master of Science en_US Department of Environmental Biology en_US
dc.rights.license All items in the Atrium are protected by copyright with all rights reserved unless otherwise indicated.

Files in this item

Files Size Format View
Draft_6_Sarah_Wood_March_27_2011_SW.pdf 3.246Mb PDF View/Open

This item appears in the following Collection(s)

Show simple item record